Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O76922
|
AUB_DROME
|
MNLPPNPVIARGRGRGRKPNNVEANRGFAPSLGQKSDPSHSEGNQASGGNGGGGDAQVGPSIEKSSLSAVQMHKSEGDPRGSVRGRRLITDLVYSRPPGMTSKKGVVGTHITVQANYFKVLKRPNWTIYQYRVDFTPDVEATRLRRSFLYEHKGILGGYIFDGTNMFCINQFKAVQDSPYVLELVTKSRAGENIEIKIKAVGSVQSTDAEQFQVLNLILRRAMEGLDLKLVSRYYYDPQAKINLENFRMQLWPGYQTSIRQHENDILLCSEICHKVMRTETLYNILSDAIRDSDDYQSTFKRAVMGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDGEISYVDYYKKRYNIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMTDAMRADFRTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNQKIFVCDARADWTNEFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIAPRQQKPTGLMSIATKVVIQMNAKLMGAPWQVVIPLHGLMTVGFDVCHSPKNKNKSYGAFVATMDQKESFRYFSTVNEHIKGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVNTLKDRLDEIYKSAGKQEGCRMTFIIVSKRINSRYFTGHRNPVPGTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESINRAPSAGLQNQLYFL
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; dorsal appendage formation [GO:0046843]; global gene silencing by mRNA cleavage [GO:0098795]; heterochromatin formation [GO:0031507]; maintenance of pole plasm mRNA location [GO:0046594]; mitotic chromosome condensation [GO:0007076]; oocyte karyosome formation [GO:0030717]; oocyte maturation [GO:0001556]; oogenesis [GO:0048477]; P granule assembly [GO:1903863]; piRNA processing [GO:0034587]; pole cell development [GO:0007277]; pole cell formation [GO:0007279]; pole plasm assembly [GO:0007315]; pole plasm protein localization [GO:0007318]; positive regulation of innate immune response [GO:0045089]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; positive regulation of oskar mRNA translation [GO:0046012]; positive regulation of post-transcriptional gene silencing by RNA [GO:1900370]; regulation of oskar mRNA translation [GO:0046011]; regulation of pole plasm oskar mRNA localization [GO:0007317]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; retrotransposon silencing [GO:0010526]; retrotransposon silencing by mRNA destabilization [GO:0141008]; secondary piRNA processing [GO:0140965]; segmentation [GO:0035282]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; P granule [GO:0043186]
|
piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891]
|
PF02170;PF02171;
|
3.40.50.2300;2.170.260.10;3.30.420.10;
|
Argonaute family, Piwi subfamily
|
PTM: Symmetrical dimethylation on Arg-11, Arg-13 and/or Arg-15, most likely by csul, is required for binding to tud, localization to the pole plasm and association with the correct piRNAs. {ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:19959991, ECO:0000269|PubMed:20713507, ECO:0000303|PubMed:19959991}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11526087, ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20953170, ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:28945271}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. In the oocyte and later in the embryo, concentrates at the posterior pole as a component of polar granules. In the cytoplasm of syncytial embryos, accumulates in discrete foci. {ECO:0000269|PubMed:11526087, ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19395009, ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:20713507, ECO:0000269|PubMed:20953170, ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:21447556, ECO:0000269|PubMed:28945271}.
| null | null | null | null | null |
FUNCTION: Acts via the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. In ovary, associates predominantly with antisense piRNAs that contain uridine at their 5' end. In testis, associates with Su(Ste) antisense piRNAs (most abundant class of piRNAs found in complex with aub in testes) and negatively regulates Ste expression, most likely by cleaving its transcripts. Also in testis, may repress translation of vas when associated with a piRNA derived from chromosome X, termed AT-chX-1, whose sequence shows strong complementarity to vas mRNA. Aub-piRNA complexes from ovary and testis possess RNA cleavage activity. Involved in telomere regulation by repressing specialized telomeric retroelements HeT-A and TART; Drosophila telomeres being maintained by transposition of specialized telomeric retroelements. Also involved in telomeric trans-silencing, a repression mechanism by which a transposon or a transgene inserted in subtelomeric heterochromatin has the capacity to repress in trans, in the female germline, a homologous transposon, or transgene located in euchromatin. Involved in the suppression of meiotic drive of sex chromosomes and autosomes. Involved in transposon silencing in the adult brain. Required for dorsal-ventral as well as anterior-posterior patterning of the egg. Required during oogenesis for primordial germ cell formation and activation of RNA interference. During early oogenesis, required for osk mRNA silencing and polarization of the microtubule cytoskeleton. During mid-oogenesis, required for osk mRNA localization to the posterior pole and efficient translation of osk and grk. During embryogenesis, required for posterior localization of nanos (nos) mRNA, independently of osk, and pole cell formation. Essential for the formation and/or structural integrity of perinuclear nuage particles. Required for the localization of Mael to the meiotic nuage. Forms a complex with smg, twin, AGO3 and specific piRNAs that targets nanos mRNA (and probably other maternal mRNAS) for deadenylation promoting its decay during early embryogenesis. {ECO:0000269|PubMed:11526087, ECO:0000269|PubMed:12154120, ECO:0000269|PubMed:12538514, ECO:0000269|PubMed:14752161, ECO:0000269|PubMed:15035984, ECO:0000269|PubMed:15090597, ECO:0000269|PubMed:15372228, ECO:0000269|PubMed:16452506, ECO:0000269|PubMed:17322028, ECO:0000269|PubMed:17346786, ECO:0000269|PubMed:1783295, ECO:0000269|PubMed:17872506, ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:19959991, ECO:0000269|PubMed:20937269, ECO:0000269|PubMed:20953170, ECO:0000269|PubMed:20980675, ECO:0000269|PubMed:23267055, ECO:0000269|PubMed:23559253, ECO:0000269|PubMed:8625849, ECO:0000269|PubMed:9927466}.
|
Drosophila melanogaster (Fruit fly)
|
O76924
|
ARI2_DROME
|
MDSDIEMDMESDNDGEYDDDYDYYNTGEDCDVERLDPKRADPEYFEYECLTVEDIEKLLNERVEKLNTILQITPSLAKVLLLEHQWNNVAVVEKYRQDANALLVTARIKPPSVAVTDTASTSAAAASAQLLRLGSSGYKTTASATPQYRSQMCPVCASSQLGDKFYSLACGHSFCKDCWTIYFETQIFQGISTQIGCMAQMCNVRVPEDLVLTLVTRPVMRDKYQQFAFKDYVKSHPELRFCPGPNCQIIVQSSEISAKRAICKACHTGFCFRCGMDYHAPTDCQVIKKWLTKCADDSETANYISAHTKDCPKCHICIEKNGGCNHMQCFNCKHDFCWMCLGDWKTHGSEYYECSRYKDNPNIANESVHVQAREALKKYLHYYERWENHSKSLKLEQQTIDRLRQRINSKVMNGSGTWIDWQYLFNAAALLAKCRYTLQYTYPYAYYMEAGSRKNLFEYQQAQLEAEIENLSWKIERAETTDLGDLENQMDIAEKRRTTLLKDFFPVDA
|
2.3.2.31
| null |
positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF19422;PF01485;
|
1.20.120.1750;3.30.40.10;
|
RBR family, Ariadne subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
| null | null | null | null |
FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
|
Drosophila melanogaster (Fruit fly)
|
O76927
|
RS21_DROME
|
MENDAGENVDLYVPRKCSASNRIIHAKDHASVQLSIVDVDPETGRQTDGSKTYAICGEIRRMGESDDCIVRLAKKDGIITKNF
| null | null |
cytoplasmic translation [GO:0002181]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000461]; lymph gland development [GO:0048542]; regulation of cell population proliferation [GO:0042127]; regulation of translation [GO:0006417]
|
cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; ribosome [GO:0005840]; rough endoplasmic reticulum [GO:0005791]
|
ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735]
|
PF01249;
|
3.30.1230.20;
|
Eukaryotic ribosomal protein eS21 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63220}. Cytoplasm {ECO:0000269|PubMed:10022917, ECO:0000305|PubMed:23636399}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P63221}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P63220, ECO:0000250|UniProtKB:P63221}.
| null | null | null | null | null |
FUNCTION: May be an associated component of the ribosome rather than a core structural subunit. May act as a translation initiation factor. Has a role in regulation of cell proliferation in the hematopoietic organs and the imaginal disks of larva. {ECO:0000269|PubMed:10022917}.
|
Drosophila melanogaster (Fruit fly)
|
O76932
|
PP4C_DROME
|
MSDYSDLDRQIEQLKRCEIIKENEVKALCAKAREILVEEGNVQRVDSPVTVCGDIHGQFYDLKELFKVGGDVPEKNYLFMGDFVDRGYYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSTAVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQYLDQIRSIDRKQEVPHDGPMCDLLWSDPEDQTGWGVSPRGAGYLFGSDVVSQFNRTNDIDMICRAHQLVMEGFKWHFNETVLTVWSAPNYCYRCGNVAAILELNEYLHRDFVIFEAAPQESRGIPSKKPQADYFL
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
|
double-strand break repair via homologous recombination [GO:0000724]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; negative regulation of smoothened signaling pathway [GO:0045879]; regulation of mitotic cell cycle [GO:0007346]
|
centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein phosphatase 4 complex [GO:0030289]
|
metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00149;
|
3.60.21.10;
|
PPP phosphatase family, PP-4 (PP-X) subfamily
|
PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26586222, ECO:0000269|PubMed:9570751}. Nucleus {ECO:0000269|PubMed:26586222, ECO:0000269|PubMed:9570751}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9570751}. Note=Localized predominantly to the cytoplasm during interphase. Exhibits a transient nuclear enrichment during early prophase. Cytoplasmic localization after breakdown of the nuclear envelope. {ECO:0000269|PubMed:26586222}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Protein phosphatase that regulates many processes such as microtubule organization at centrosomes. The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase-induced cell death (in vitro). {ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:9570751}.
|
Drosophila melanogaster (Fruit fly)
|
O76997
|
TRK1_LYMST
|
MRGPRRFRLWTRANVLTVISILTSILSGAGCSPLSQLPSDNPAHVGVQDGVTTERVDRSKNHRNTTASSGAHRVTSGEPLGDRVTTRSTTAPDQVPGDASRNTTMAGTKCSLQVDLSTFACPADCQCNATSEGMVVSCVTPDTLREFPVIAREVARAVIKLELRGQSKLTSLKTELKFFTCLKHLTIENCGLNNIQGIAFKTLTSLETINLRHNHLTEFPQELLRTLNLRELWLEGNALTCSCTNLWLRSVDVAADRSEMTCSTRDGVSKMKMTQFKCEPCGIPDIRNMTLVFEPKNGMFLLRFVISGCPKPKIDLLRNHHHVLRSGSSQFKLTDFKSEFNGQVVTGTITILPHMETSQTTYVLTAVNSKGQANQTFHLYDQTTPASSIHIPLSNIPPRISSATTPRASPTEDFGPQTQVILPVVGVVILLISAVFIIYLCQRAKHRSHARQRCKKALLDKKFNEFQEGVPLTGLQLVDNPNYNLTKKKHVATTCPKTVRLQTILLMRVIGEGAFGRVFLGTCAHLIQKNEFAIVAVKTLKGSCSDSLKRDFEREAEMLATIEHANIVTFYGVCTESDQWMMIFEFMENGDLNKYLRMHGPDAAFLKDRDSMDSDEGQLTREQLMKIVLQIASAMEYLALQHFVHRDLATRNCLVGCDLVVKLGDFGMSRDVYTTDYYRVEGTAMLPVRWMPPESIIYRTFTTESDVWSFGVTLWEVFTYGKQPWFEYSNSEVIEHIKNSRTLKRPPRTCTDGVYRVMQGCWKPNPQDRLTMKDIAELLREEVSGDPVYIDIIA
|
2.7.10.1
| null |
cell differentiation [GO:0030154]; cellular response to nerve growth factor stimulus [GO:1990090]; nervous system development [GO:0007399]; phosphorylation [GO:0016310]; positive regulation of neuron projection development [GO:0010976]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; membrane [GO:0016020]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; neurotrophin binding [GO:0043121]; neurotrophin receptor activity [GO:0005030]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF13855;PF07714;
|
2.60.40.10;3.80.10.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: May bind an endogenous invertebrate neurotrophin. Binds human NT-3, but not NGF or BDNF.
|
Lymnaea stagnalis (Great pond snail) (Helix stagnalis)
|
O77051
|
E2F2_DROME
|
MYKRKTASIVKRDSSAAGTTSSAMMMKVDSAETSVRSQSYESTPVSMDTSPDPPTPIKSPSNSQSQSQPGQQRSVGSLVLLTQKFVDLVKANEGSIDLKAATKILDVQKRRIYDITNVLEGIGLIDKGRHCSLVRWRGGGFNNAKDQENYDLARSRTNHLKMLEDDLDRQLEYAQRNLRYVMQDPSNRSYAYVTRDDLLDIFGDDSVFTIPNYDEEVDIKRNHYELAVSLDNGSAIDIRLVTNQGKSTTNPHDVDGFFDYHRLDTPSPSTSSHSSEDGNAPACAGNVITDEHGYSCNPGMKDEMKLLENELTAKIIFQNYLSGHSLRRFYPDDPNLENPPLLQLNPPQEDFNFALKSDEGICELFDVQCS
| null | null |
DNA endoreduplication [GO:0042023]; endomitotic cell cycle [GO:0007113]; G1/S transition of mitotic cell cycle [GO:0000082]; imaginal disc development [GO:0007444]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA replication [GO:0008156]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oogenesis [GO:0048477]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; Myb complex [GO:0031523]; nucleus [GO:0005634]; Rb-E2F complex [GO:0035189]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF02319;
|
6.10.250.540;1.10.10.10;
|
E2F/DP family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:9792788}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that binds to E2f sites and represses E2f-regulated target genes. Binding to E2f sites requires transcription factor Dp. Acts synergistically with Rbf2 to antagonize E2f1-mediated transcriptional activation. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. The DREAM complex is required for recruiting E2f2 at differentiation-specific promoters and for stabilizing E2f2-Rbf complexes during S phase. During development, the complex represses transcription of developmentally controlled E2f target genes. During oogenesis, plays a role in restricting DNA synthesis to sites of chorion gene amplification in late stage ovarian follicle cells. Plays an inhibitory role in ionizing radiation (IR)-induced p53-independent apoptosis. May be involved in cell cycle exit by temporarily limiting CycE-dependent activation of E2f-regulated transcription. {ECO:0000269|PubMed:11511545, ECO:0000269|PubMed:11748144, ECO:0000269|PubMed:12234932, ECO:0000269|PubMed:12612083, ECO:0000269|PubMed:15456884, ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:20548101, ECO:0000269|PubMed:20659447, ECO:0000269|PubMed:22451490, ECO:0000269|PubMed:9792788}.
|
Drosophila melanogaster (Fruit fly)
|
O77059
|
CRY1_DROME
|
MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV
| null |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:23746849}; Note=Binds 1 FAD per subunit. The bound form of FAD in the inactive state of cry is oxidized FAD, not reduced. After activation by blue light the FAD is in an anionic radical state, which would be paramagnetic. Green light, which reduces levels of radical intermediate, has an antagonistic effect on function. {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:23746849};
|
blue light signaling pathway [GO:0009785]; cellular response to light stimulus [GO:0071482]; circadian behavior [GO:0048512]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; detection of light stimulus involved in magnetoreception [GO:0050980]; entrainment of circadian clock [GO:0009649]; entrainment of circadian clock by photoperiod [GO:0043153]; gravitaxis [GO:0042332]; locomotor rhythm [GO:0045475]; magnetoreception [GO:0050958]; negative regulation of DNA-templated transcription [GO:0045892]; phototransduction [GO:0007602]; regulation of circadian rhythm [GO:0042752]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; response to blue light [GO:0009637]; response to light stimulus [GO:0009416]; response to magnetism [GO:0071000]; UV-A, blue light phototransduction [GO:0009588]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
blue light photoreceptor activity [GO:0009882]; DNA binding [GO:0003677]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; photoreceptor activity [GO:0009881]
|
PF00875;PF03441;
|
1.25.40.80;1.10.579.10;3.40.50.620;
|
DNA photolyase class-1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Nucleus {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Note=Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per. {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}.
| null | null | null | null | null |
FUNCTION: Blue light-dependent regulator that is the input of the circadian feedback loop (PubMed:10063806, PubMed:10233998, PubMed:10417378, PubMed:16527739, PubMed:17298948, PubMed:18597555, PubMed:36994075, PubMed:9845369). Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts (PubMed:10063806). Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms (PubMed:10063806, PubMed:10233998, PubMed:9845369). Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells (PubMed:10417378, PubMed:16527739, PubMed:36994075, PubMed:9845370). Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (PubMed:10417378, PubMed:16527739). Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate (PubMed:18641630). Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing (PubMed:18641630). {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:10233998, ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:16527739, ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:18641630, ECO:0000269|PubMed:36994075, ECO:0000269|PubMed:9845369, ECO:0000269|PubMed:9845370}.
|
Drosophila melanogaster (Fruit fly)
|
O77081
|
TPSTA_CAEEL
|
MRKNRELLLVLFLVVFILFYFITARTADDPYYSNHREKFNGAAADDGDESLPFHQLTSVRSDDGYNRTSPFIFIGGVPRSGTTLMRAMLDAHPEVRCGEETRVIPRILNLRSQWKKSEKEWNRLQQAGVTGEVINNAISSFIMEIMVGHGDRAPRLCNKDPFTMKSAVYLKELFPNAKYLLMIRDGRATVNSIISRKVTITGFDLNDFRQCMTKWNAAIQIMVDQCESVGEKNCLKVYYEQLVLHPEAQMRRITEFLDIPWDDKVLHHEQLIGKDISLSNVERSSDQVVKPVNLDALIKWVGTIPEDVVADMDSVAPMLRRLGYDPNANPPNYGKPDELVAKKTEDVHKNGAEWYKKAVQVVNDPGRVDKPIVDNEVSKL
|
2.8.2.20
| null |
collagen metabolic process [GO:0032963]; cuticle development involved in collagen and cuticulin-based cuticle molting cycle [GO:0042338]; regulation of locomotion [GO:0040012]; regulation of nematode larval development [GO:0061062]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802]
|
protein-tyrosine sulfotransferase activity [GO:0008476]
|
PF13469;
|
3.40.50.300;
|
Protein sulfotransferase family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60704}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20; Evidence={ECO:0000250|UniProtKB:O60704};
| null | null | null | null |
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000250|UniProtKB:O60704}.
|
Caenorhabditis elegans
|
O77086
|
C3G_DROME
|
MPQFDESFLSDCALADRWHFYSYTVKQLPPHPSPKPNRNRNPYPSGASHDDHQHQLHHHHHQQHHHNHHRLWKTQRQSWSPRDTNNNHSLTSNNCNCNSSNTCNSISATGNTLHSIKFHRRRKYKKLARLALSTPAIPLQMDVDVDVNVTVDREFDMEMDTPVPLKNAVCHGSISSPSTPGTCSSGIGVGGGGCSSSSNNSINSGSYSTACTPPPPTHQHHSQHQQLQGTPGGSSRVGGAGAGGGGGVPPAPPSAGSSGHKNSLKGTKLARRARSFKDDLIEKISLMRTTNNTLGRSHSPHSPRTKHGTKAPPTTEEVLRSTQTLETHVKDISNALKHFRDVILKKKLEVLPGNGTVILETIASMYSVIQTYTLNENSAIMSSATLQVYQSLGKLIKLCDEVMLSEDSGECASLSNENVREVIDLLEDAVRNLVTLAQGKLKEQDQCAFRYSGSGLGGIGAAAEIMGAVTASPGASVPGTGVMRVSAAESAAQRTSLPDIALTPKERDILEQHNVNPMRGSHSTESILRDTSPPPKPPLPNRASNPPPLPPKRRSQPSASAGTVGVGCSSSTSTSNQASPLPYAQSHNISLNSDLDCSSNISLLNYGVDRLSVRSRSPDENSQCSFDSALNHSREEEDQQQQHQHLRSFPKLAAMMDEDMDKMVSYSAAIDDKTQTPLSTGGGIAGVAGGTGGAGEGVAAAASGDGETNSNRHSNESGFVSMREFRTSTQTTDYSVQSSTKSSSSNSEIAFSISESTAVGSSSEYQQISQLVSHSQRHISSSSSSCTTTTTSSSTTTGYGSSEVEQLQQQQQQQTTTTPADLAPALPPKSIQRSSLTRHDSPGVGDELDEVQSSSGWASHRSSQSEVAELRQLSPLHHLNHHPHTASAGQLQQWHSKHHSLIEGPRLQLAGSGSCSAFDQRHLDQEPPPLPIKKKHILAYMEICSASTRSIEQHRHTMHACNISRNISHSQTMNIMPMSKELSPELEMPPALPPKNYKQRKATSMVASPTLQPVIVTTPPPSPKPTLGENGSTGRPDSRMATVCEELNDAVASEDAMPEPRSPVLDSNENVSAVDDGQTFYCHSHQLPAAEMEMSEDASSADNQPITTPQVLEEQEEPTAESRPLVAVHESVKPANVDEDEEAERADMLINMLEEVNITRYLILKKREEDGPEVKGGYIDALIVHASRVQKVADNAFCEAFITTFRTFIQPIDVIEKLTHRYTYFFCQVQDNKQKAAKETFALLVRVVNDLTSTDLTSQLLSLLVEFVYQLVCSGQLYLAKLLRNKFVEKVTLYKEPKVYGFVGELGGAGSVGGAGIAGSGGCSGTAGGGNQPSLLDLKSLEIAEQMTLLDAELFTKIEIPEVLLFAKDQCEEKSPNLNKFTEHFNKMSYWARSKILRLQDAKEREKHVNKFIKIMKHLRKMNNYNSYLALLSALDSGPIRRLEWQKGITEEVRSFCALIDSSSSFRAYRQALAETNPPCIPYIGLILQDLTFVHVGNQDYLSKGVINFSKRWQQYNIIDNMKRFKKCAYPFRRNERIIRFFDNFKDFMGEEEMWQISEKIKPRGRRPVNY
| null | null |
muscle attachment [GO:0016203]; positive regulation of smoothened signaling pathway [GO:0045880]; Ras protein signal transduction [GO:0007265]; sarcomere organization [GO:0045214]; somatic muscle development [GO:0007525]
|
plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; SH3 domain binding [GO:0017124]
|
PF00617;PF00618;
|
1.10.840.10;1.20.870.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Guanine nucleotide-releasing protein that binds to SH3 domain of Crk. Transduces signals from Crk to activate RAS. Also involved in MAPK activation. {ECO:0000269|PubMed:9878058}.
|
Drosophila melanogaster (Fruit fly)
|
O77150
|
BM02_DROME
|
MKFFSVVTVFVFGLLALANAVPLSPDPGNVVINGDCKYCNVHGGK
| null | null |
defense response [GO:0006952]; innate immune response [GO:0045087]; response to bacterium [GO:0009617]
|
extracellular region [GO:0005576]
| null |
PF08194;
| null |
Bomanin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
| null | null | null | null | null |
FUNCTION: Secreted immune-induced peptide induced by Toll signaling (PubMed:25915418, PubMed:29920489, PubMed:9736738). Has a role in resistance to bacterial and fungal infections (PubMed:25915418, PubMed:29920489, PubMed:9736738). {ECO:0000269|PubMed:25915418, ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
|
Drosophila melanogaster (Fruit fly)
|
O77203
|
PIAA_DICDI
|
MTSSDSSVNTTSSSFGNISISSPNHSSSTPPLNNGNGNNVSASETELKKHVLYSLQCLDEKTLTLKVKLDHLNKLVELKKSIPDLNKLGISPTQLYKSVRPFIALPPKTIRTAGLRVMRYYLSNSNNVKELLDLKVQYFITRSLERDKHSEPERIQALKIIRTIMEIDCSLMPHCFVKGLVSIAENQEDNFCRVCLECLTEISIRNPQISSHCGGIRTVFDAVLDPFYQGIQESLLICILYLLSDKDTRIYIRPKSDLEIILAPLTNSFNIGVKLKGASKEKEKEKEKEDEVAMKKWTASSKAVLTLIKSWIGIISLNSDDQGLKSVVDTLRMPQIELQEKALDSIFEIFRVQLPKSIQETFGPQKATQTFNFGSETLQDLPSRTRSLRHNLLNNYLSVLLIAFIDNGLIEGLVYLGNYVANRDGMSEQEKECSKNISLKSTVLLAELLHMSNALLPPSQCAKLQTLPSLVNSAISFRLDPRLRSSSNTMVTNLHSYSHNKSSTTLMDSTLAIGLTGANKWRRIKGQDRRLDKVDDVKMKMEWHMDDNQFQQKIKDTQVLVTKDYQKWSWELMFELLEGPLNNPQHLSNTLKTKFIKRILSFLRPNKKLFSTMAWTTENLKYVRTACVALEVLISHEIGFDFLKDNKTIIQIADMLKVELDYNIKPPPSSSSSSENKKDNVRLLNPEKVLKTMSREYFTMLGTLSSNLLGLEILARNNIFDYIKPLAELPGRDDLSHLIMTSLDYNVNGASRTILQKILTSSSRVVRYLATKYLRFLLRSGVQDFSNWGVELLVQQLNDVDAKVSALSLNVLDEACDDPSCLEVLIDLKPNLLKLGKPGKSLLLRFLSSPKGLENLLQNNGFVEQEEQLWITSENATYVNAIESAVSESLSPSVWRFKEAPDGSSTSGVYLPPHFFGELAKTEKGCQLIRKSNNYQRFLKIIQDPTAKQLDKRASLIAIGHIGSSVDGYSFVKESDTIKLLIGIAEKSQCLALRSTCFYALGMISCIEEAQPIFNSFGWESPSDLNSRILLPKDLKNSTFLSVPQYQYQGSWADHSFETLPSNHFSDPIKNEIISFVGNLSSHITAEGASKNLKRLKIKYPDHFATSEILNAVFILLNTFKYRLGARRFIYDLFDVAIFSSDPYHDLN
| null | null |
aggregation involved in sorocarp development [GO:0031152]; chemotaxis [GO:0006935]; chemotaxis to cAMP [GO:0043327]; establishment of cell polarity [GO:0030010]; G protein-coupled chemorepellent receptor signaling pathway [GO:0140986]; mitotic cytokinesis [GO:0000281]; negative regulation of asexual reproduction [GO:1903665]; negative regulation of phagocytosis [GO:0050765]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of myosin II filament assembly [GO:0043520]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; response to electrical stimulus [GO:0051602]; sorocarp development [GO:0030587]; TORC2 signaling [GO:0038203]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; TORC2 complex [GO:0031932]
|
adenylate cyclase activator activity [GO:0010856]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF14663;PF14666;PF14664;PF14668;
| null |
RICTOR family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Regulates cell growth, chemotaxis, signal relay and the actin cytoskeleton. Required for chemoattractant receptor and G protein-mediated activation of the 12 transmembrane domain adenylyl cyclase. Functions as a part of protein complex TORC2. TORC2, is presumed to be indirectly negatively modulated by rapamycin and regulates actin polarization. TORC2, but not TORC1, negatively regulates phagocytosis. This protein and dagA protein CRAC, a cytosolic regulator, are both essential for activation of the enzyme adenylyl cyclase. This protein and CRAC do not function redundantly. Both proteins are integral components of the adenylyl cyclase activation pathway. {ECO:0000269|PubMed:11973364, ECO:0000269|PubMed:18635356, ECO:0000269|PubMed:9389653}.
|
Dictyostelium discoideum (Social amoeba)
|
O77229
|
CATA_DICDI
|
MSAPVLTTSSGSPIDNNLNSMTAGVNGPILIQDFTLIDKLAHFDRERIPERVVHAKGAGAHGYFEVPSSDVPKWCKAKFLNKVGKRTPIFTRFSTVGGEKGSSDSERDPRGFAVKFYTEEGNFDMVGNNTPVFFIRDPSKFPDFIHTQKRNPQTNCKDPNMFWDFLGQTPESTHQVSILFSDRGTPKSYRHMHGFSSHTLKFVNAQGKPYWVKLHFTSETGIQNYTAEEAAKMSMNDPDSATRDLFETIAKGGEPAWKVSIQLMEFEDALKYRFNPFDVTKIWSHKDYPLIQIGRMVLNRNPENYFAEVEQAAFSPSHMVPGIEPSPDKMLQGRLFSYPDTHRHRLGVNYQQIPVNCPFAVKGGVKNYQRDGFMAVNGNGGKGPNYQPNSFGGPEPHPEFAQHKFDVSGFAARQPYNHPNDDFVQPGDLYRLMSEDAKSRFVSNLVGHMSGVTIKEIQVRAVSNFYKADKDLGARLCKGLGIDVNDVIKFAARSNL
|
1.11.1.6
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04040};
|
hydrogen peroxide catabolic process [GO:0042744]; response to curcumin [GO:1904643]; response to hydrogen peroxide [GO:0042542]; response to methanol [GO:0033986]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]; phagocytic vesicle [GO:0045335]
|
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00199;PF06628;
|
2.40.180.10;
|
Catalase family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P04040}.
|
CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
| null | null | null | null |
FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. {ECO:0000269|PubMed:11782526}.
|
Dictyostelium discoideum (Social amoeba)
|
O77237
|
PELI_DROME
|
MVKRTDGTESPILAEDGGDGHDKPRLRYGELVILGYNGYLPQGDRGRRRSKFVLHKRTEASGVKRSKHYIVQSPQTSKAILDANQHSISYTLSRNQAVIVEYKEDTETDMFQVGRSSESPIDFVVMDTLPGDKKDAKVMQSTISRFACRILVNRCEPAKARIFAAGFDSSRNIFLGEKATKWQDNVEIDGLTTNGVLIMHPKGSFCGGNAKCGLWRECSVGGDVFSLRESRSAQQKGQPIYDECNILQDGTLIDLCGATLLWRSAEGLQHSPTKHDLEKLIDAINAGRPQCPVGLNTLVIPRKVNIGDQVNQPYVYLNCGHVQGHHDWGQDENTGARRCPMCLELGPVVTLCMGLEPAFYVDVGAPTYAFNPCGHMATEKTVKYWANVEIPHGTNGFQAVCPFCATPLDGATGYIKLIFQDNLD
| null | null |
innate immune response [GO:0045087]; negative regulation of antifungal innate immune response [GO:1905035]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of Toll signaling pathway [GO:0045751]; positive regulation of antimicrobial peptide production [GO:0002225]; positive regulation of Toll signaling pathway [GO:0045752]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]
|
cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]
|
kinase regulator activity [GO:0019207]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF04710;PF20723;
| null |
Pellino family
| null | null | null | null | null | null | null |
FUNCTION: Scaffold protein involved in the Toll signaling pathway via its interaction with pelle/pll kinase.
|
Drosophila melanogaster (Fruit fly)
|
O77277
|
TORS_DROME
|
MMSFPRMLSLCLSVLVILPLPLQSVDPLTIGAVGAVALGAYFKEHTYCRFAECCDDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGNKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNYVTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIFDEVDKMPSGVFDQLTSLVDYNAFVDGTDNTKAIFIFLSNTAGSHIASHLGSVMKNGRLREDTRLSDFEPLLRKAAYNMDGGMKKTTMIESHVIDHFIPFLPMEKAHVIKCLEAELLRWRRDPKQANNQKIIEDIINSSISYDRTHSLFAISGCKTLEKKVAMAIY
| null | null |
cellular lipid metabolic process [GO:0044255]; cellular response to misfolded protein [GO:0071218]; chaperone cofactor-dependent protein refolding [GO:0051085]; eye pigment granule organization [GO:0008057]; larval fat body development [GO:0007504]; membrane lipid biosynthetic process [GO:0046467]; neuron cellular homeostasis [GO:0070050]; nuclear envelope budding [GO:0140591]; positive regulation of cell growth [GO:0030307]; regulation of dopamine metabolic process [GO:0042053]; regulation of lipid storage [GO:0010883]; triglyceride homeostasis [GO:0070328]; vesicle scission [GO:0099050]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; nuclear envelope [GO:0005635]; nuclear membrane protein complex [GO:0106083]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
|
PF06309;
|
3.40.50.300;
|
ClpA/ClpB family, Torsin subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. {ECO:0000250}.
|
Drosophila melanogaster (Fruit fly)
|
O77334
|
YVH1_PLAF7
|
MIVKVFDYIYISNVYNANDIYELIKLNIGGVLTCFDCTCIEWCHHNDTNVTNKIFYKDIFVNTKKDLIKCDVPIITNKSVNSDIIGGTHQINNYYNEQNNNYHDNTYKEFTQTHKTNIDPSQIKSDHINEERKEHYDYIIFPSDIINNTQCNNNNLKDYIKSMLILKEDAYIDFDVIHMDQLKNKHNNNNNNNNNNNNNNNNNNNNNNCCTFKNPDISNTSQHHVEHIQIHKSNSHSNIPSDNINFCNKKYDKNLSRSVEISEKDKHPENSLLYEFVNKDKLNYKINQEEDTVSSEKNKLCDNNNNNNMVHTRHIYNVCELNKCLRENKLIPYNNIYKMKHLYLNILDTFDENILKHVNKAHLFIDSVIQKKKNILIHCMAGISRCSSIILSYVSKKNKKGIEYNFNLLKSKYPFAHPNENFYRQLLLYEKMNYTLDGCTDYHNIYKKIKMNRENLEELKILNLKNDKQPIYNFRCKHCNYVLFNDNEIIKHDFKISKIKKNYGNSCTSIFIEKKEWILTENKMKGVLNCPNVNCNIKLGKWSWTGICCSCGYLQIPAFMINSSNVDRMNISKTV
|
3.1.3.16; 3.1.3.48
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14698441}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:14698441};
|
negative regulation of nucleocytoplasmic transport [GO:0046823]; peptidyl-serine dephosphorylation [GO:0070262]; protein phosphorylation [GO:0006468]; regulation of cell development [GO:0060284]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; structural constituent of nuclear pore [GO:0017056]; zinc ion binding [GO:0008270]
|
PF00782;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14698441}. Nucleus {ECO:0000269|PubMed:14698441}. Note=Localizes to the cytoplasm at the ring stage, translocates to the nucleus in the trophozoite stage and returns to the cytoplasm at the schizont stage. {ECO:0000269|PubMed:14698441}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:14698441}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000269|PubMed:14698441}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:14698441}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000269|PubMed:14698441};
| null | null | null | null |
FUNCTION: Dual specificity protein phosphatase which dephosphorylates both phosphotyrosine and phosphoserine residues. {ECO:0000269|PubMed:14698441}.
|
Plasmodium falciparum (isolate 3D7)
|
O77410
|
EIF3E_DROME
|
MANFDLTRINCQFLDRHLTFPLLEFLCGKEIYNQQELLEYILETVNKTNMIDYTMDTRKRLNLSQEMPEELVQRKAEVLATLKQLQNEVAPIMKATDILKNGESMKDSKTFVNALQKDYNFKVEHLESAYKLAKYLYECGNYQESTSYLYFCLIVMSPNDKNYLNVLWGKLAAEILTLNWNTALEDLTRLRDYIDNANFSTIQALQQRTWLIHWSVLVFFNHPKGRDLIIEMFLYKPLYLNAIQTMCPHIMRYLATAVVINRTRRNALKDLIKVIQQESYTYRDPITEFLECLYVNFDFEGARLKLHECQTVILNDFFIVACLNEFVEDARLMIFETFCRIHQCITISMLADKLNMKPNEAECWIVNLIRNARLNAKIDSKLGHVVMGTQPLSPYQQLVEKIDSLSMRSEHLAGLIERKSKQKQNQESADSWKYY
| null | null |
formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
endoplasmic reticulum [GO:0005783]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3e [GO:0071540]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]
|
translation initiation factor activity [GO:0003743]
|
PF09440;PF01399;
| null |
EIF-3 subunit E family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:28505193}. Microsome {ECO:0000269|PubMed:10375641}. Endoplasmic reticulum {ECO:0000269|PubMed:10375641}. Note=Uniformly distributed in interphase and mitotic cells. {ECO:0000269|PubMed:28505193}.
| null | null | null | null | null |
FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (PubMed:18493598). In addition to its role in the eIF-3 complex, also functions in protein ubiquitination and degradation (PubMed:18493598, PubMed:28505193). During mitosis required for regulating mitotic microtubule growth and kinetochore formation, and consequently is required for satisfying the spindle assembly checkpoint (SAC) during metaphase to prevent delays in mitotic progression (PubMed:28505193). This is likely by promoting the ubiquitination and degradation of Klp67A, a kinesin-like protein that suppresses microtubule polymerization at plus ends (PubMed:28505193). Acts in the COP9 signalosome (CSN) mediated regulation of cullin neddylation by promoting Cul1 and Cul3 neddylation and negatively regulating the CSN complex subunit CSN5 (PubMed:18493598). {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:18493598, ECO:0000269|PubMed:28505193}.
|
Drosophila melanogaster (Fruit fly)
|
O77448
|
TERT_TETTS
|
MQKINNINNNKQMLTRKEDLLTVLKQISALKYVSNLYEFLLATEKIVQTSELDTQFQEFLTTTIIASEQNLVENYKQKYNQPNFSQLTIKQVIDDSIILLGNKQNYVQQIGTTTIGFYVEYENINLSRQTLYSSNFRNLLNIFGEEDFKYFLIDFLVFTKVEQNGYLQVAGVCLNQYFSVQVKQKKWYKNNFNMNGKATSNNNQNNANLSNEKKQENQYIYPEIQRSQIFYCNHMGREPGVFKSSFFNYSEIKKGFQFKVIQEKLQGRQFINSDKIKPDHPQTIIKKTLLKEYQSKNFSCQEERDLFLEFTEKIVQNFHNINFNYLLKKFCKLPENYQSLKSQVKQIVQSENKANQQSCENLFNSLYDTEISYKQITNFLRQIIQNCVPNQLLGKKNFKVFLEKLYEFVQMKRFENQKVLDYICFMDVFDVEWFVDLKNQKFTQKRKYISDKRKILGDLIVFIINKIVIPVLRYNFYITEKHKEGSQIFYYRKPIWKLVSKLTIVKLEEENLEKVEEKLIPEDSFQKYPQGKLRIIPKKGSFRPIMTFLRKDKQKNIKLNLNQILMDSQLVFRNLKDMLGQKIGYSVFDNKQISEKFAQFIEKWKNKGRPQLYYVTLDIKKCYDSIDQMKLLNFFNQSDLIQDTYFINKYLLFQRNKRPLLQIQQTNNLNSAMEIEEEKINKKPFKMDNINFPYYFNLKERQIAYSLYDDDDQILQKGFKEIQSDDRPFIVINQDKPRCITKDIIHNHLKHISQYNVISFNKVKFRQKRGIPQGLNISGVLCSFYFGKLEEEYTQFLKNAEQVNGSINLLMRLTDDYLFISDSQQNALNLIVQLQNCANNNGFMFNDQKITTNFQFPQEDYNLEHFKISVQNECQWIGKSIDMNTLEIKSIQKQTQQEINQTINVAISIKNLKSQLKNKLRSLFLNQLIDYFNPNINSFEGLCRQLYHHSKATVMKFYPFMTKLFQIDLKKSKQYSVQYGKENTNENFLKDILYYTVEDVCKILCYLQFEDEINSNIKEIFKNLYSWIMWDIIVSYLKKKKQFKGYLNKLLQKIRKSRFFYLKEGCKSLQLILSQQKYQLNKKELEAIEFIDLNNLIQDIKTLIPKISAKSNQQNTN
|
2.7.7.49
| null |
telomere maintenance via telomerase [GO:0007004]
|
chromosome, telomeric region [GO:0000781]; telomerase catalytic core complex [GO:0000333]; telomerase holoenzyme complex [GO:0005697]
|
metal ion binding [GO:0046872]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activity [GO:0003721]; telomeric DNA binding [GO:0042162]
|
PF11474;PF00078;PF12009;
|
1.10.132.70;3.30.70.2630;1.10.10.1970;
|
Reverse transcriptase family, Telomerase subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU365061}. Chromosome, telomere {ECO:0000255|RuleBase:RU365061, ECO:0000269|PubMed:16462747}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000269|PubMed:10944124, ECO:0000269|PubMed:15696174, ECO:0000269|PubMed:16462747, ECO:0000269|PubMed:20713447};
| null | null | null | null |
FUNCTION: Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447). {ECO:0000269|PubMed:10944124, ECO:0000269|PubMed:15696174, ECO:0000269|PubMed:16462747, ECO:0000269|PubMed:17322903, ECO:0000269|PubMed:20713447}.
|
Tetrahymena thermophila (strain SB210)
|
O77459
|
KEN_DROME
|
MKEFQRMLMLQYSKHGECILKEIGAAFRGEHPADLTIVCENKVKLHAHKLVLAAASPLIRNLLEDTHLSDCSTTVYFPDVNATYFKFLLDFLYSGQTCITSRDVNYLHDLLLLLQIKSDSWKTTDSAYLSSKCGGLRDRADRRKQQYTSPQNLEPDQTLKYEVDSVDESRNAADFSSAFNSNDNCESAAECERSGGHNNKEEDEDDCTHKDNKSDKDTDEIVNLSNAPPSGTSGSNSNISTSSNHQQQQHHHHHHHNHNNNNNNNNNNSSSSTINPVNLSLDLRTKSENSASRTLGSGSDHSGIDLAVTASESTKRKGLFFDSHKDVMKPLSDGSDINSSPENYVVTPHRKRRPGFHNTQSDNQPFTSYPHSLLEELRLAKSTTSPISGFGSEKNMLAHLEDGALNGDTLTPDRKHLLEAQRNRAQSPEIPMHLGPQFVYQWQSNQNAAMSAMPNLQSRLSSLSHISLNLDHPEGRSGSASGSGANLAGSNTHASSVREYRCEYCGKQFGMSWNLKTHLRVHTGEKPFACRLCVAMFKQKAHLLKHLCSVHRNVITTTNGADTENRYSCCFCSMCFESVQELVRHLSGHHNNLLLTKNLRE
| null | null |
female analia development [GO:0045497]; female genitalia development [GO:0030540]; male analia development [GO:0045496]; male genitalia development [GO:0030539]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00651;
|
3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor required for terminalia development. Negative regulator of the JAK/STAT pathway: represses JAK/STAT-dependent expression of ventral veins lacking (vvl) in the posterior spiracles. {ECO:0000269|PubMed:14518006, ECO:0000269|PubMed:16401426}.
|
Drosophila melanogaster (Fruit fly)
|
O77460
|
IPYR_DROME
|
MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGGQVEEVSDTVDTWHFIHLK
|
3.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
chromatin remodeling [GO:0006338]; nucleosome organization [GO:0034728]; phosphate-containing compound metabolic process [GO:0006796]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of hemocyte proliferation [GO:0035206]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; NURF complex [GO:0016589]
|
inorganic diphosphate phosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287]
|
PF00719;
|
3.90.80.10;
|
PPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:9784495}.
|
CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000269|PubMed:9784495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577; Evidence={ECO:0000269|PubMed:9784495};
| null | null | null | null |
FUNCTION: Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin (PubMed:9784495). NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis (PubMed:8521501, PubMed:9784495). Inorganic pyrophosphatase (PPase), hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential for driving critical biosynthetic reactions including transcription, replication, and DNA repair (PubMed:9784495). {ECO:0000269|PubMed:9784495, ECO:0000303|PubMed:8521501, ECO:0000303|PubMed:9784495}.
|
Drosophila melanogaster (Fruit fly)
|
O77469
|
FBLN1_CAEEL
|
MRICFLLLAFLVAETFANELTRCCAGGTRHFKNSNTCSSIKSEGTSMTCQRAASICCLRSLLDNACDSGTDIAKEEESCPSNINILGGGLKKECCDCCLLAKDLLNRNEPCVAPVGFSAGCLRSFNKCCNGDIEITHASEIITGRPLNDPHVLHLGDRCASSHCEHLCHDRGGEKVECSCRSGFDLAPDGMACVDRNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHGHCVDVDECNLGSHDCGPLYQCRNTQGSYRCDAKKCGDGELQNPMTGECTSITCPNGYYPKNGMCNDIDECVTGHNCGAGEECVNTPGSFRCQQKGNLCAHGYEVNGATGFCEDVNECQQGVCGSMECINLPGTYKCKCGPGYEFNDAKKRCEDVDECIKFAGHVCDLSAECINTIGSFECKCKPGFQLASDGRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDGTKCEDIDECSIWAGSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRTCVDVDECAMGECAGSDKVCVNTLGSFKCHSIDCPTNYIHDSLNKNQIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSKYPF
| null | null |
extracellular matrix organization [GO:0030198]; positive regulation of locomotion [GO:0040017]; protein localization [GO:0008104]
|
basement membrane [GO:0005604]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]; peptidase activator activity [GO:0016504]
|
PF12662;PF07645;
|
2.10.25.10;
|
Fibulin family
| null |
SUBCELLULAR LOCATION: [Isoform a]: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:17043142}.
| null | null | null | null | null |
FUNCTION: Incorporated into fibronectin-containing matrix fibers. Plays a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Important for certain developmental processes and contributes to the supramolecular organization of ECM architecture, in particular to those of basement membranes. {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639, ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:19104038, ECO:0000269|PubMed:22298704}.; FUNCTION: [Isoform a]: Involved in regulating the shape and adhesion of cells in the developing pharynx, intestine, body-wall muscle and gonadal tissue (PubMed:16120639). During gonadogenesis, regulates the width of gonads and the migration of distal tip cells (DTC) (PubMed:15556862, PubMed:17043142, PubMed:22298704). Together with type IV collagen let-2 and downstream of metalloprotease mig-17, recruits nidogen nid-1 to the gonad basement membrane thereby inducing basement membrane remodeling required for the directional migration of DTCs (PubMed:15556863, PubMed:19104038). Acts antagonistically with metalloprotease gon-1 to maintain optimal levels of type IV collagen emb-9 in the gonad basement membrane during gonadogenesis (PubMed:15556862, PubMed:17043142, PubMed:22298704). Required for larval development (PubMed:17043142). {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639, ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:19104038}.; FUNCTION: [Isoform c]: Involved in the assembly of the flexible hemicentin-containing tracks found joining the pharynx and body-wall-muscle basement membranes. {ECO:0000269|PubMed:16120639}.
|
Caenorhabditis elegans
|
O77485
|
FUT2_PANTR
|
MLVVQMPFSFPVAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWMGIAADLSPLLKH
|
2.4.1.344; 2.4.1.69
| null |
carbohydrate metabolic process [GO:0005975]; fucosylation [GO:0036065]; glycolipid metabolic process [GO:0006664]; protein glycosylation [GO:0006486]; regulation of cell adhesion [GO:0030155]; regulation of endothelial cell proliferation [GO:0001936]
|
Golgi cisterna membrane [GO:0032580]
|
alpha-(1,2)-fucosyltransferase activity [GO:0031127]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107]
|
PF01531;
| null |
Glycosyltransferase 11 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48800, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90376, ChEBI:CHEBI:90803; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48801; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a ganglioside Fuc-GM1 + GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639, ChEBI:CHEBI:90189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + GDP-beta-L-fucose = a ganglioside Fuc-GA1 + GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069, ChEBI:CHEBI:90262; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + Lc4Cer = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90802; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48793; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175, ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1b + GDP-beta-L-fucose = a ganglioside Fuc-GD1b + GDP + H(+); Xref=Rhea:RHEA:48324, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82939, ChEBI:CHEBI:90265; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48325; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + GDP-beta-L-fucose = a ganglioside Fuc-GM1 (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42040, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:77709, ChEBI:CHEBI:78607; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a globoside GalGb4Cer (d18:1(4E)) + GDP-beta-L-fucose = a globoside Globo-H (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62571, ChEBI:CHEBI:62649; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a lactoside III(4)-a-Fuc-Lc4Cer + GDP-beta-L-fucose = a lactoside IV(2),III(4)-a-[Fuc]2-Lc4Cer + GDP + H(+); Xref=Rhea:RHEA:62616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90811, ChEBI:CHEBI:142612; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62617; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:84728, ChEBI:CHEBI:546807; Evidence={ECO:0000250|UniProtKB:Q28113}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965; Evidence={ECO:0000250|UniProtKB:Q28113};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9JL27}.
| null | null |
FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. {ECO:0000250|UniProtKB:Q9JL27}.
|
Pan troglodytes (Chimpanzee)
|
O77486
|
FUT2_GORGO
|
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSQPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
|
2.4.1.344; 2.4.1.69
| null |
fucosylation [GO:0036065]; glycolipid metabolic process [GO:0006664]; oligosaccharide biosynthetic process [GO:0009312]; protein glycosylation [GO:0006486]; regulation of cell adhesion [GO:0030155]; regulation of endothelial cell proliferation [GO:0001936]
|
Golgi cisterna membrane [GO:0032580]
|
alpha-(1,2)-fucosyltransferase activity [GO:0031127]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107]
|
PF01531;
| null |
Glycosyltransferase 11 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48800, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90376, ChEBI:CHEBI:90803; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48801; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a ganglioside Fuc-GM1 + GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639, ChEBI:CHEBI:90189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + GDP-beta-L-fucose = a ganglioside Fuc-GA1 + GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069, ChEBI:CHEBI:90262; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + Lc4Cer = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90802; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48793; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175, ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1b + GDP-beta-L-fucose = a ganglioside Fuc-GD1b + GDP + H(+); Xref=Rhea:RHEA:48324, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82939, ChEBI:CHEBI:90265; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48325; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + GDP-beta-L-fucose = a ganglioside Fuc-GM1 (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42040, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:77709, ChEBI:CHEBI:78607; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a globoside GalGb4Cer (d18:1(4E)) + GDP-beta-L-fucose = a globoside Globo-H (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62571, ChEBI:CHEBI:62649; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a lactoside III(4)-a-Fuc-Lc4Cer + GDP-beta-L-fucose = a lactoside IV(2),III(4)-a-[Fuc]2-Lc4Cer + GDP + H(+); Xref=Rhea:RHEA:62616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90811, ChEBI:CHEBI:142612; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62617; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:84728, ChEBI:CHEBI:546807; Evidence={ECO:0000250|UniProtKB:Q28113}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965; Evidence={ECO:0000250|UniProtKB:Q28113};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9JL27}.
| null | null |
FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. {ECO:0000250|UniProtKB:Q9JL27}.
|
Gorilla gorilla gorilla (Western lowland gorilla)
|
O77487
|
FUT2_PONPY
|
MLVVQMPFSFPVAHFILFVFTVSTIFHIQQRLAKIQAMWELPEQIPVLASTSKALGPSQLRGIWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSTTASRIPWQNYHLNDWMEEKYRHIPGEYVRLTGYPCSWTFYHHLRHEILQEFTLHDHVREEAQKFLRGLQVNGSQPSTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCQENIDTSHSDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLAGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
|
2.4.1.344; 2.4.1.69
| null |
carbohydrate metabolic process [GO:0005975]; fucosylation [GO:0036065]; glycolipid metabolic process [GO:0006664]; protein glycosylation [GO:0006486]; regulation of cell adhesion [GO:0030155]; regulation of endothelial cell proliferation [GO:0001936]
|
Golgi cisterna membrane [GO:0032580]
|
alpha-(1,2)-fucosyltransferase activity [GO:0031127]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107]
|
PF01531;
| null |
Glycosyltransferase 11 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48800, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90376, ChEBI:CHEBI:90803; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48801; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a ganglioside Fuc-GM1 + GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639, ChEBI:CHEBI:90189; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + GDP-beta-L-fucose = a ganglioside Fuc-GA1 + GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069, ChEBI:CHEBI:90262; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + Lc4Cer = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90802; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48793; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175, ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GD1b + GDP-beta-L-fucose = a ganglioside Fuc-GD1b + GDP + H(+); Xref=Rhea:RHEA:48324, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82939, ChEBI:CHEBI:90265; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48325; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + GDP-beta-L-fucose = a ganglioside Fuc-GM1 (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42040, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:77709, ChEBI:CHEBI:78607; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a globoside GalGb4Cer (d18:1(4E)) + GDP-beta-L-fucose = a globoside Globo-H (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62571, ChEBI:CHEBI:62649; Evidence={ECO:0000250|UniProtKB:Q10984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045; Evidence={ECO:0000250|UniProtKB:Q10984}; CATALYTIC ACTIVITY: Reaction=a lactoside III(4)-a-Fuc-Lc4Cer + GDP-beta-L-fucose = a lactoside IV(2),III(4)-a-[Fuc]2-Lc4Cer + GDP + H(+); Xref=Rhea:RHEA:62616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90811, ChEBI:CHEBI:142612; Evidence={ECO:0000250|UniProtKB:Q9JL27}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62617; Evidence={ECO:0000250|UniProtKB:Q9JL27}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:84728, ChEBI:CHEBI:546807; Evidence={ECO:0000250|UniProtKB:Q28113}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965; Evidence={ECO:0000250|UniProtKB:Q28113};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9JL27}.
| null | null |
FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. {ECO:0000250|UniProtKB:Q9JL27}.
|
Pongo pygmaeus (Bornean orangutan)
|
O77503
|
AGO2_RABIT
|
GYAFKPPPRPDFGTSGRTIKLQANFFEMDIPKIDIYHYELDIKPEKCPRRVNREIVEHMVQHFKAQIFGDRKPVFDGRKNLYTAMPLPIGREKVELEVTLPGEGKDRIFKVSIKWVSCVSLQALHDALSGRLPSVPFETIQALDVVMRHLPSMRYTPVGRSFFTASEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFVCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPYVREFGIMVKDEMTDVTGRVLQPPSILYGGRNKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVGPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDHQALAKAVQVHQDTLRTMYFA
|
3.1.26.n2
| null |
miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated gene silencing by mRNA destabilization [GO:0035279]; negative regulation of translational initiation [GO:0045947]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; pre-miRNA processing [GO:0031054]; regulation of DNA-templated transcription [GO:0006355]; regulatory ncRNA-mediated gene silencing [GO:0031047]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]
|
endoribonuclease activity, cleaving siRNA-paired mRNA [GO:0070551]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA cap binding [GO:0098808]; RNA 7-methylguanosine cap binding [GO:0000340]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197]
|
PF08699;PF16488;PF16487;PF16486;PF02170;PF02171;
|
3.40.50.2300;2.170.260.10;3.30.420.10;
|
Argonaute family, Ago subfamily
|
PTM: Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_03031}.; PTM: Ubiquitinated on surface-exposed lysines by a SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 during target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). Ubiquitination by the SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 leads to its subsequent degradation, thereby exposing miRNAs for degradation. ZSWIM8 recognizes and binds AGO2 when it is engaged with a TDMD target. {ECO:0000250|UniProtKB:Q9UKV8}.; PTM: Phosphorylation at Ser-368 by AKT3; leads to up-regulate translational repression of microRNA target and down-regulate endonucleolytic cleavage. {ECO:0000250|UniProtKB:Q9UKV8}.; PTM: A phosphorylation cycle of C-terminal serine cluster (Ser-805-Ser-815) regulates the release of target mRNAs. Target-binding leads to phosphorylation of these residues by CSNK1A1, which reduces the affinity of AGO2 for mRNA and enables target release. The ANKRD52-PPP6C phosphatase complex dephosphorylates the residues, which primes AGO2 for binding a new target. {ECO:0000250|UniProtKB:Q9UKV8}.
|
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}. Note=Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8. {ECO:0000255|HAMAP-Rule:MF_03031}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.n2; Evidence={ECO:0000255|HAMAP-Rule:MF_03031};
| null | null | null | null |
FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. {ECO:0000255|HAMAP-Rule:MF_03031}.
|
Oryctolagus cuniculus (Rabbit)
|
O77504
|
S22A1_RABIT
|
MPTVDDVLEQVGEFGWFQKRTFLFLCLISAILAPIYLGIVFLGFTPDHRCRSPGVDELSQRCGWSPEEELNYTVPGLGATDGAFVRQCMRYEVDWNQSSLGCVDPLASLAPNRSHLPLGPCQHGWVYDTPGSSIVTEFNLVCADAWKVDLFQSCVNLGFFLGSLGVGYIADRFGRKLCLLLTTLINAVSGVLTAVAPDYTSMLLFRLLQGLVSKGSWMSGYTLITEFVGSGYRRTVAILYQVAFSVGLVALSGVAYAIPNWRWLQLTVSLPTFLCLFYYWCVPESPRWLLSQKRNTDAVKIMDNIAQKNGKLPPADLKMLSLDEDVTEKLSPSLADLFRTPNLRKHTFILMFLWFTCSVLYQGLILHMGATGGNVYLDFFYSSLVEFPAAFVILVTIDRVGRIYPMAASNLAAGVASVILIFVPQDLHWLTIVLSCVGRMGATIVLQMICLVNAELYPTFVRNLGVMVCSALCDVGGIITPFMVFRLMEVWQPLPLIVFGVLGLLAGGMTLLLPETKGVALPETIEDAENLRRKAKPKESKIYLQVQTSELKGP
| null | null |
(R)-carnitine transmembrane transport [GO:1902270]; acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; dopamine transport [GO:0015872]; monoamine transport [GO:0015844]; monoatomic ion transport [GO:0006811]; norepinephrine transport [GO:0015874]; prostaglandin transport [GO:0015732]; putrescine transport [GO:0015847]; serotonin transport [GO:0006837]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934]; thiamine transport [GO:0015888]; xenobiotic transport [GO:0042908]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]
|
(R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:O08966}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O08966}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of hepatocytes (By similarity). Mainly localized to the basolateral membrane of renal proximal tubular cells (By similarity). However, also identified at the apical side of proximal tubular cells. Mainly expressed at the lateral membrane of enterocytes (By similarity). Also observed at the apical side of enterocytes (By similarity). Localized to the basal membrane of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O08966, ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089}.
|
CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959, ChEBI:CHEBI:16347; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-isobutanoyl-(R)-carnitine(in) = O-isobutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74315, ChEBI:CHEBI:84838; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-acetyl-(R)-carnitine(in) = O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:74319, ChEBI:CHEBI:57589; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-3-hydroxybutanoyl-(R)-carnitine(in) = O-3-hydroxybutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74323, ChEBI:CHEBI:84842; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-propanoyl-(R)-carnitine(in) = O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74327, ChEBI:CHEBI:53210; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-butanoyl-(R)-carnitine(in) = O-butanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74331, ChEBI:CHEBI:21949; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-2-methylbutanoyl-(R)-carnitine(in) = O-2-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74335, ChEBI:CHEBI:84840; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-3-methylbutanoyl-(R)-carnitine(in) = O-3-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74339, ChEBI:CHEBI:70819; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=O-hexanoyl-(R)-carnitine(in) = O-hexanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74343, ChEBI:CHEBI:84834; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15245};
| null | null | null | null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:12060594, PubMed:9528667). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation. Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline. Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover. Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism. Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:12060594). {ECO:0000250|UniProtKB:O08966, ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:12060594, ECO:0000269|PubMed:9528667}.
|
Oryctolagus cuniculus (Rabbit)
|
O77507
|
RAD51_RABIT
|
MAMQMQLEANADTSVEEESFGPQPVSRLEQCGINANDVKKLEEAGFHTEEAVAYAPKKELINIKGISEAKADKILTEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVTVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
| null | null |
cellular response to camptothecin [GO:0072757]; cellular response to ionizing radiation [GO:0071479]; chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA damage response [GO:0006974]; DNA recombinase assembly [GO:0000730]; DNA strand invasion [GO:0042148]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; mitotic recombination [GO:0006312]; mitotic recombination-dependent replication fork processing [GO:1990426]; reciprocal meiotic recombination [GO:0007131]; regulation of double-strand break repair via homologous recombination [GO:0010569]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; site of double-strand break [GO:0035861]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA strand exchange activity [GO:0000150]; double-stranded DNA binding [GO:0003690]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116]
|
PF14520;PF08423;
|
1.10.150.20;3.40.50.300;
|
RecA family, RAD51 subfamily
|
PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA. Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination. {ECO:0000250|UniProtKB:Q06609}.; PTM: Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. Phosphorylated at Ser-14 by PLK1, triggering phosphorylation at Thr-13 by CK2, thereby promoting interaction with TOPBP1 and recruitment to DNA damage sites during S-phase. Phosphorylation by ABL1 inhibits function. {ECO:0000250|UniProtKB:Q06609}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Recruited at sites of DNA damage following interaction with TOPBP1 in S-phase. Colocalizes with ERCC5/XPG to nuclear foci in S phase (By similarity). {ECO:0000250|UniProtKB:Q06609}.
| null | null | null | null | null |
FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair. {ECO:0000250|UniProtKB:Q06609}.
|
Oryctolagus cuniculus (Rabbit)
|
O77510
|
TNFA_PAPHU
|
MSTESMIRDVELAEEALPRKTAGPQGSRRCWFLSLFSFLLVAGATTLFCLLHFGVIGPQREEFPKDPSLISPLAQAVRSSSRTPSDKPVVHVVANPQAEGQLQWLNRRANALLANGVELTDNQLVVPSEGLYLIYSQVLFKGQGCPSNHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINLPDYLDFAESGQVYFGIIAL
| null | null |
extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; necroptotic signaling pathway [GO:0097527]; negative regulation of protein-containing complex disassembly [GO:0043242]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of biological quality [GO:0065008]; regulation of developmental process [GO:0050793]; regulation of multicellular organismal process [GO:0051239]; regulation of secretion [GO:0051046]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor production [GO:0010573]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). {ECO:0000250}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By similarity). {ECO:0000250}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated by SIRT6, promoting its secretion. {ECO:0000250|UniProtKB:P01375}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). {ECO:0000250|UniProtKB:P01375, ECO:0000250|UniProtKB:P06804}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
|
Papio hamadryas ursinus (Chacma baboon)
|
O77564
|
FOLH1_PIG
|
MWNPLHETDSTSVAWRRPRWLCAGALVLAAGLFVLGFLFGWFIKSPNEAANISPQHNVKKAFLDELKAENIKTFLYNFTRIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTRPNYISIIDEDGNEIFNTSLFEPPPPGYENVSDVVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKILIARYGKIFRGNKVKNAQLAGAKGIILYSDPADYFAPGVQSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRLQIAEAVGLPRIPVHPIGYSDAQKLLEKMGGSAPPDDSWKGSLHVPYNVGPGFTGNFSTQKVKMHIHSDNKVKRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGKLKKEGWRPRRTVLFASWDAEEYGLFGSTEWAEENSRILQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLFESWNEKSPSPEFSGLPRISKLGSGNDFEVFFQRLGIASGRARYTKDWVTNKFSSYPLYHSVYETYELVEKFYDPTFKYHLAVAQVRGGIVFELANSVVRPFDCRDYAVVLRNYADKLYNISMNHPQEMKAYSVSFDSLFSAVKNFTEIASNFSERVQDLDKNNPILLRIMNDQLMFLERAFIVPLGLPDRAFYRHVIYAPSSHNKYMGESFPGIYDALFDIENKVDPSKAWGEVKRQISIAAFTVQAAAGTLREVA
|
3.4.17.21
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.;
|
proteolysis [GO:0006508]
|
plasma membrane [GO:0005886]
|
carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181]
|
PF02225;PF04389;PF04253;
|
3.50.30.30;1.20.930.40;3.40.630.10;
|
Peptidase M28 family, M28B subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}.
|
CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.;
| null |
FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. {ECO:0000250}.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. {ECO:0000250}.
|
Sus scrofa (Pig)
|
O77627
|
JUN_BOVIN
|
MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGLVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGSLSSGGGAPSYGAAGLAFPAQPQQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
| null | null |
cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; negative regulation by host of viral transcription [GO:0043922]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of DNA-templated transcription initiation [GO:2000144]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; release from viral latency [GO:0019046]; response to endoplasmic reticulum stress [GO:0034976]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]
|
cAMP response element binding [GO:0035497]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; general transcription initiation factor binding [GO:0140296]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription cis-regulatory region binding [GO:0000976]; ubiquitin protein ligase binding [GO:0031625]
|
PF00170;PF03957;
|
1.20.5.170;
|
BZIP family, Jun subfamily
|
PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-247; this primes the protein for subsequent phosphorylation by GSK3B at Thr-243. Phosphorylated at Thr-243, Ser-247 and Ser-253 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-290 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity (By similarity). Phosphorylated by VRK1 (By similarity). {ECO:0000250|UniProtKB:P05412}.; PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.; PTM: Acetylated at Lys-275 by EP300. {ECO:0000250|UniProtKB:P05412}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
| null | null | null | null | null |
FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28. Binds to the USP28 promoter. {ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P05627}.
|
Bos taurus (Bovine)
|
O77633
|
ADA10_PIG
|
MVLLRVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYDVDSLHQKHQRAKRAVSHEDQFLRLNFHAHGRHFNLRMKRDTSLFSDEFRVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTHGGTFYIEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQTPQEKHANNGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEQCDCGYSDQCKDECCYDANQPEGKKCRLKPEKECSPSQGPCCTAQCKFKSKTEKCRDDSDCAKEGICNGITALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMEPLTCASTGSEKWKKHFLGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAYWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQTIQPPQRQRPRESYQMGHMRR
|
3.4.24.81
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O14672}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O14672};
|
membrane protein ectodomain proteolysis [GO:0006509]; Notch signaling pathway [GO:0007219]
|
adherens junction [GO:0005912]; axon [GO:0030424]; clathrin-coated vesicle [GO:0030136]; dendrite [GO:0030425]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]
|
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metalloendopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902945]; SH3 domain binding [GO:0017124]
|
PF21299;PF00200;PF13574;
|
3.40.390.10;4.10.70.10;
| null |
PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14672}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O14672}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O14672}. Cell projection, axon {ECO:0000250|UniProtKB:O35598}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35598}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O14672}. Cytoplasm {ECO:0000250|UniProtKB:O14672}. Note=Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (By similarity). During long term depression, it is recruited to the cell membrane by DLG1 (By similarity). The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane (By similarity). The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11 (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000250|UniProtKB:O35598}.
|
CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000250|UniProtKB:O14672};
| null | null | null | null |
FUNCTION: Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis. Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (By similarity). Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (By similarity). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE-cadherin/CDH5 in endothelial cells (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000250|UniProtKB:O35598}.
|
Sus scrofa (Pig)
|
O77636
|
ADA17_PIG
|
MRQCALFLTSLVPIVLAPRPPDEPGFGSPQRLEKLDSLLSDYDILSLSSIRQHSVRKRDLQASTHLETLLTFSALNRHFKLYLTSSTERFSQNFKVVVVDGEDESEYPVKWQDFFSGHVVGEPDSRVLAHIGDDDITVRINTDGAEYNIEPLWRLINDTKDKRVLVYKSEDIKNVSRLQSPKVCGYIKADNEELLPKGLVDREPPDELVHRVKRRADPNPLRNTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGERHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPIGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLRPGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGNAEDDTVCLDLGRCKDGKCVPFCEREQRLESCACNETDHSCKVCCRAPSGRCLPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWEFIDKLSINTFGKFLADNIVGSVLVFSLMLWIPVSILVHCVDKKLDKQYESLSLLHPSNVEMLSSMDSASVRIIKPFPAPQTPGRLQPLQPLQPGPVLPSAPSVPVAPKLDHQRMDTIQEDPSTDSHVDEDGFEKDPFPNSSAAAKSFEDLTDHPVTRSEKASSFKLQRQSRVDSKETEC
|
3.4.24.86
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P78536}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78536};
|
membrane protein ectodomain proteolysis [GO:0006509]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; proteolysis [GO:0006508]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
plasma membrane [GO:0005886]
|
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; Notch binding [GO:0005112]
|
PF16698;PF00200;PF13688;
|
4.10.70.30;3.40.390.10;4.10.70.10;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P78536}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNFalpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.; EC=3.4.24.86; Evidence={ECO:0000250|UniProtKB:P78536};
| null | null | null | null |
FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (By similarity). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells. {ECO:0000250|UniProtKB:P78536, ECO:0000250|UniProtKB:Q9Z0F8}.; FUNCTION: (Microbial infection) Acts as a receptor for classical swine fever virus. {ECO:0000269|PubMed:33684175}.
|
Sus scrofa (Pig)
|
O77642
|
1433S_SHEEP
|
MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEESSEEKGPEVQEYREKVETELRGVCDTVLGLLDTHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPEEPQS
| null | null |
establishment of skin barrier [GO:0061436]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; keratinization [GO:0031424]; keratinocyte development [GO:0003334]; keratinocyte proliferation [GO:0043616]; negative regulation of innate immune response [GO:0045824]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]; positive regulation of epidermal cell differentiation [GO:0045606]; positive regulation of protein export from nucleus [GO:0046827]; protein export from nucleus [GO:0006611]; protein kinase A signaling [GO:0010737]; regulation of cell cycle [GO:0051726]; regulation of epidermal cell division [GO:0010482]; release of cytochrome c from mitochondria [GO:0001836]; stem cell proliferation [GO:0072089]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; phosphoserine residue binding [GO:0050815]; protein kinase binding [GO:0019901]; protein sequestering activity [GO:0140311]
|
PF00244;
|
1.20.190.20;
|
14-3-3 family
|
PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation. {ECO:0000250|UniProtKB:P31947}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P31947}. Nucleus {ECO:0000250|UniProtKB:O70456}. Secreted {ECO:0000250|UniProtKB:P31947}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250|UniProtKB:P31947}.
| null | null | null | null | null |
FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response. Also acts as a TP53/p53-regulated inhibitor of G2/M progression (By similarity). When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity). {ECO:0000250|UniProtKB:O70456, ECO:0000250|UniProtKB:P31947}.
|
Ovis aries (Sheep)
|
O77656
|
MMP13_BOVIN
|
MHPRVLAGFLFFSWTACWSLPLPSDGDSEDLSEEDFQFAESYLKSYYYPQNPAGILKKTAASSVIDRLREMQSFFGLEVTGRLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFRKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPYSKHPKTPDKCDPSLSLDAITSLRGETLIFKDRFFWRLHPQQVEAELFLTKSFGPELPNRIDAAYEHPSHDLIFIFRGRKFWALSGYDILEDYPKKISELGFPKHVKKISAALHFEDSGKTLFFSENQVWSYDDTNHVMDKDYPRLIEEVFPGIGDKVDAVYQKNGYIYFFNGPIQFEYSIWSNRIVRVMTTNSLLWC
|
3.4.24.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
|
bone morphogenesis [GO:0060349]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O77667
|
DHI2_BOVIN
|
MESWPWPSGGAWLLVPARALLQLLRADLRLGRPLLAALALLAALDWLCQRLLPPLAALAVLAATGWIVLSRLARPQRLPVATRAVLITGCDSGFGNATAKKLDTMGFTVLATVLDLNSPGALELRACCSSRLKLLQMDLTKPGDISRVLEFTKVHTPSTGLWGLVNNAGQNIFVADAELCPVATFRTCMEVNFFGALEMTKGLLPLLRRSSGRIVTVSSPAGDMPFPCLAAYGTSKAALALLMGNFSCELLPWGVKVSIIQPACFKTESVKDVHQWEERKQQLLATLPQELLQAYGEDYIEHLNGQFLHSLSQALPDLSPVVDAITDALLAAQPLRRYYPGHGLGLIYFIHYYLPEGLRQRFLQSFFISPYVPRALQAGQPGLTSARDIAQDQGPRPDPSPTAQ
|
1.1.1.-
| null |
glucocorticoid metabolic process [GO:0008211]
|
endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]
|
11-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0070523]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Microsome {ECO:0000250|UniProtKB:P80365}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P80365}.
|
CATALYTIC ACTIVITY: Reaction=an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH; Xref=Rhea:RHEA:53116, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346, ChEBI:CHEBI:47787, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:10822012, ECO:0000269|PubMed:17470521, ECO:0000305|PubMed:26519454}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53117; Evidence={ECO:0000269|PubMed:10822012, ECO:0000305|PubMed:17470521, ECO:0000305|PubMed:26519454}; CATALYTIC ACTIVITY: Reaction=corticosterone + NAD(+) = 11-dehydrocorticosterone + H(+) + NADH; Xref=Rhea:RHEA:42204, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600; Evidence={ECO:0000269|PubMed:10822012}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42205; Evidence={ECO:0000269|PubMed:10822012}; CATALYTIC ACTIVITY: Reaction=cortisol + NAD(+) = cortisone + H(+) + NADH; Xref=Rhea:RHEA:50208, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:10822012, ECO:0000269|PubMed:17470521, ECO:0000305|PubMed:26519454}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50209; Evidence={ECO:0000269|PubMed:10822012, ECO:0000305|PubMed:17470521, ECO:0000305|PubMed:26519454}; CATALYTIC ACTIVITY: Reaction=11beta,17beta-dihydroxyandrost-4-ene-3-one + NAD(+) = 17beta-hydroxyandrost-4-ene-3,11-dione + H(+) + NADH; Xref=Rhea:RHEA:69368, ChEBI:CHEBI:15378, ChEBI:CHEBI:34133, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:81481; Evidence={ECO:0000250|UniProtKB:P80365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69369; Evidence={ECO:0000250|UniProtKB:P80365}; CATALYTIC ACTIVITY: Reaction=11beta-hydroxyandrost-4-ene-3,17-dione + NAD(+) = androst-4-ene-3,11,17-trione + H(+) + NADH; Xref=Rhea:RHEA:69408, ChEBI:CHEBI:2495, ChEBI:CHEBI:15378, ChEBI:CHEBI:27967, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P80365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69409; Evidence={ECO:0000250|UniProtKB:P80365};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45.6 nM for cortisol {ECO:0000269|PubMed:10822012}; KM=5.5 nM for corticosterone {ECO:0000269|PubMed:10822012}; KM=71.8 nM for dexamethasone {ECO:0000269|PubMed:10822012}; Vmax=106.3 pmol/min/mg enzyme with cortisol as substrate {ECO:0000269|PubMed:10822012}; Vmax=31.6 pmol/min/mg enzyme using corticosterone as substrate {ECO:0000269|PubMed:10822012}; Vmax=36 pmol/min/mg enzyme using dexamethasone as substrate {ECO:0000269|PubMed:10822012};
|
PATHWAY: Steroid metabolism. {ECO:0000305}.
| null | null |
FUNCTION: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) (PubMed:10822012, PubMed:17470521, PubMed:26519454). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (PubMed:10822012). Affinity towards corticosterone is higher than cortisol or dexamethasone (PubMed:10822012). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone. Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro. 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (PubMed:17470521, PubMed:26519454). {ECO:0000250|UniProtKB:P51661, ECO:0000250|UniProtKB:P80365, ECO:0000269|PubMed:10822012, ECO:0000269|PubMed:17470521, ECO:0000269|PubMed:26519454, ECO:0000303|PubMed:17470521, ECO:0000303|PubMed:26519454}.
|
Bos taurus (Bovine)
|
O77668
|
OREX_PIG
|
MNPPFAKVSWATVTLLLLLLLLPPAVLSPGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRLCPGRRCLAAAASSVAPGGRSGI
| null | null |
eating behavior [GO:0042755]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of transmission of nerve impulse [GO:0051971]; regulation of neurotransmitter secretion [GO:0046928]; response to starvation [GO:0042594]; sleep [GO:0030431]; temperature homeostasis [GO:0001659]
|
cytoplasmic vesicle [GO:0031410]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791]; synapse [GO:0045202]
|
neuropeptide hormone activity [GO:0005184]; type 1 orexin receptor binding [GO:0031771]; type 2 orexin receptor binding [GO:0031772]
|
PF02072;
| null |
Orexin family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. {ECO:0000250|UniProtKB:O55232}.
|
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O55232}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O55232}. Synapse {ECO:0000250|UniProtKB:O55232}. Note=Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. {ECO:0000250|UniProtKB:O55232}.
| null | null | null | null | null |
FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-A]: Binds to orexin receptors HCRTR1/OX1R and HCRTR2/OX2R with a high affinity (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-B]: Binds to orexin receptor HCRTR2/OX2R only (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.
|
Sus scrofa (Pig)
|
O77676
|
KGP1_RABIT
|
MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKFERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLAYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENEEYSIRQGARGDTFFIISKGKVNVTREDSPSEDPIFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDGFPEDNDEPPPDDNSGWDIDF
|
2.7.11.12
| null |
negative regulation of platelet aggregation [GO:0090331]; phosphorylation [GO:0016310]; regulation of GTPase activity [GO:0043087]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; protein serine kinase activity [GO:0106310]
|
PF00027;PF16808;PF00069;
|
2.60.120.10;1.20.5.490;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily
|
PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.; PTM: 65 kDa monomer is produced by proteolytic cleavage. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with TRPC7 in the plasma membrane. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.12;
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase that acts as a key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle (By similarity). {ECO:0000250, ECO:0000269|PubMed:16885398}.
|
Oryctolagus cuniculus (Rabbit)
|
O77698
|
TRFL_BUBBU
|
MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWLKCHRWQWRMKKLGAPSITCVRRAFVLECIRAITEKKADAVTLDGGMVFEAGLDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRNSCHTGLGRSAGWNIPMGILRPYLSWTESLEPFQGAVAKFFSASCVPCVDRQAYPNLCQLCKGEGENQCACSPREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNTRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSGSFQLFGSPPGQRDLLFKDCALGFLRIPSKVDSALYLGSRYLTALKNLRETAEEVQARRARVVWCAVGPEEQKKCQQWSQQSGQIVTCATASTTDDCIALVLKGEADALSLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKGKKSCHTAVDRTAGWNIPMGLIANQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSLSERAAHVEQVLLHQQALFGENGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
|
3.4.21.-
| null |
antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; bone morphogenesis [GO:0060349]; innate immune response in mucosa [GO:0002227]; iron ion transport [GO:0006826]; negative regulation of apoptotic process [GO:0043066]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of osteoclast development [GO:2001205]; negative regulation of single-species biofilm formation in or on host organism [GO:1900229]; negative regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000308]; ossification [GO:0001503]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; proteolysis [GO:0006508]; regulation of cytokine production [GO:0001817]; regulation of tumor necrosis factor production [GO:0032680]
|
early endosome [GO:0005769]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; specific granule [GO:0042581]
|
iron ion binding [GO:0005506]; serine-type endopeptidase activity [GO:0004252]
|
PF00405;
|
3.40.190.10;
|
Transferrin family
|
PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation. {ECO:0000250|UniProtKB:P02788}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (PspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250|UniProtKB:P02788}.
|
Bubalus bubalis (Domestic water buffalo)
|
O77708
|
KCC2D_RABIT
|
MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWISHRATVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKINNKANVVTSPKENIPTPALEPQTTVIHNPDGNKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALSKSNKPIHTIILNPHVHLVGEDAACIAYIRLTQYMDGSGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTVPIKPPCIPNGKENYSGGTSLWQNI
|
2.7.11.17
| null |
positive regulation of cardiac muscle hypertrophy [GO:0010613]; protein phosphorylation [GO:0006468]; regulation of cellular localization [GO:0060341]
|
sarcolemma [GO:0042383]; sarcoplasmic reticulum membrane [GO:0033017]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
|
PF08332;PF00069;
|
3.10.450.50;6.10.140.620;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
|
PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17;
| null | null | null | null |
FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q13557, ECO:0000250|UniProtKB:Q6PHZ2}.
|
Oryctolagus cuniculus (Rabbit)
|
O77726
|
ZP2_MACRA
|
MACGQRGGSWRPSGWFNAGWSTYRSISLFFALVTSVNSIDVFQLVNPAFPGTVICDERGITVEFPSSPGTKKWHASVVDPLGLNVPNCTYILNPEKFTLRVTYENCTRRVHGGYQMTIRVMNDSAALRHGAVMYQFFCPAMQVEETQGLSASTICKKDFMSFSLPRVFSGLADDNKVTKLKMGWSIEVGDGARVKTLTLPEAMKEGFSLLIDNHRMIFHVPFNATGVTHYVQGNSHLYMVSLKLTFISPGQKVIFSSQAICAPDPVNCNATHMTLTIPEFPGKLKSVSFENQNIDVSQLHDNGIDLEATNGTKLHFSKTLLKTKLSEKCLLHQFYLASLRLTFLLQSETVSMVIYPECVCESPVSIVTGELCTQDGFMDFEVYSYQTQPALDLDTLRVGNSSCQPVFKAQSQGLVRFHIPLNGCGTRYKFEDDKVIYENEIHALWTDLPPSKISRDSEFRMTVKCSYSRNDMLLNINVESLTPPVASVKLGPFTLILQSYPDNSYQQPYGENEYPLVRFLRQPIYMEVRVINRDDPNIKLVLDDCWATSTMDPDSFPQWNIVVDGCAYELDNYQTTFHPVGSSVTHPDHYQRFDMKAFAFVSEAHVLSSLVYFHCSALICNRLSPDSPLCSVTCPVSSRHRRATEATEAEKMTVSLPGPILLLSDDSSFRGVGSSDLKASGSSGENSRSETGEEVGSRDVMDTKGHRTAGDVGSKAVAAVAALAGVVATLGFICYLYKKRTVSNH
| null | null |
binding of sperm to zona pellucida [GO:0007339]; prevention of polyspermy [GO:0060468]
|
collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
acrosin binding [GO:0032190]; structural constituent of egg coat [GO:0035804]
|
PF00100;
|
2.60.40.4100;2.60.40.3210;
|
ZP domain family, ZPA subfamily
|
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. {ECO:0000250|UniProtKB:P20239}.; PTM: Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos. {ECO:0000250|UniProtKB:P20239}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20239}.; PTM: O-glycosylated; contains sulfate-substituted glycans. {ECO:0000250|UniProtKB:P20239}.
|
SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida {ECO:0000269|PubMed:9590540}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20239}.
| null | null | null | null | null |
FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. {ECO:0000250|UniProtKB:P20239}.
|
Macaca radiata (Bonnet macaque)
|
O77736
|
TNR6_PIG
|
MSGIWVLLSLVFTCIAGPLSKGDDAQVTDPDSEMVKLNITKRESECPEGQHREGQFCCQPCPPGKRKHADCTSPGGAPQCVPCSEGEDYTDKNHHSSKCRRCRVCDGEHGLEVEKNCTRTQNTKCRCKPNFFCHTSQCEHCNPCTTCEHGVIENCTPTSNTKCREVFQSAGSRSNLHWLWALLILIPVPALVYREVKRRCRRKENGYQKPITSNAEEVPMIKDVDLGKYITRIAEQMKITEVKDFVRKNGIEETKIDEIMHDNPKDTAEQKVQLLRNWYLYHGKKDAYCTLIQGLRKAKLSALADKINDIVQKDVTSEQENANSQNENESLT
| null | null |
activation-induced cell death of T cells [GO:0006924]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; immune response [GO:0006955]; motor neuron apoptotic process [GO:0097049]; necroptotic signaling pathway [GO:0097527]; negative regulation of apoptotic process [GO:0043066]; regulation of stress-activated MAPK cascade [GO:0032872]
|
CD95 death-inducing signaling complex [GO:0031265]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]
|
calmodulin binding [GO:0005516]; tumor necrosis factor receptor activity [GO:0005031]
|
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null |
PTM: Palmitoylated. Palmitoylation by ZDHHC7 prevents the lysosomal degradation of FAS regulating its expression at the plasma membrane. {ECO:0000250|UniProtKB:P25445}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51867}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P51867}. Membrane raft {ECO:0000250|UniProtKB:P25445}.
| null | null | null | null | null |
FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase CASP8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs CASP8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity). {ECO:0000250|UniProtKB:P25445}.
|
Sus scrofa (Pig)
|
O77737
|
B2CL1_PIG
|
MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK
| null | null |
endocytosis [GO:0006897]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of execution phase of apoptosis [GO:1900118]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; regulation of cytokinesis [GO:0032465]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nuclear membrane [GO:0031965]; synaptic vesicle membrane [GO:0030672]
|
protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]
|
PF00452;PF02180;
|
1.10.437.10;
|
Bcl-2 family
|
PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. {ECO:0000250}.; PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. {ECO:0000250|UniProtKB:Q07817}.
|
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}.
|
Sus scrofa (Pig)
|
O77741
|
NRAM1_PIG
|
MTGDTDPPKQSRTQYGSISSSPSPGPPQVPPGGTYLSEKIPIPNAEPGTFSLRKLWAFTGPGFLMSIAYLDPGNIQSDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEICHLYYPKVPRTLLWLNMELAIVGSDMQEVIGTAIAFNLLSAGRIPLWGGVLITVVDTFFFLYLNNYGLRKLEAFFAFLIAIMAFTFGYEYVVARPAQGALLRGLFLPSCSGCGQPELLQAVGIVGAIIMPHNIYLHSALVKSREVDRTRREDIREANMYFLIESTIALFVSFFINLFVMAVFGQAFYQQTNQAAFNICANSSLHDYAKIFPRNNLTVAVDFYQGGVILGCLFGPAALYIWAVGLLAAGQSSTMTGTYAGQFVMEGFLKLRWSRFARLLLTRSCAILPALLVAVFKELQDLSSLNDLLNVLQSLLLPFAVLPILTFTSMPALMQEFASGRVNKVITSSIMLLVCAINFYFLVSYLPSLPHPAYFGLVALLAVIYLGLTTYLVWTCLIAHGATLLVHSSHQHFLYGLLE
| null | null |
intracellular iron ion homeostasis [GO:0006879]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transport [GO:0006828]; MAPK cascade [GO:0000165]; response to lipopolysaccharide [GO:0032496]
|
endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]
|
cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; metal cation:proton antiporter activity [GO:0051139]
|
PF01566;
| null |
NRAMP family
| null |
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P49279}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) + H(+)(out) = Fe(2+)(out) + H(+)(in); Xref=Rhea:RHEA:29439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P49279}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + Mn(2+)(in) = H(+)(in) + Mn(2+)(out); Xref=Rhea:RHEA:73063, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P49279};
| null | null | null | null |
FUNCTION: Macrophage-specific antiporter that fluxes metal ions in either direction against a proton gradient. Localized to late endosomal lysosomal membranes, delivers bivalent cations from the cytosol into these acidic compartments where they may directly affect antimicrobial activity. Involved in iron metabolism and host natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes. {ECO:0000250|UniProtKB:P49279}.
|
Sus scrofa (Pig)
|
O77742
|
OMD_BOVIN
|
MGFSSLVCVLFFFLGVKVYCQYESYQWDEDYDQEPDDVYQTEFQFQQNINYEAPFHQHTLGCASECFCPPNFPSSMYCDNRKLKTIPNIPAHIQQVYLQFNEIEAVTADSFINATHLKEINLSHNKIKSQKIDHGVFATLPNLLQLHLQHNNLEDFPFPLPKSLERIFLGYNEISRLQTNAVNGLVNLTMLDLCFNKIDDSVLQEKVLAKMEKLMQLNLCNNRLESMPPGLPSSLMYLSLENNSISSIPENYFNKLPKLHALRISHNKLQDIPYNIFNLSNLIELNVGHNKLKQAFYIPRNLEHLYLENNEIENVNVTVMCPSVDPLHYHHLTHIRIDQNKLKAPISSYIFLCFPHIHTIYYGEQQSTNGQTIQLKTQVFRRFQDDGDSEDHDDHHEGPEEEGTEENIDAHYYGSQEWQETI
| null | null |
cell adhesion [GO:0007155]
|
extracellular space [GO:0005615]
| null |
PF13855;PF01462;
|
3.80.10.10;
|
Small leucine-rich proteoglycan (SLRP) family, SLRP class II subfamily
|
PTM: The N-terminus is blocked.; PTM: Glycosylated; contains keratan sulfate. {ECO:0000269|PubMed:9566981}.; PTM: Sulfated on tyrosine residue(s). {ECO:0000305}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin. {ECO:0000269|PubMed:9566981}.
|
Bos taurus (Bovine)
|
O77746
|
PDE5A_CANLF
|
MERGSPGAGAARLPRDQDSVEAWLDDHRDFTFSYFVKKATREMVNAWFAERVHTIPVCKEGIRGHAESCSCSSQQSSRADSSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLADSEKKEQMPLTPPRFDNDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKLPDTLTRERDANRINYMYAQYVKNTMEPLNIPDVSKDKRFPWTNENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETKELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKTLINGESSQAKRN
|
3.1.4.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76074}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76074}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O76074}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000250|UniProtKB:O76074};
|
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]
|
cytosol [GO:0005829]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; metal ion binding [GO:0046872]
|
PF01590;PF00233;
|
3.30.450.40;1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family
|
PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites. Phosphorylation by PRKG1 leads to its activation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Note=PDE5A1 and PDE5A2 are located mostly to soluble cellular fractions and some to particulate cellular fractions.
|
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:O76074}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000250|UniProtKB:O76074};
| null |
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
| null | null |
FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. {ECO:0000250|UniProtKB:O76074}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O77750
|
AQP4_BOVIN
|
MSDRPAARRWGKCGPLCTRESIMVAFKGVWTQTFWKAVTAEFLAMLIFVLLSLGSTINWGGAEKPLPVDMVLISLCFGLSIATMVQCFGHISGGHINPAVTVAMVCTRRISIAKSVFYIAAQCLGAIIGAGILYLVTPPSVVGGLGVTTVHGNLSAGHGLLVELIITFQLVFTIFASCDSKRTDVTGSIALAIGISVAIGHLFAINYTGASMNPARSFGPAVIMGNWENHWIYWVGPIIGAVLAGGLYEYVFCPDVELKRRFKEAFSKAAQQTKGSYMEVEDNRSQVETDDLILKPGVVHVIDIDRGEEKKGKDPSGEVLSSV
| null | null |
cerebrospinal fluid circulation [GO:0090660]; intracellular water homeostasis [GO:0009992]; multicellular organismal-level water homeostasis [GO:0050891]; protein homotetramerization [GO:0051289]; water transport [GO:0006833]
|
astrocyte end-foot [GO:0097450]; basolateral plasma membrane [GO:0016323]; endosome membrane [GO:0010008]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]
|
water channel activity [GO:0015250]
|
PF00230;
|
1.20.1080.10;
|
MIP/aquaporin (TC 1.A.8) family
|
PTM: Phosphorylation by PKC at Ser-180 reduces conductance by 50%. Phosphorylation by PKG at Ser-111 in response to glutamate increases conductance by 40% (By similarity). {ECO:0000250}.; PTM: Isoform 2: Palmitoylated on its N-terminal region. Isoform 1: Not palmitoylated. {ECO:0000250|UniProtKB:P47863}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P55088}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Basolateral cell membrane {ECO:0000250|UniProtKB:P55088}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Endosome membrane {ECO:0000250|UniProtKB:P47863}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P55088}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cell projection {ECO:0000250|UniProtKB:P55088}. Note=Activation of the vasopressin receptor AVPR1A triggers AQP4 phosphorylation at Ser-180 and promotes its internalization from the cell membrane (By similarity). Detected on brain astrocyte processes and astrocyte endfeet close to capillaries (By similarity). {ECO:0000250|UniProtKB:P47863, ECO:0000250|UniProtKB:P55088}.
|
CATALYTIC ACTIVITY: Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; Evidence={ECO:0000250|UniProtKB:P55087};
| null | null | null | null |
FUNCTION: Forms a water-specific channel. Plays an important role in brain water homeostasis and in glymphatic solute transport. Required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability. {ECO:0000250|UniProtKB:P55088}.
|
Bos taurus (Bovine)
|
O77751
|
TM109_RABIT
|
MAGSGSSAPWGKHLLHAVLMVLVALVLLHSALAQSHRDFAPPGQQRREAPVDLLTQIGRSVRETLDTWIGPETMHLISETLSQVMWAISSAISVAFFALSGIAAQLLTALGLDGDHLTQGLKLSPSQVQTFLLWGAGALVVYWLLSLLLGLVLAVLGRILGGLKLVIFLAGFVALVRSVPDPSTRALLLLALLTLYALLSRLTGSRASGAQLEAKVRGLERQVDELRWRQRRAAKGARSVEEE
| null | null |
cellular response to gamma radiation [GO:0071480]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]
|
endoplasmic reticulum [GO:0005783]; monoatomic ion channel complex [GO:0034702]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]; sarcoplasmic reticulum membrane [GO:0033017]
|
voltage-gated monoatomic cation channel activity [GO:0022843]
|
PF14965;
| null | null |
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000269|PubMed:21381722}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:21381722}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:21381722};
| null | null | null | null |
FUNCTION: Functions as a voltage-gated monoatomic cation channel permeable to both potassium and calcium (PubMed:21381722). Plays a role in the cellular response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q3UBX0, ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:21381722}.
|
Oryctolagus cuniculus (Rabbit)
|
O77759
|
SOAT2_CHLAE
|
MEPGGARLRLQRTEGPGGEREHQPCRDGNTETHRAPDLVKWTRHMEAVKAQLLEQAQGQLRELLDRAMWEAIQSYPSQDKPPPLPPPDSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARPGARGTWTLGAGLGCALLAAHALVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYIRWNYVAKNFAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGAQARGVAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQHTGPAWNVLMWTMLFLGQGIQVSLYCQEWYARRHCPLPQTTFWGLVTPRSWSCHT
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]
|
endoplasmic reticulum membrane [GO:0005789]
|
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
|
PTM: Polyubiquitinated by AMFR/gp78 at Cys-281, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-281 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization. {ECO:0000250|UniProtKB:O75908}.; PTM: Oxidized at Cys-281: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-281, preventing ubiquitination at the same site, and resulting in protein stabilization. {ECO:0000250|UniProtKB:O75908}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46612, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:73862, ChEBI:CHEBI:84969; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46613; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46620, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:84341; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46621; Evidence={ECO:0000250|UniProtKB:O75908}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000250|UniProtKB:O75908};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa. {ECO:0000250|UniProtKB:O75908}.
|
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
|
O77760
|
SOAT1_CHLAE
|
MVGEEKMSLRNRLSKSRENPEEDEDQRKPAKESLEAPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSILEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQRWATGYSKSSHPLINSLFHGFLFMVFQIGILGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMQFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVMMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]
|
endoplasmic reticulum membrane [GO:0005789]
|
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35610}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + hexadecanoyl-CoA = cholesteryl hexadecanoate + CoA; Xref=Rhea:RHEA:42792, ChEBI:CHEBI:3663, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + octadecanoyl-CoA = cholesteryl octadecanoate + CoA; Xref=Rhea:RHEA:42812, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:82750; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + cholesterol = cholesteryl (9Z,12Z)-octadecadienoate + CoA; Xref=Rhea:RHEA:42796, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + cholesterol = cholesteryl (9Z)-hexadecenoate + CoA; Xref=Rhea:RHEA:64320, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:84323; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + cholesterol = cholesteryl (11Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64324, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121, ChEBI:CHEBI:88768; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(7Z)-octadecenoyl-CoA + cholesterol = cholesteryl (7Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64328, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:152049, ChEBI:CHEBI:152050; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329; Evidence={ECO:0000250|UniProtKB:P35610};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions. {ECO:0000250|UniProtKB:P35610}.
|
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
|
O77761
|
SOAT1_MACFA
|
MVGEEKMSLRNRLSKSRENPEEDEDQRKPAKESLEAPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSILEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQRWATGYSKSSHPLINSLFHGFLFMVFQIGILGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMQFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAAFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVMMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]
|
endoplasmic reticulum membrane [GO:0005789]
|
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35610}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + hexadecanoyl-CoA = cholesteryl hexadecanoate + CoA; Xref=Rhea:RHEA:42792, ChEBI:CHEBI:3663, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + octadecanoyl-CoA = cholesteryl octadecanoate + CoA; Xref=Rhea:RHEA:42812, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:82750; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + cholesterol = cholesteryl (9Z,12Z)-octadecadienoate + CoA; Xref=Rhea:RHEA:42796, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + cholesterol = cholesteryl (9Z)-hexadecenoate + CoA; Xref=Rhea:RHEA:64320, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:84323; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + cholesterol = cholesteryl (11Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64324, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121, ChEBI:CHEBI:88768; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(7Z)-octadecenoyl-CoA + cholesterol = cholesteryl (7Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64328, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:152049, ChEBI:CHEBI:152050; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329; Evidence={ECO:0000250|UniProtKB:P35610};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions. {ECO:0000250|UniProtKB:P35610}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
O77762
|
IL4_CANLF
|
MGLTSQLIPTLVCLLALTSTFVHGHNFNITIKEIIKMLNILTARNDSCMELTVKDVFTAPKNTSDKEIFCRAATVLRQIYTHNCSNRYLRGLYRNLSSMANKTCSMNEIKKSTLKDFLERLKVIMQKKYYRH
| null | null |
B cell activation [GO:0042113]; B cell costimulation [GO:0031296]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; innate immune response in mucosa [GO:0002227]; interleukin-4-mediated signaling pathway [GO:0035771]; microglial cell activation [GO:0001774]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of apoptotic process [GO:0043066]; negative regulation of chronic inflammatory response [GO:0002677]; negative regulation of complement-dependent cytotoxicity [GO:1903660]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of inflammatory response [GO:0050728]; negative regulation of macrophage activation [GO:0043031]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; positive regulation of amyloid-beta clearance [GO:1900223]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of eosinophil chemotaxis [GO:2000424]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of isotype switching to IgE isotypes [GO:0048295]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mast cell degranulation [GO:0043306]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of mononuclear cell migration [GO:0071677]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of immune response [GO:0050776]; regulation of phosphorylation [GO:0042325]; T-helper 2 cell differentiation [GO:0045064]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-4 receptor binding [GO:0005136]
|
PF00727;
|
1.20.1250.10;
|
IL-4/IL-13 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. {ECO:0000250|UniProtKB:P07750}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O77763
|
IFNG_EQUAS
|
MNYTSFILAFQLCAILGSSTYYCQAAFFKEIENLKEYFNASSPDVGDGGPLFLDILKNWKEDSDKKIIQSQIVSFYFKLFENLKDNQVIQKSMDTIKEDLFVKFFNSSTSKLEDFQKLIQIPVNDLKVQRKAISELIKVMNDLSPKANLRKRKRSQNPFRGRRALQ
| null | null |
adaptive immune response [GO:0002250]; astrocyte activation [GO:0048143]; defense response to virus [GO:0051607]; extrinsic apoptotic signaling pathway [GO:0097191]; humoral immune response [GO:0006959]; macrophage activation involved in immune response [GO:0002281]; macrophage differentiation [GO:0030225]; microglial cell activation [GO:0001774]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of smooth muscle cell proliferation [GO:0048662]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of autophagy [GO:0010508]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response [GO:0032834]; positive regulation of chemokine production [GO:0032722]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of fructose 1,6-bisphosphate metabolic process [GO:0060552]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-23 production [GO:0032747]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of killing of cells of another organism [GO:0051712]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of neurogenesis [GO:0050769]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of protein deacetylation [GO:0090312]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; positive regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000309]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vitamin D biosynthetic process [GO:0060557]; regulation of insulin secretion [GO:0050796]; type II interferon-mediated signaling pathway [GO:0060333]; type III interferon-mediated signaling pathway [GO:0038196]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; type II interferon receptor binding [GO:0005133]
|
PF00714;
|
1.20.1250.10;
|
Type II (or gamma) interferon family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}.
| null | null | null | null | null |
FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity). {ECO:0000250|UniProtKB:P01579, ECO:0000250|UniProtKB:P01580}.
|
Equus asinus (Donkey) (Equus africanus asinus)
|
O77764
|
TNFA_NOTEU
|
MSTENMIRDVELAEEELQRKARGPQGPGRCLCLILTFFLLLAGATLLFCLLHFGVIGPQNEEASTDAFLGMKPVTQRVRSCQTESNKPVAHVIADPLAEGKLQWLKRRANVLLSNGMDLVDNQLVVPSTGLYLVYSQLLFKGEDCANEPLLLTHTVSRVALSYQSKVNLLSAIKSPCQKTVKGAREASPWYEPIYLGGVFQLEKGDKLSADTNYPNYLDFAESGQVYFGVIAL
| null | null |
extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; necroptotic signaling pathway [GO:0097527]; negative regulation of protein-containing complex disassembly [GO:0043242]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex disassembly [GO:0043243]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of biological quality [GO:0065008]; regulation of developmental process [GO:0050793]; regulation of multicellular organismal process [GO:0051239]; regulation of secretion [GO:0051046]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vascular endothelial growth factor production [GO:0010573]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). {ECO:0000250}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By similarity). {ECO:0000250}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated by SIRT6, promoting its secretion. {ECO:0000250|UniProtKB:P01375}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). {ECO:0000250|UniProtKB:P01375, ECO:0000250|UniProtKB:P06804}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
|
Notamacropus eugenii (Tammar wallaby) (Macropus eugenii)
|
O77783
|
EXT2_BOVIN
|
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSGDWSVEKRTGRDVPLVRLPADSPVPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYPLKKYVGEAGVPVSSTISREYNELLTAISDSDYYTDDVTRACLFVPSIDLLNQNSLRVKETAQALAQLSRWDRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEVDLPEKGPGPRRYFLLSSQVALHPEYREDLAALQARHGEAVLVLDKCSNLSEGVPAARRRCHQQQAFDYPQVLQEATFCMVLRGARLGQAVLSDVLRAGCVPVIIADSYVLPFSEVLDWKRASVVVPEEKMSDVYSILQSIPRRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYPYAAISYEDWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVPSLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDDIIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFYHKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAIDGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
|
2.4.1.224
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q93063};
|
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; N-acetylglucosamine metabolic process [GO:0006044]; protein glycosylation [GO:0006486]
|
catalytic complex [GO:1902494]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
acetylglucosaminyltransferase activity [GO:0008375]; glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0050508]; glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity [GO:0050509]
|
PF03016;PF09258;
| null |
Glycosyltransferase 47 family
|
PTM: A soluble form is generated by proteolytic processing. {ECO:0000269|PubMed:9756849}.; PTM: N-glycosylated at Asn-637. {ECO:0000250|UniProtKB:Q93063}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:9756849}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized in the Golgi apparatus though both proteins are also detected in the endoplasmic reticulum (By similarity). A soluble form is found in the serum (PubMed:9756849). {ECO:0000250|UniProtKB:Q93063, ECO:0000269|PubMed:9756849}.
|
CATALYTIC ACTIVITY: Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621, Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416; EC=2.4.1.224; Evidence={ECO:0000269|PubMed:10639137, ECO:0000269|PubMed:9756849}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16214; Evidence={ECO:0000305|PubMed:9756849};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10639137, ECO:0000269|PubMed:9756849}.
| null | null |
FUNCTION: Glycosyltransferase forming with EXT1 the heterodimeric heparan sulfate polymerase which catalyzes the elongation of the heparan sulfate glycan backbone. Glycan backbone extension consists in the alternating transfer of (1->4)-beta-D-GlcA and (1->4)-alpha-D-GlcNAc residues from their respective UDP-sugar donors (PubMed:10639137, PubMed:9756849). Both EXT1 and EXT2 are required for the full activity of the polymerase since EXT1 bears the N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity within the complex while EXT2 carries the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity (By similarity). Heparan sulfate proteoglycans are ubiquitous components of the extracellular matrix and play an important role in tissue homeostasis and signaling (By similarity). {ECO:0000250|UniProtKB:Q93063, ECO:0000269|PubMed:10639137, ECO:0000269|PubMed:9756849}.
|
Bos taurus (Bovine)
|
O77788
|
NFM_BOVIN
|
MSYTLDSLGNPSAYRRVTETRSSFSRISGSPSSGFRSQSWSRGSPSTVSSSYKRSALAPRLTYSSAMLSSAESSLDFSQSSSLLDGGSGPGGDYKLSRSNEKEQIQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTFAGSITGPLYTHRQPSIAISSKIQKTKVEAPKLKVQHKFVEEIIEETKVEDEKSEMEEALTAITEELAVSVKEEVKEEEAEEKEEKEEAEEEVVAAKKSPVKATAPELKEEEGEKEEEEGQEEEEEEEEAAKSDQAEEGGSEKEGSSEKEEGEQEEEGETEAEGEGEEAAAEAKEEKKMEEKAEEVAPKEELAAEAKVEKPEKAKSPVAKSPTTKSPTAKSPEAKSPEAKSPTAKSPTAKSPVAKSPTAKSPEAKSPEAKSPTAKSPTAKSPAAKSPAPKSPVEEVKPKAEAGAEKGEQKEKVEEEKKEAKESPKEEKAEKKEEKPKDVPEKKKAESPVKAESPVKEEVPAKPVKVSPEKEAKEEEKPQEKEKEKEKVEEVGGKEEGGLKESRKEDIAINGEVEGKEEEQETKEKGSGGEEEKGVVTNGLDVSPGDEKKGGDKSEEKVVVTKMVEKITSEGGDGATKYITKSVTVTQKVEEHEETFEEKLVSTKKVEKVTSHAIVKEVTQSD
| null | null |
neurofilament bundle assembly [GO:0033693]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; postsynaptic intermediate filament cytoskeleton [GO:0099160]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylated on a number of serine residues in the repeated K-S-P tripeptide motif. Phosphorylation of NFH may result in the formation of interfilament cross-links that are important in the maintenance of axonal caliber (By similarity). {ECO:0000250}.; PTM: Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function. {ECO:0000250}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08553}. Cell projection, axon {ECO:0000250|UniProtKB:P08553}.
| null | null | null | null | null |
FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}.
|
Bos taurus (Bovine)
|
O77793
|
PA24A_HORSE
|
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISSTPDSRKRTRHFNNNINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTLSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYLAGLSGSSWYMSTLYSHPDFPEKGPEEINKELMKNVSYDPLLLLTPQKIKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDESQEPKGTENEDAERDYQNDNQASWVHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLRNFTTQESLDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKNAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLNKPTA
|
3.1.1.4; 3.1.1.5
| null |
arachidonic acid metabolic process [GO:0019369]; glycerol metabolic process [GO:0006071]; glycerophospholipid catabolic process [GO:0046475]; leukotriene biosynthetic process [GO:0019370]; monoacylglycerol biosynthetic process [GO:0006640]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylglycerol catabolic process [GO:0034478]; prostaglandin biosynthetic process [GO:0001516]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; ceramide 1-phosphate binding [GO:1902387]; lysophospholipase activity [GO:0004622]; O-acyltransferase activity [GO:0008374]; phosphatidyl phospholipase B activity [GO:0102545]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; phospholipase A2 activity [GO:0004623]
|
PF00168;PF01735;
|
2.60.40.150;3.40.1090.10;
| null |
PTM: Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:60657, ChEBI:CHEBI:74344; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387, ChEBI:CHEBI:73858, ChEBI:CHEBI:78022; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41071, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:77694; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:41123, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72828, ChEBI:CHEBI:75163; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:40451, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:74565, ChEBI:CHEBI:77091; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O = H(+) + prostaglandin E2 + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:53704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:137581, ChEBI:CHEBI:143890, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:57409, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78837, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H(+) + prostaglandin E2 + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:137585, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78836, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:77695, ChEBI:CHEBI:77696; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41099, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:75612; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41087, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:75610, ChEBI:CHEBI:78022; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088; Evidence={ECO:0000250|UniProtKB:P47712};
| null |
PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000250|UniProtKB:P47713}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000250|UniProtKB:P47712}.
| null | null |
FUNCTION: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
|
Equus caballus (Horse)
|
O77801
|
INSL3_BOVIN
|
MDRRPLTWALVLLGPALAIALGPAAAQEAPEKLCGHHFVRALVRLCGGPRWSSEEDGRPVAGGDRELLRWLEGQHLLHGLMASGDPVLVLAPQPLPQASRHHHHRRATAINPARHCCLSGCTRQDLLTLCPH
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]
|
extracellular space [GO:0005615]
|
G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O77809
|
CP1A2_MACFA
|
MALSQSVPFLATELLLASAIFCLVFWVLRGSRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQLYGDVLQIRIGSTPVLVLSGLDTIRQALVRQGDDFKGRPDLYSFTFITDGQSMSFSPDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAEALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNSHEFVESASSGNPVDFFPILRYLPNPALQRFKAFNQRFRRFLQKTVQEHYQDFDKNSVQDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTIATAISWSLMYLVTKPEIQRKIQKELDAVIGRGRRPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTTLNGFYIPRECCVFINQWQVNHDPQLWGDPSEFRPERFLTAEGTTINKPLSEKIMLFGLGKRRCIGEVLGKWEVFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHFQARLRFSIK
|
1.14.14.1; 4.2.1.152
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
arachidonic acid metabolic process [GO:0019369]; cholesterol metabolic process [GO:0008203]; estrogen metabolic process [GO:0008210]; hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; retinol metabolic process [GO:0042572]
|
endoplasmic reticulum membrane [GO:0005789]
|
17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:0020037]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}.
|
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131965; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131964; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136524; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285; Evidence={ECO:0000250|UniProtKB:P05177};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P05177}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. {ECO:0000250|UniProtKB:P05177}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
O77810
|
CP1A2_CALJA
|
MALSQFVPFSATELLLTSTVFCLVFWVFKGLRPRVPKGLKSPPEPWRWPLLGHVLTLGKNPHLALTKMSQRYGDVLQIHIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYSFTLITDGQSMSFSPDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAEALIGRLQELMAGPGRFDPYNQIVESVVKVIGAMCFGQHFPESSDEMLSLMKNSHVFVENATSGNPVDFFPILRYLPNPALQRFKAFNQRFLRFLRETVQEHYQDSDKNSVQDITGALFKHCEKRSGASGDLIPQEKIVNLVNDIFGAGFDTITTAISWSLMYLVTKPEIQRKIQKELDTVIGRGRRPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTTLKGFYIPKECCVFINQWQVNHDPQLWGDPSEFRPERFLTAKGTALNKPLSEKILLFGLGKRRCIGEVLGKWEVFLFLAILLQQLEFSVPPGVQIDLTPTYGLTMKHARCEHVQARLRFSFQ
|
1.14.14.1; 4.2.1.152
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
arachidonic acid metabolic process [GO:0019369]; cholesterol metabolic process [GO:0008203]; estrogen metabolic process [GO:0008210]; hormone biosynthetic process [GO:0042446]; progesterone metabolic process [GO:0042448]; retinol metabolic process [GO:0042572]
|
endoplasmic reticulum membrane [GO:0005789]
|
17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:0020037]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; steroid 17-alpha-monooxygenase activity [GO:0004508]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}.
|
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131965; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:131964; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136524; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; Evidence={ECO:0000250|UniProtKB:P05177}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522; Evidence={ECO:0000250|UniProtKB:P05177}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285; Evidence={ECO:0000250|UniProtKB:P05177};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P05177}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. {ECO:0000250|UniProtKB:P05177}.
|
Callithrix jacchus (White-tufted-ear marmoset)
|
O77811
|
TRFL_HORSE
|
LGLCLAAPRKSVRWCTISPAEAAKCAKFQRNMKKVRGPSVSCIRKTSSFECIQAIAANKADAVTLDGGLVYEAGLHPYKLRPVAAEVYQTRGKPQTRYYAVAVVKKGSGFQLNQLQGVKSCHTGLGRSAGWNIPIGTLRPYLNWTGPPEPLQKAVANFFSASCVPCADGKQYPNLCRLCAGTEADKCACSSQEPYFGYSGAFKCLENGAGDVAFVKDSTVFENLPDEADRDKYELLCPDNTRKPVDAFKECHLARVPSHAVVARSVDGREDLIWRLLHRAQEEFGRNKSSAFQLFKSTPENKDLLFKDSALGFVRIPSQIDSGLYLGANYLTATQNLRETAAEVAARRERVVWCAVGPEEERKCKQWSDVSNRKVACASASTTEECIALVLKGEADALNLDGGFIYVAGKCGLVPVLAENQKSQNSNAPDCVHRPPEGYLAVAVVRKSDADLTWNSLSGKKSCHTGVGRTAAWNIPMGLLFNQTGSCKFDKFFSQSCAPGADPQSSLCALCVGNNENENKCMPNSEERYYGYTGAFRCLAEKAGDVAFVKDVTVLQNTDGKNSEPWAKDLKQEDFELLCLDGTRKPVAEAESCHLARAPNHAVVSQSDRAQHLKKVLFLQQDQFGGNGPDCPGKFCLFKSETKNLLFNDNTECLAELQGKTTYEQYLGSEYVTSITNLRRCSSSPLLEACAFLRA
|
3.4.21.-
| null |
antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; bone morphogenesis [GO:0060349]; innate immune response in mucosa [GO:0002227]; iron ion transport [GO:0006826]; negative regulation of apoptotic process [GO:0043066]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of osteoclast development [GO:2001205]; negative regulation of single-species biofilm formation in or on host organism [GO:1900229]; negative regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000308]; ossification [GO:0001503]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; proteolysis [GO:0006508]; regulation of cytokine production [GO:0001817]; regulation of tumor necrosis factor production [GO:0032680]
|
early endosome [GO:0005769]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; specific granule [GO:0042581]
|
metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236]
|
PF00405;
|
3.40.190.10;
|
Transferrin family
|
PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation. {ECO:0000250|UniProtKB:P02788}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (PspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250|UniProtKB:P02788}.
|
Equus caballus (Horse)
|
O77819
|
ROCK1_RABIT
|
MSTGDSFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGDEETFPIPKAFVGNQLPFVGFTYYSNRRYLSPANPNDNRTSSNVDKSLQENLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLAQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAVLEAERRDRGHDSEMIGDLQARITSLQEEVKHLKYNLERMEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTENKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHAVSRLEETNSILTKDIELLRKENEELTDKMRKSEEEYKLQKEEEISNLKATYEKNINTERTLKTQAVNKLAEIMNRKDFKIDKKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECTHRNELQMQLASKESDIEQLRAKLSDLSDSTSVASFPSADETDPNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEVEPVQQAEKTNFQNHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLISPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
actomyosin structure organization [GO:0031032]; apoptotic process [GO:0006915]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; mitotic cytokinesis [GO:0000281]; myoblast migration [GO:0051451]; negative regulation of phosphorylation [GO:0042326]; podocyte cell migration [GO:0090521]; positive regulation of focal adhesion assembly [GO:0051894]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell migration [GO:0030334]; regulation of microtubule cytoskeleton organization [GO:0070507]; Rho protein signal transduction [GO:0007266]
|
bleb [GO:0032059]; centriole [GO:0005814]; cytoplasmic stress granule [GO:0010494]; cytoskeleton [GO:0005856]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267]
|
PF00069;PF08912;
|
1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
|
PTM: Autophosphorylated on serine and threonine residues.; PTM: Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70335}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P70335}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q13464}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13464}. Cell projection, bleb {ECO:0000250|UniProtKB:Q13464}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P70335}. Cell membrane {ECO:0000250|UniProtKB:P70335}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P70335}. Cell projection, ruffle {ECO:0000250|UniProtKB:P70335}. Note=A small proportion is associated with Golgi membranes (By similarity). Associated with the mother centriole and an intercentriolar linker (By similarity). Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers (By similarity). Localizes at the cell membrane in an ITGB1BP1-dependent manner (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q13464}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13464}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13464}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13464}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13464};
| null | null | null | null |
FUNCTION: Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (By similarity). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (By similarity) (PubMed:9139666). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (By similarity). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q13464, ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:9139666}.
|
Oryctolagus cuniculus (Rabbit)
|
O77834
|
PRDX6_BOVIN
|
MPGGLLLGDEAPNFEANTTIGRIRFHDYLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKMIALSIDSVEDHLAWSKDINAYNGEEPTEKLPFPIIDDKNRDLAIQLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVIISLQLTAEKRVATPVDWKNGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
|
1.11.1.27; 2.3.1.23; 3.1.1.4
|
COFACTOR: Note=Does not need Ca(2+) as cofactor. {ECO:0000269|PubMed:9787801};
|
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glycerophospholipid catabolic process [GO:0046475]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; response to reactive oxygen species [GO:0000302]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; calcium-independent phospholipase A2 activity [GO:0047499]; glutathione peroxidase activity [GO:0004602]; identical protein binding [GO:0042802]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004623]; ubiquitin protein ligase binding [GO:0031625]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, Prx6 subfamily
|
PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.; PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (By similarity). {ECO:0000250|UniProtKB:O35244}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9787801}. Lysosome {ECO:0000269|PubMed:9787801}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000269|PubMed:9787801}.
|
CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000269|PubMed:10409692, ECO:0000269|PubMed:2373154}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:9787801}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P30041};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for H(2)O(2) {ECO:0000269|PubMed:2373154}; KM=180 uM for H(2)O(2) {ECO:0000269|PubMed:10409692}; KM=22 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:2373154}; KM=142 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:10409692}; KM=170 uM for cumene hydroperoxide {ECO:0000269|PubMed:2373154}; KM=120 uM for cumene hydroperoxide {ECO:0000269|PubMed:10409692}; KM=12 uM for triphenylcarbinyl hydroperoxide {ECO:0000269|PubMed:2373154}; KM=34 uM for linoleic hydroperoxide {ECO:0000269|PubMed:2373154}; KM=141 uM for linolenoyl hydroperoxide {ECO:0000269|PubMed:10409692}; KM=135 uM for arachidonoyl hydroperoxide {ECO:0000269|PubMed:10409692}; KM=120 uM for PLCP hydroperoxide {ECO:0000269|PubMed:10409692}; KM=129 uM for PACP hydroperoxide {ECO:0000269|PubMed:10409692}; KM=22 uM for 5-phenyl-3-pentenyl hydroperoxide {ECO:0000269|PubMed:2373154}; KM=350 uM for dipalmitoyl phosphatidylcholine (at pH 4) {ECO:0000269|PubMed:9787801}; Vmax=5.07 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:2373154}; Vmax=1810 nmol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:10409692}; Vmax=8.56 umol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:2373154}; Vmax=1270 nmol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=9.18 umol/min/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:2373154}; Vmax=1120 nmol/min/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=2.57 umol/min/mg enzyme for triphenylcarbinyl hydroperoxide {ECO:0000269|PubMed:2373154}; Vmax=9.88 umol/min/mg enzyme for linoleic hydroperoxide {ECO:0000269|PubMed:2373154}; Vmax=1390 nmol/min/mg enzyme for linolenoyl hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=7.34 umol/min/mg enzyme for 5-phenyl-3-pentenyl hydroperoxide {ECO:0000269|PubMed:2373154}; Vmax=1380 nmol/min/mg enzyme for arachidonoyl hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=1500 nmol/min/mg enzyme for PLCP hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=1640 nmol/min/mg enzyme for PACP hydroperoxide {ECO:0000269|PubMed:10409692}; Vmax=4225 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine (at pH 4) {ECO:0000269|PubMed:9787801};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:10409692};
| null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:10409692, PubMed:2373154). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10409692). Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10409692, PubMed:2373154, PubMed:9787801). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:10409692, ECO:0000269|PubMed:2373154, ECO:0000269|PubMed:9787801}.
|
Bos taurus (Bovine)
|
O77836
|
MGT4A_BOVIN
|
MRLRNGTVATVLAFITSFLTLSWYTTWQNGKEKVIAYQREFLALKERLRIAEHRISQRSSELSAIVQQFKRVEAETNRSKDPVNKFSDDTLKILKELTSKKSLQVPSIYYHLPHLLQNEGSLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGETDTDYVNGVVANLEKEFSKEISSGLVEIISPPESYYPDLTNLKETFGDSKERVRWRTKQNLDYCFLMMYAQEKGTYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMFQAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQHVGLHSSLTGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWAITPVAGDYILFKFDKPVNVESYLFHSGNQDHPGDILLNTTVEVLPLKSEGLDISKETKDKRLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKVTN
|
2.4.1.145
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:9278430};
|
glyoxylate metabolic process [GO:0046487]; N-glycan processing [GO:0006491]; protein N-linked glycosylation [GO:0006487]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; peroxisome [GO:0005777]
|
acetylglucosaminyltransferase activity [GO:0008375]; alanine-glyoxylate transaminase activity [GO:0008453]; alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity [GO:0008454]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]
|
PF04666;
| null |
Glycosyltransferase 54 family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9278430}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9D4R2}.; SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]: Secreted {ECO:0000305|PubMed:9565571}.
|
CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507; EC=2.4.1.145; Evidence={ECO:0000269|PubMed:9278430, ECO:0000269|PubMed:9565571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058; Evidence={ECO:0000269|PubMed:9278430, ECO:0000305|PubMed:9565571}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69615, Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615, ChEBI:CHEBI:187873; Evidence={ECO:0000269|PubMed:9278430}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616; Evidence={ECO:0000269|PubMed:9278430}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187874, ChEBI:CHEBI:187875; Evidence={ECO:0000269|PubMed:9278430}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620; Evidence={ECO:0000269|PubMed:9278430}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:13532, Rhea:RHEA-COMP:18198, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137207, ChEBI:CHEBI:187877; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187878, ChEBI:CHEBI:187879; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631, Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880, ChEBI:CHEBI:187881; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187882, ChEBI:CHEBI:187883; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636; Evidence={ECO:0000250|UniProtKB:Q9UM21};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.73 mM for Gn2(2',2)core-PA {ECO:0000269|PubMed:9278430}; KM=0.13 mM for Gn2(29,2)core-PAGn3(6',2',2)core-PA {ECO:0000269|PubMed:9278430}; KM=0.22 mM for UDP-N-acetyl-alpha-D-glucosamine (with 0.8 mM Gn2(2',2)core-PA as an acceptor) {ECO:0000269|PubMed:9278430};
|
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9278430, ECO:0000269|PubMed:9565571}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|PubMed:9278430};
| null |
FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:9278430, PubMed:9565571). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:Q812G0, ECO:0000269|PubMed:9278430, ECO:0000269|PubMed:9565571}.
|
Bos taurus (Bovine)
|
O77932
|
DXO_HUMAN
|
MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK
|
3.1.13.-; 3.6.1.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O70348}; Note=Binds 2 magnesium ions. {ECO:0000250|UniProtKB:O70348};
|
mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nucleic acid metabolic process [GO:0090304]; RNA destabilization [GO:0050779]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
5'-3' exonuclease activity [GO:0008409]; magnesium ion binding [GO:0000287]; mRNA 5'-diphosphatase activity [GO:0034353]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; RNA NAD-cap (NAD-forming) hydrolase activity [GO:0110152]
|
PF08652;
| null |
DXO/Dom3Z family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21750099, ECO:0000269|PubMed:29601584}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H(+); Xref=Rhea:RHEA:78683, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:138282, ChEBI:CHEBI:167618; Evidence={ECO:0000250|UniProtKB:O70348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78684; Evidence={ECO:0000250|UniProtKB:O70348}; CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:31101919}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881; Evidence={ECO:0000305|PubMed:28283058}; CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-end phospho-ribonucleoside in snoRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000250|UniProtKB:O70348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893; Evidence={ECO:0000250|UniProtKB:O70348}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:172876, ChEBI:CHEBI:172877; Evidence={ECO:0000269|PubMed:29601584}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929; Evidence={ECO:0000305|PubMed:29601584}; CATALYTIC ACTIVITY: Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282, ChEBI:CHEBI:172372; Evidence={ECO:0000269|PubMed:32374864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493; Evidence={ECO:0000269|PubMed:32374864}; CATALYTIC ACTIVITY: Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282, ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:O70348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497; Evidence={ECO:0000250|UniProtKB:O70348};
| null | null | null | null |
FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed:28283058). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:28283058). Preferentially acts on NAD-capped transcripts in response to environmental stress (PubMed:31101919). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (By similarity). Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:29601584). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA (By similarity). Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:29601584). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). Exhibits decapping activity towards FAD-capped RNAs (PubMed:32374864). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:O70348, ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:29601584, ECO:0000269|PubMed:31101919, ECO:0000269|PubMed:32374864}.
|
Homo sapiens (Human)
|
O78310
|
SODC2_ARATH
|
MAATNTILAFSSPSRLLIPPSSNPSTLRSSFRGVSLNNNNLHRLQSVSFAVKAPSKALTVVSAAKKAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGLTPL
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
cellular response to light intensity [GO:0071484]; cellular response to oxidative stress [GO:0034599]; cellular response to ozone [GO:0071457]; cellular response to salt stress [GO:0071472]; cellular response to sucrose stimulus [GO:0071329]; cellular response to UV-B [GO:0071493]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; response to copper ion [GO:0046688]; response to iron ion [GO:0010039]; response to oxidative stress [GO:0006979]; response to salt stress [GO:0009651]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]; thylakoid [GO:0009579]
|
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9765550}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Mediates tolerance to stress, including photo-oxidative stress. {ECO:0000269|PubMed:11457901, ECO:0000269|PubMed:12885779, ECO:0000269|PubMed:16861386}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O78749
|
COX1_SHEEP
|
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMIFIIWEAFASKREVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK
|
7.1.1.9
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:27654913}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000269|PubMed:27654913}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:27654913}; Note=Binds a copper B center. {ECO:0000269|PubMed:27654913};
|
electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]
|
mitochondrial respiratory chain complex III [GO:0005750]; mitochondrial respiratory chain complex IV [GO:0005751]; respiratory chain complex IV [GO:0045277]
|
cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00115;
|
1.20.210.10;
|
Heme-copper respiratory oxidase family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27654913}; Multi-pass membrane protein {ECO:0000269|PubMed:27654913}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00401};
| null |
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
|
Ovis aries (Sheep)
|
O78750
|
COX2_SHEEP
|
MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILIMIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSELKPGELRLLEVDNRVVLPMEMTVRMLISSEDVLPSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLFYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML
|
7.1.1.9
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P68530}; Note=Binds a dinuclear copper A center per subunit. {ECO:0000250|UniProtKB:P68530};
|
ATP synthesis coupled electron transport [GO:0042773]
|
mitochondrial respiratory chain complex IV [GO:0005751]; respiratory chain complex IV [GO:0045277]
|
copper ion binding [GO:0005507]; cytochrome-c oxidase activity [GO:0004129]
|
PF00116;PF02790;
|
1.10.287.90;2.60.40.420;
|
Cytochrome c oxidase subunit 2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27654913}; Multi-pass membrane protein {ECO:0000269|PubMed:27654913}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00410};
| null | null | null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00410}.
|
Ovis aries (Sheep)
|
O80323
|
RNS3_PYRPY
|
MVHVVMMVFLLIVLILCSSTVGYDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGPDPSKCPIKNIRKREKLLEHQLEIIWPNVFDRTKNNLFWDKEWMKHGSCGYPTIDNENHYFETVIKMYISKKQNVSRILSKAKIEPDGKKRALLDIENAIRNGADNKKPKLKCQKKGTTTELVEITLCSDKSGEHFIDCPHPFEPISPHYCPTNNIKY
|
4.6.1.19
| null |
RNA catabolic process [GO:0006401]
|
extracellular region [GO:0005576]
|
ribonuclease T2 activity [GO:0033897]; RNA binding [GO:0003723]
|
PF00445;
|
3.90.730.10;
|
RNase T2 family
|
PTM: N-linked core structure at Asn-138 contains xylose. {ECO:0000269|PubMed:10469125}.
| null |
CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10045};
| null | null | null | null |
FUNCTION: Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species, self-incompatibility is controlled by the single, multiallelic locus S.
|
Pyrus pyrifolia (Chinese pear) (Pyrus serotina)
|
O80337
|
EF100_ARATH
|
MSMTADSQSDYAFLESIRRHLLGESEPILSESTASSVTQSCVTGQSIKPVYGRNPSFSKLYPCFTESWGDLPLKENDSEDMLVYGILNDAFHGGWEPSSSSSDEDRSSFPSVKIETPESFAAVDSVPVKKEKTSPVSAAVTAAKGKHYRGVRQRPWGKFAAEIRDPAKNGARVWLGTFETAEDAALAYDRAAFRMRGSRALLNFPLRVNSGEPDPVRIKSKRSSFSSSNENGAPKKRRTVAAGGGMDKGLTVKCEVVEVARGDRLLVL
| null | null |
cell division [GO:0051301]; defense response [GO:0006952]; ethylene-activated signaling pathway [GO:0009873]; phloem or xylem histogenesis [GO:0010087]; response to nematode [GO:0009624]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. {ECO:0000269|PubMed:10715325, ECO:0000269|PubMed:11950980, ECO:0000269|PubMed:9756931}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80339
|
ERF82_ARATH
|
MRRGRGSSAVAGPTVVAAINGSVKEIRFRGVRKRPWGRFAAEIRDPWKKARVWLGTFDSAEEAARAYDSAARNLRGPKAKTNFPIDSSSPPPPNLRFNQIRNQNQNQVDPFMDHRLFTDHQQQFPIVNRPTSSSMSSTVESFSGPRPTTMKPATTKRYPRTPPVVPEDCHSDCDSSSSVIDDDDDIASSSRRRNPPFQFDLNFPPLDCVDLFNGADDLHCTDLRL
| null | null |
defense response [GO:0006952]; ethylene-activated signaling pathway [GO:0009873]; negative regulation of ethylene-activated signaling pathway [GO:0010105]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional repressor. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways and could also regulate other AtERFs. {ECO:0000269|PubMed:10715325, ECO:0000269|PubMed:11487705, ECO:0000269|PubMed:9756931}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80340
|
ERF78_ARATH
|
MAKMGLKPDPATTNQTHNNAKEIRYRGVRKRPWGRYAAEIRDPGKKTRVWLGTFDTAEEAARAYDTAARDFRGAKAKTNFPTFLELSDQKVPTGFARSPSQSSTLDCASPPTLVVPSATAGNVPPQLELSLGGGGGGSCYQIPMSRPVYFLDLMGIGNVGRGQPPPVTSAFRSPVVHVATKMACGAQSDSDSSSVVDFEGGMEKRSQLLDLDLNLPPPSEQA
| null | null |
cellular response to hypoxia [GO:0071456]; ethylene-activated signaling pathway [GO:0009873]; induced systemic resistance, jasmonic acid mediated signaling pathway [GO:0009864]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ethylene-activated signaling pathway [GO:0010105]; response to abscisic acid [GO:0009737]; response to ethylene [GO:0009723]
|
nuclear body [GO:0016604]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional repressor. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways, and could also regulate other AtERFs. {ECO:0000269|PubMed:10715325, ECO:0000269|PubMed:11487705, ECO:0000269|PubMed:9756931}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80345
|
CDKF1_ARATH
|
MDKQPATSWSIHTRPEIIAKYEIFERVGSGAYADVYRARRLSDGLIVALKEIFDYQSAFREIDALTILNGSPNVVVMHEYFWREEENAVLVLEFLRSDLAAVIRDGKRKKKVEGGDGFSVGEIKRWMIQILTGVDACHRNLIVHRDLKPGNMLISDDGVLKLADFGQARILMEHDIVASDENQQAYKLEDKDGETSEPPEVIPDYENSPRQGSDGQEREAMSKDEYFRQVEELKAKQVVRDDTDKDSNVHDGDISCLATCTVSEMDDDLGRNSFSYDADEAVDDTQGLMTSCVGTRWFRPPELLYGSTMYGLEVDLWSLGCVFAELLSLEPLFPGISDIDQISRVTNVLGNLNEEVWPGCVDLPDYKSISFAKVESPLGIEGCLPNHSGDVISLLKKLICYDPASRATTMEMLNDKYLSEEPLPVPVSELYVPPTMSGPDEDSPRKWNDYREMDSDSDFDGFGPMNVKPTSSGFTIEFP
|
2.7.11.22; 2.7.11.23
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; maintenance of root meristem identity [GO:0010078]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cyclin-dependent protein kinase activating kinase activity [GO:0019912]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23;
| null | null | null | null |
FUNCTION: CDK-activating kinase that modulates CDKD-2 and CDKD-3 activities by phosphorylation of the T-loop. Activates CDKD-2 C-terminal domain (CTD) kinase activity. Activates CDKA-1 probably by phosphorylation. Posseses a CDK kinase activity independently of association with cyclin CYCH1-1. Phosphorylates the CTD of the large subunit of RNA polymerase II. {ECO:0000269|PubMed:12084729, ECO:0000269|PubMed:15486101, ECO:0000269|PubMed:16856985}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80358
|
FPG_ARATH
|
MPELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKTIISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKGVAVTKYKRSAVKDSEEWPSKYSKFFVELDDGLELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKKITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTSIKEVIEKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPELQKLYGKDAEKAAKVRPAKRGVKPKEDDGDGEEDEQETEKEDESAKSKKGQKPRGGRGKKPASKTKTEESDDDGDDSEAEEEVVKPKGRGTKPAIKRKSEEKATSQAGKKPKGRKS
|
3.2.2.23; 4.2.99.18
| null |
base-excision repair [GO:0006284]; DNA repair [GO:0006281]; response to oxidative stress [GO:0006979]
|
nucleus [GO:0005634]
|
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; zinc ion binding [GO:0008270]
|
PF01149;PF21218;PF06831;
|
1.10.8.50;3.20.190.10;
|
FPG family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.; EC=3.2.2.23; Evidence={ECO:0000269|PubMed:22789755}; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE-ProRule:PRU00392, ECO:0000269|PubMed:22789755};
| null | null | null | null |
FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Can process efficiently 4,6-diamino-5-formamidopyrimidine (FapyA), 2,6-diamino-4- hydroxy-5-formamidopyrimidine (FapyG) and the further oxidation products of 8-oxoguanine (8-oxoG), such as guanidinohydantoin and spiroiminodihydantoin. Has marginal activity towards 8-oxoG. Has AP (apurinic/apyrimidinic) lyase activity. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:11272725, ECO:0000269|PubMed:22789755, ECO:0000269|PubMed:9819050}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80366
|
ARR9_ARATH
|
MGMAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSNDPNAFSKAPVNHQVVEVNLIITDYCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKLKPHMMKTKLKNQKLEEIETTSKVENGVPTAVADPEIKDSTNIEIEILPLQQDLLLVQQEEQTLSINNKRKSVEEGISTDRARPRFDGIATAV
| null | null |
circadian rhythm [GO:0007623]; cytokinin-activated signaling pathway [GO:0009736]; phosphorelay signal transduction system [GO:0000160]; regulation of DNA-templated transcription [GO:0006355]; response to cytokinin [GO:0009735]
|
nucleus [GO:0005634]
|
phosphorelay response regulator activity [GO:0000156]
|
PF00072;
|
3.40.50.2300;
|
ARR family, Type-A subfamily
|
PTM: Two-component system major event consists of a His-to-Asp phosphorelay between a sensor histidine kinase (HK) and a response regulator (RR). In plants, the His-to-Asp phosphorelay involves an additional intermediate named Histidine-containing phosphotransfer protein (HPt). This multistep phosphorelay consists of a His-Asp-His-Asp sequential transfer of a phosphate group between first an His and an Asp of the HK protein, followed by the transfer to a conserved His of the HPt protein and finally the transfer to an Asp in the receiver domain of the RR protein.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. {ECO:0000269|PubMed:14973166}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80396
|
M2K3_ARATH
|
MAALEELKKKLSPLFDAEKGFSSSSSLDPNDSYLLSDGGTVNLLSRSYGVYNFNELGLQKCTSSHVDESESSETTYQCASHEMRVFGAIGSGASSVVQRAIHIPNHRILALKKINIFEREKRQQLLTEIRTLCEAPCHEGLVDFHGAFYSPDSGQISIALEYMNGGSLADILKVTKKIPEPVLSSLFHKLLQGLSYLHGVRHLVHRDIKPANLLINLKGEPKITDFGISAGLENSMAMCATFVGTVTYMSPERIRNDSYSYPADIWSLGLALFECGTGEFPYIANEGPVNLMLQILDDPSPTPPKQEFSPEFCSFIDACLQKDPDARPTADQLLSHPFITKHEKERVDLATFVQSIFDPTQRLKDLADMLTIHYYSLFDGFDDLWHHAKSLYTETSVFSFSGKHNTGSTEIFSALSDIRNTLTGDLPSEKLVHVVEKLHCKPCGSGGVIIRAVGSFIVGNQFLICGDGVQAEGLPSFKDLGFDVASRRVGRFQEQFVVESGDLIGKYFLAKQELYITNLD
|
2.7.12.2
| null |
abscisic acid-activated signaling pathway [GO:0009738]; defense response to other organism [GO:0098542]; induced systemic resistance, ethylene mediated signaling pathway [GO:0009866]; induced systemic resistance, jasmonic acid mediated signaling pathway [GO:0009864]; phosphorylation [GO:0016310]; response to abscisic acid [GO:0009737]; response to herbivore [GO:0080027]; response to wounding [GO:0009611]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; JUN kinase kinase activity [GO:0008545]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
3.10.450.50;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
|
PTM: Phosphorylation at Ser-235 and Thr-241 by MAP kinase kinase kinases positively regulates kinase activity (Probable). Phosphorylated by MAPKKK20 (PubMed:28848569). {ECO:0000269|PubMed:28848569, ECO:0000305|PubMed:17369371, ECO:0000305|PubMed:17933903, ECO:0000305|PubMed:21419340}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28848569}. Cytoplasm {ECO:0000269|PubMed:28848569, ECO:0000269|PubMed:30081740}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
| null | null | null | null |
FUNCTION: MKK3-MPK6 module plays an important role in the jasmonate signal transduction pathway through the negative regulation of MYC2/JIN1 expression. Activates by phosphorylation the downstream MPK6, MPK7 and MPK8. MKK3-MPK7 module acts as a positive regulator of PR1 gene expression. MKK3-MPK8 module negatively regulates ROS accumulation through controlling expression of the RBOHD gene. Component of the abscisic acid (ABA) signaling pathway that may act as ABA signal transducer in the context of abiotic stresses. Activator of the C group MAP kinases. Activates MPK7 in response to ABA (PubMed:25720833). Mitogen-activated protein kinase (MAPK) that is specifically regulated by MAPKKK20 and mediates signaling that regulates cortical microtubule functions (PubMed:28848569). {ECO:0000269|PubMed:17369371, ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340, ECO:0000269|PubMed:25720833, ECO:0000269|PubMed:28848569}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80397
|
M2K4_ARATH
|
MRPIQSPPGVSVPVKSRPRRRPDLTLPLPQRDVSLAVPLPLPPTSGGSGGSSGSAPSSGGSASSTNTNSSIEAKNYSDLVRGNRIGSGAGGTVYKVIHRPSSRLYALKVIYGNHEETVRRQICREIEILRDVNHPNVVKCHEMFDQNGEIQVLLEFMDKGSLEGAHVWKEQQLADLSRQILSGLAYLHSRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLNQGKYDGYAGDIWSLGVSILEFYLGRFPFPVSRQGDWASLMCAICMSQPPEAPATASPEFRHFISCCLQREPGKRRSAMQLLQHPFILRASPSQNRSPQNLHQLLPPPRPLSSSSSPTT
|
2.7.12.2
| null |
defense response to other organism [GO:0098542]; floral organ abscission [GO:0010227]; inflorescence development [GO:0010229]; phosphorylation [GO:0016310]; plant-type hypersensitive response [GO:0009626]; pollen-pistil interaction [GO:0009875]
|
chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; JUN kinase kinase activity [GO:0008545]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
|
PTM: Phosphorylation at Thr-224 and Ser-230 by MAP kinase kinase kinases positively regulates kinase activity. Phosphorylation at Ser-230 and Thr-234 by GSK3/Shaggy-like kinase ASKs negatively regulates kinase activity. Phosphorylated by MAPKKK5 (PubMed:27679653). {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:27679653}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Plastid, chloroplast stroma.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
| null | null | null | null |
FUNCTION: Involved in the second phase of hydrogen peroxide generation during hypersensitive response-like cell death. Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. Activates by phosphorylation the downstream MPK3 and MPK6. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the guard mother cell (GMC) is specified. This MAPK cascade also functions downstream of the ER receptor in regulating coordinated local cell proliferation, which shapes the morphology of plant organs. MKK4 and MKK5 participate in the regulation of floral organ abscission. Mediates osmotic-stress response via its regulation of MPK3 activity. Target of the Pseudomonas syringae type III effector HopF2. {ECO:0000269|PubMed:11687590, ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:17259259, ECO:0000269|PubMed:18809915, ECO:0000269|PubMed:21806969, ECO:0000269|PubMed:23263767, ECO:0000269|PubMed:23341468}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80400
|
VPS_HUMLU
|
MASVTVEQIRKAQRAEGPATILAIGTAVPANCFNQADFPDYYFRVTKSEHMTDLKKKFQRMCEKSTIKKRYLHLTEEHLKQNPHLCEYNAPSLNTRQDMLVVEVPKLGKEAAINAIKEWGQPKSKITHLIFCTGSSIDMPGADYQCAKLLGLRPSVKRVMLYQLGCYAGGKVLRIAKDIAENNKGARVLIVCSEITACIFRGPSEKHLDCLVGQSLFGDGASSVIVGADPDASVGERPIFELVSAAQTILPNSDGAIAGHVTEAGLTFHLLRDVPGLISQNIEKSLIEAFTPIGINDWNNIFWIAHPGGPAILDEIEAKLELKKEKMKASREMLSEYGNMSCASVFFIVDEMRKQSSKEGKSTTGDGLEWGALFGFGPGLTVETVVLHSVPTNV
|
2.3.1.156; 2.3.1.74
| null |
polyketide biosynthetic process [GO:0030639]
| null |
chalcone synthase activity [GO:0102128]; naringenin-chalcone synthase activity [GO:0016210]; phloroisovalerophenone synthase activity [GO:0050634]
|
PF02797;PF00195;
|
3.40.47.10;
|
Thiolase-like superfamily, Chalcone/stilbene synthases family
| null | null |
CATALYTIC ACTIVITY: Reaction=3-methylbutanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + phlorisovalerophenone; Xref=Rhea:RHEA:23572, ChEBI:CHEBI:15378, ChEBI:CHEBI:15951, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:57384; EC=2.3.1.156; Evidence={ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:15170123}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23573; Evidence={ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:15170123}; CATALYTIC ACTIVITY: Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74; Evidence={ECO:0000269|PubMed:15170123}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11129; Evidence={ECO:0000269|PubMed:15170123}; CATALYTIC ACTIVITY: [Phloroisovalerophenone synthase]: Reaction=2-methylpropanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + phlorisobutanophenone; Xref=Rhea:RHEA:67000, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:57384, ChEBI:CHEBI:133419; EC=2.3.1.156; Evidence={ECO:0000269|PubMed:15170123}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67001; Evidence={ECO:0000269|PubMed:15170123};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 uM for 3-methylbutanoyl-CoA {ECO:0000269|PubMed:10336650}; KM=10 uM for 2-methylpropanoyl-CoA {ECO:0000269|PubMed:10336650}; KM=33 uM for malonyl-CoA {ECO:0000269|PubMed:10336650};
|
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:10336650};
| null |
FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Polyketide synthase that can use 3-methylbutanoyl-CoA (isovaleryl-CoA) and 2-methylpropanoyl-CoA (isobutyryl-CoA) as substrates to produce phlorisovalerophenone (PIVP) and phlorisobutyrophenone (2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one), respectively, intermediates in the biosynthesis of the bitter acids (alpha and beta) acids (PubMed:10336650, PubMed:11272819, PubMed:15170123). Can also produce naringenin-chalcone (2',4,4',6'-tetrahydroxychalcone) from 4-coumaroyl-CoA with a lower efficiency (PubMed:15170123). {ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:15170123, ECO:0000305|PubMed:30468448}.
|
Humulus lupulus (European hop)
|
O80434
|
LAC4_ARATH
|
MGSHMVWFLFLVSFFSVFPAPSESMVRHYKFNVVMKNVTRLCSSKPTVTVNGRYPGPTIYAREDDTLLIKVVNHVKYNVSIHWHGVRQVRTGWADGPAYITQCPIQPGQVYTYNYTLTGQRGTLWWHAHILWLRATVYGALVILPKRGVPYPFPKPDNEKVIVLGEWWKSDTENIINEALKSGLAPNVSDSHMINGHPGPVRNCPSQGYKLSVENGKTYLLRLVNAALNEELFFKVAGHIFTVVEVDAVYVKPFKTDTVLIAPGQTTNVLLTASKSAGKYLVTASPFMDAPIAVDNVTATATVHYSGTLSSSPTILTLPPPQNATSIANNFTNSLRSLNSKKYPALVPTTIDHHLFFTVGLGLNACPTCKAGNGSRVVASINNVTFIMPKTALLPAHYFNTSGVFTTDFPKNPPHVFNYSGGSVTNMATETGTRLYKLPYNATVQLVLQDTGVIAPENHPVHLHGFNFFEVGRGLGNFNSTKDPKNFNLVDPVERNTIGVPSGGWVVIRFRADNPGVWFMHCHLEVHTTWGLKMAFLVENGKGPNQSILPPPKDLPKC
|
1.10.3.2
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 4 Cu cations per monomer. {ECO:0000250};
|
lignin biosynthetic process [GO:0009809]; lignin catabolic process [GO:0046274]; plant-type secondary cell wall biogenesis [GO:0009834]
|
apoplast [GO:0048046]; plant-type cell wall [GO:0009505]
|
copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491]
|
PF00394;PF07731;PF07732;
|
2.60.40.420;
|
Multicopper oxidase family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
| null | null | null | null |
FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Required for secondary xylem cell wall lignification. {ECO:0000250, ECO:0000269|PubMed:15980264}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80438
|
MAK3_ARATH
|
MEKEMEDKEEFDEGEIEYTSYAGEHHLPLIMSLVDQELSEPYSIFTYRYFVYLWPQLCFLAFHKGKCVGTIVCKMGDHRQTFRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHYYLNGMDAFRLKLLFPKPRVPQIPSQVQTQQEYETFPRPRVP
|
2.3.1.256
| null | null |
cytoplasm [GO:0005737]; NatC complex [GO:0031417]
|
peptide alpha-N-acetyltransferase activity [GO:0004596]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family, MAK3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12897255}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]; Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256; Evidence={ECO:0000303|PubMed:12897255}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256; Evidence={ECO:0000303|PubMed:12897255}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256; Evidence={ECO:0000303|PubMed:12897255}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256; Evidence={ECO:0000303|PubMed:12897255}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]; Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256; Evidence={ECO:0000303|PubMed:12897255};
| null | null | null | null |
FUNCTION: Probably required for N-acetylation of some chloroplast precursor proteins and efficient accumulation of thylakoid multiprotein complexes. In yeast, can replace the NatC complex (composed of MAK3, MAK10 and MAK31) by acetylating N termini of endogenous proteins and the N-terminus Met of L-A virus Gag protein. However, the formation of a NatC complex is not required for this function. {ECO:0000269|PubMed:12897255}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80448
|
PDX11_ARATH
|
MAGTGVVAVYGEGAMTETKQKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDDKVERFASRSE
|
4.3.3.6
| null |
amino acid metabolic process [GO:0006520]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615]
|
chloroplast [GO:0009507]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]
|
protein heterodimerization activity [GO:0046982]; pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity [GO:0036381]
|
PF01680;
|
3.20.20.70;
|
PdxS/SNZ family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16157873}.
|
CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000269|PubMed:17468224};
| null |
PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
| null | null |
FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers. {ECO:0000269|PubMed:16157873, ECO:0000269|PubMed:17468224}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80449
|
JOX4_ARATH
|
MATCWPEPIVSVQSLSQTGVPTVPNRYVKPAHQRPVFNTTQSDAGIEIPVLDMNDVWGKPEGLRLVRSACEEWGFFQMVNHGVTHSLMERVRGAWREFFELPLEEKRKYANSPDTYEGYGSRLGVVKDAKLDWSDYFFLNYLPSSIRNPSKWPSQPPKIRELIEKYGEEVRKLCERLTETLSESLGLKPNKLMQALGGGDKVGASLRTNFYPKCPQPQLTLGLSSHSDPGGITILLPDEKVAGLQVRRGDGWVTIKSVPNALIVNIGDQLQILSNGIYKSVEHQVIVNSGMERVSLAFFYNPRSDIPVGPIEELVTANRPALYKPIRFDEYRSLIRQKGPCGKNQVDSLLLTR
|
1.14.11.-
|
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805};
|
defense response [GO:0006952]; negative regulation of defense response to insect [GO:1900366]; regulation of defense response to fungus [GO:1900150]; regulation of jasmonic acid mediated signaling pathway [GO:2000022]
|
cytosol [GO:0005829]
|
dioxygenase activity [GO:0051213]; iron ion binding [GO:0005506]; jasmonic acid hydrolase [GO:0120091]
|
PF03171;PF14226;
| null |
Iron/ascorbate-dependent oxidoreductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + jasmonate + O2 = (1R,2R)-12-hydroxyjasmonate + CO2 + succinate; Xref=Rhea:RHEA:67144, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58431, ChEBI:CHEBI:132022; Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67145; Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
| null | null | null | null |
FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the oxidation of jasmonate (JA), a stress-induced phytohormone synthesized in response to attack by pathogens and herbivores, which triggers the activation of defense responses via the JA-mediated signaling pathway (PubMed:28559313, PubMed:28760569). Converts JA to 12-hydroxyjasmonate (12OH-JA), an inactive form of JA (PubMed:28559313, PubMed:28760569). Is specific to free JA, and cannot oxidize the bioactive form jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates (PubMed:28760569). Prevents over-accumulation of JA and indirectly its bioactive form JA-Ile under stress response (PubMed:28559313, PubMed:28760569). Acts as a negative regulator of JA-mediated defense signaling, by contributing to 12OH-JA accumulation, which represses JA defense responses upon infection by the fungal pathogen Botrytis cinerea (PubMed:28559313, PubMed:28760569). Acts as a negative regulator of JA-mediated defense responses upon infestation by the herbivorous caterpillar Mamestra brassicae (PubMed:28559313). {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80450
|
TGT3B_ARATH
|
MDGHQHHHLHQLQYLNKHHLHTQSQTPEIASPVAVGDRFPQWSVEETKELIGIRGELDQTFMETKRNKLLWEVISNKMRDKSFPRSPEQCKCKWKNLVTRFKGCETMEAETARQQFPFYDDMQNIFTTRMQRMLWAESEGGGGGTSGAARKREYSSDEEEENVNEELVDVSNDPKILNPKKNIAKKRKGGSNSSNSNNGVREVLEEFMRHQVRMESEWREGWEAREKERAEKEEEWRRKMEELEKERLAMERMWRDREEQRRSREEMRAEKRDSLINALLAKLTRDGSL
| null | null |
regulation of DNA-templated transcription [GO:0006355]
|
mediator complex [GO:0016592]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]
|
PF13837;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor that may play a role in the induction of CAM4 in response to pathogen and salt. {ECO:0000269|PubMed:15310827}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80452
|
AMPD_ARATH
|
MEPNIYQLALAALFGASFVAVSGFFMHFKALNLVLERGKERKENPDGDEPQNPTLVRRRSQVRRKVNDQYGRSPASLPDATPFTDGGGGGGGDTGRSNGHVYVDEIPPGLPRLHTPSEGRASVHGASSIRKTGSFVRPISPKSPVASASAFESVEESDDDDNLTNSEGLDASYLQANGDNEMPADANEEQISMAASSMIRSHSVSGDLHGVQPDPIAADILRKEPEQETFVRLNVPLEVPTSDEVEAYKCLQECLELRKRYVFQETVAPWEKEVISDPSTPKPNTEPFAHYPQGKSDHCFEMQDGVVHVFANKDAKEDLFPVADATAFFTDLHHVLKVIAAGNIRTLCHRRLVLLEQKFNLHLMLNADKEFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLREVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLGEITKQVFSDLEASKYQMAEYRISIYGRKMSEWDQLASWIVNNDLYSENVVWLIQLPRLYNIYKDMGIVTSFQNILDNIFIPLFEATVDPDSHPQLHVFLKQVVGFDLVDDESKPERRPTKHMPTPAQWTNAFNPAFSYYVYYCYANLYVLNKLRESKGMTTITLRPHSGEAGDIDHLAATFLTCHSIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPVFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASVWKLSACDLCEIARNSVYQSGFSHALKSHWIGKDYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLGKAVISDEVVP
|
3.5.4.6
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16543243}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16543243};
|
AMP metabolic process [GO:0046033]; embryo development ending in seed dormancy [GO:0009793]; IMP salvage [GO:0032264]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]
|
AMP deaminase activity [GO:0003876]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein histidine kinase binding [GO:0043424]
|
PF19326;
|
4.10.800.20;3.20.20.140;
|
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16543243}; Single-pass membrane protein {ECO:0000269|PubMed:16543243}. Microsome membrane {ECO:0000269|PubMed:16543243}. Note=Might be associated with the inner mitochondrial membrane. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:16543243};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 mM for AMP (in the absence of ATP) {ECO:0000269|PubMed:16543243}; KM=0.26 mM for AMP (in the presence of 1 mM ATP) {ECO:0000269|PubMed:16543243}; Vmax=17 umol/min/mg enzyme (in the absence of ATP) {ECO:0000269|PubMed:16543243}; Vmax=375 umol/min/mg enzyme (in the presence of 1 mM ATP) {ECO:0000269|PubMed:16543243};
|
PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
| null | null |
FUNCTION: AMP deaminase plays a critical role in energy metabolism. Essential for the transition from zygote to embryo. {ECO:0000269|PubMed:15918887}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80458
|
DDPS1_ARATH
|
MLSLLSSDSSLLSLLFLFLIPCLFITSYIGFPVFLLKLIGLIKIKAARDNEKRDEGTYVVREDGLQRELMPRHVAFILDGNRRWAKRAGLTTSQGHEAGAKRLIDIAELCFELGVHTVSAFAFSTENWGRDKIEIDNLMSLIQHYRNKSNIKFFHRSEVRVSVIGNKTKIPESLLKEIHEIEEATKGYKNKHLIMAVDYSGKFDIMHACKSLVKKSEKGLIREEDVDEALIERELLTNCSDFPSPDLMIRTSGEQRISNFFLWQLAYSELFFSPVFWPDFDKDKLLEALASYQRRERRFGCRV
|
2.5.1.87
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
dolichol biosynthetic process [GO:0019408]; plastid membrane organization [GO:0009668]; protein glycosylation [GO:0006486]; response to cold [GO:0009409]
|
chloroplast stroma [GO:0009570]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
dehydrodolichyl diphosphate synthase activity [GO:0045547]; polyprenyltransferase activity [GO:0002094]
|
PF01255;
|
3.40.1180.10;
|
UPP synthase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10764783, ECO:0000269|PubMed:10908715}; Single-pass membrane protein {ECO:0000269|PubMed:10764783, ECO:0000269|PubMed:10908715}.
|
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; Evidence={ECO:0000269|PubMed:10764783, ECO:0000269|PubMed:10908715};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 uM for farnesyl diphosphate (FPP); KM=3.62 uM for geranylgeranyl diphosphate (GGPP); KM=23 uM for isopentenyl diphosphate (IPP);
|
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein. {ECO:0000269|PubMed:10764783, ECO:0000269|PubMed:10908715}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80460
|
PCEP3_ARATH
|
MATINVYVFAFIFLLTISVGSIEGRKLTKFTVTTSEEIRAGGSVLSSSPPTEPLESPPSHGVDTFRPTEPGHSPGIGHSVHN
| null | null |
cellular response to nitrogen starvation [GO:0006995]; nitrate import [GO:1902025]; regulation of lateral root development [GO:2000023]; regulation of leaf morphogenesis [GO:1901371]; regulation of root development [GO:2000280]; regulation of shoot system development [GO:0048831]; response to auxin [GO:0009733]; response to carbon dioxide [GO:0010037]; response to light intensity [GO:0009642]; response to nitrate starvation [GO:0090548]; response to nitrogen compound [GO:1901698]; response to osmotic stress [GO:0006970]; response to potassium ion [GO:0035864]; response to salt stress [GO:0009651]; response to sucrose [GO:0009744]; response to temperature stimulus [GO:0009266]; root development [GO:0048364]
|
apoplast [GO:0048046]
|
hormone activity [GO:0005179]
| null | null |
C-terminally encoded plant signaling peptide (CEP) family
|
PTM: The mature small signaling peptide is generated by proteolytic processing of the longer precursor. {ECO:0000269|PubMed:25324386}.
|
SUBCELLULAR LOCATION: [C-terminally encoded peptide 3]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.
| null | null | null | null | null |
FUNCTION: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Promotes shoot growth. Modulates leaf morphology (PubMed:24179096). Regulates systemic nitrogen (N)-demand signaling. Mediates systemic up-regulation of genes involved in N uptake and assimilation pathways (PubMed:25324386). {ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80462
|
XLG1_ARATH
|
MPLKEDDCCLFAEEYDGPPLSYNIPCAVPINVEKIPVAAVVSPVCISDNMSFPVIQPILSVESKKFLIDSVSPTSVIANCGSNQLELVSDSITVSPTSVIEHTEEEEEEEGGDGEDCELSSSGELLLRSCSVKESLDLNESSSNPLVPDWESNESVLSMDYPSSRVTGDCVSETNGDGKKQPVVTFLGIASDDGFEEEESCSNLRRVRVVPVKKQPQTKGKKGSCYRCFKGSRFTEKEVCLVCDAKYCNSCVLRAMGSMPEGRKCVTCIGFPIDESKRGSLGKCSRMLKRLLNDLEVKQIMKTERFCEANQLPAEYVYVNGQPLYPEELVTLQTCSNPPKKLKPGDYWYDKVSGLWGKEGEKPYQIISPHLNVGGPISPEASNGNTQVFINGREITKVELRMLQLAGVQCAGNPHFWVNEDGSYQEEGQKNTKGYIWGKAGTKLLCAVLSLPVPSKSTANASGEQLYSANSRSILDHLEHRTLQKILLVGNSGSGTSTIFKQAKILYKDVPFLEDERENIKVIIQTNVYGYLGMLLEGRERFEEEALALRNTKQCVLENIPADEGDAKSNDKTVTMYSIGPRLKAFSDWLLKTMAAGNLGVIFPAASREYAPLVEELWRDAAIQATYKRRSELGLLPSVASYFLERAIDVLTPDYEPSDLDILYAEGVTSSSGLACLDFSFPQTASEENLDPSDHHDSLLRYQLIRVPSRGLGENCKWIDMFEDVGMVVFVVSMSDYDQVSEDGTNKMLLTKKLFESIITHPIFENMDFLLILNKYDLLEEKVERVPLARCEWFQDFNPVVSRHRGSNNGNPTLGQLAFHFMAVKFKRFYSSLTGKKLFVSSSKSLDPNSVDSSLKLAMEILKWSEERTNICMSEYSMYSTEPSSFSN
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:22232549};
|
G protein-coupled receptor signaling pathway [GO:0007186]
|
nucleus [GO:0005634]
|
G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, XLG subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17999646}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation. {ECO:0000250, ECO:0000269|PubMed:17999646}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80467
|
SDT_ARATH
|
MPIHIGSSIPLMVEKMLTEMVKPSKHIPQQTLNLSTLDNDPYNEVIYKACYVFKAKNVADDDNRPEALLREALSDLLGYYYPLSGSLKRQESDRKLQLSCGGDGGGVPFTVATANVELSSLKNLENIDSDTALNFLPVLHVDIDGYRPFALQVTKFECGGFILGMAMSHAMCDGYGEGHIMCALTDLAGGKKKPMVTPIWERERLVGKPEDDQPPFVPGDDTAASPYLPTDDWVTEKITIRADSIRRLKEATLKEYDFSNETITTFEVIGAYLWKSRVKALNLDRDGVTVLGLSVGIRNVVDPPLPDGYYGNAYIDMYVPLTAREVEEFTISDIVKLIKEAKRNAHDKDYLQEELANTEKIIKMNLTIKGKKDGLFCLTDWRNIGIFGSMDFGWDEPVNIVPVVPSETARTVNMFMRPSRLESDMVGGVQIVVTLPRIAMVKFKEEMEALE
|
2.3.1.248
| null |
polyamine biosynthetic process [GO:0006596]; spermidine metabolic process [GO:0008216]
| null |
sinapoyl spermidine:sinapoyl CoA N-acyltransferase activity [GO:0080089]; spermidine:sinapoyl CoA N-acyltransferase activity [GO:0080072]
|
PF02458;
|
3.30.559.10;
|
Plant acyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 (E)-sinapoyl-CoA + spermidine = 2 CoA + 2 H(+) + N(1),N(8)-bis[(E)-sinapoyl]-spermidine; Xref=Rhea:RHEA:45168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57834, ChEBI:CHEBI:85006; EC=2.3.1.248; Evidence={ECO:0000269|PubMed:19168716};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.3 uM for sinapoyl-CoA (with spermidine as the acyl acceptor, at 30 degrees Celsius) {ECO:0000269|PubMed:19168716}; KM=37.4 uM for spermidine (with sinapoyl-CoA as the acyl donor, at 30 degrees Celsius) {ECO:0000269|PubMed:19168716}; KM=236.9 uM for putrescine (with sinapoyl-CoA as the acyl donor, at 30 degrees Celsius) {ECO:0000269|PubMed:19168716}; KM=34.6 uM for disinapoyl-spermidine (with CoA as cosubstrate, at 30 degrees Celsius) {ECO:0000269|PubMed:19168716}; KM=83.6 uM for CoA (with disinapoyl-spermidine as cosubstrate, at 30 degrees Celsius) {ECO:0000269|PubMed:19168716}; Note=kcat is 5.1 sec(-1) with sinapoyl-CoA as substrate (in the presence of spermidine as the acyl acceptor). kcat is 5.6 sec(-1) with spermidine as substrate (in the presence of sinapoyl-CoA as the acyl donor). kcat is 0.3 sec(-1) with putrescine as substrate (in the presence of sinapoyl-CoA as the acyl donor). kcat is 37.8 sec(-1) with disinapoyl-spermidine as substrate (in the presence of CoA as cosubstrate). kcat is 39.6 sec(-1) with CoA as substrate (in the presence of disinapoyl-spermidine as cosubstrate). All analyses are done at 30 degrees Celsius. {ECO:0000269|PubMed:19168716};
|
PATHWAY: Amine and polyamine metabolism; spermidine metabolism. {ECO:0000269|PubMed:19168716}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 using spermidine and sinapoyl-CoA as substrates. {ECO:0000269|PubMed:19168716};
| null |
FUNCTION: Spermidine sinapoyl-CoA acyltransferase that mediates the accumulation of disinapoyl spermidine conjugates in seeds (PubMed:19168716). Catalyzes the two conjugating steps required for the biosynthesis of N1,N8-disipanoyl-spermidine (PubMed:19168716, PubMed:33519864). Can also use putrescine as an acyl acceptor to convert it into monosinapoyl-putrescine (PubMed:19168716). {ECO:0000269|PubMed:19168716, ECO:0000269|PubMed:33519864}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80472
|
MES7_ARATH
|
MDKNNQKKFVLVHGICHGAWCWYKVKAQLEAAGHSVTAVDLAASGVNMTSLDEIQTLKDYCKPLLEFLSSLGSDDDKVILVAHSMGGISASLAADIFPSKVAAIVFVAAFMPDISNPPAYVFQKLVKDVTQEVWMDTVFGKPDRPLEFALFGPEFMAKYLYNLSPLQDFELAKMSVRVSPFMTNNLAGTISFSEDRYGSVTRIYIVCGEDVAVPVDYQRGMINDFPVKEVLEIKDADHMPMFSKPQELCALLLEIADKYA
|
3.1.1.-
| null |
defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; jasmonic acid metabolic process [GO:0009694]; salicylic acid metabolic process [GO:0009696]; systemic acquired resistance [GO:0009627]
| null |
hydrolase activity, acting on ester bonds [GO:0016788]; methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031]
|
PF12697;
|
3.40.50.1820;
|
AB hydrolase superfamily, Methylesterase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + methyl (indol-3-yl)acetate = (indol-3-yl)acetate + H(+) + methanol; Xref=Rhea:RHEA:32919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30854, ChEBI:CHEBI:72782; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32920; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate; Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612; Evidence={ECO:0000269|PubMed:18467465};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=12.82 nmol/min/ug enzyme with methyl salicylate (MeSA) as substrate {ECO:0000269|PubMed:18643994};
|
PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.
| null | null |
FUNCTION: Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl salicylate (MeSA) esterase activity in vitro. Required to convert methyl salicylate (MeSA) to salicylic acid (SA) as part of the signal transduction pathways that activate systemic acquired resistance in systemic tissue. MeSA is believed to be an inactive form that needs to be demethylated to exert a biological effect. {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:18643994}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80476
|
MES2_ARATH
|
MSEEKRKQHFVLVHGACHGAWCWYKVKPLLEALGHRVTALDLAASGIDTTRSITDISTCEQYSEPLMQLMTSLPNDEKVVLVGHSFGGLSLALAMDKFPDKISVSVFVTAFMPDTKHSPSFVEEKFASSMTPEGWMGSELETYGSDNSGLSVFFSTDFMKHRLYQLSPVEDLELGLLLKRPSSLFINELSKMENFSEKGYGSVPRAYIVCKEDNIISEDHQRWMIHNYPANLVIEMEETDHMPMFCKPQLLSDHLLAIADNFC
|
3.1.1.-
| null |
jasmonic acid metabolic process [GO:0009694]; nicotinate metabolic process [GO:1901847]; oxylipin biosynthetic process [GO:0031408]; salicylic acid metabolic process [GO:0009696]
|
cytosol [GO:0005829]; vacuole [GO:0005773]
|
carboxylic ester hydrolase activity [GO:0052689]; hydrolase activity, acting on ester bonds [GO:0016788]; methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031]
|
PF12697;
|
3.40.50.1820;
|
AB hydrolase superfamily, Methylesterase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + methyl (indol-3-yl)acetate = (indol-3-yl)acetate + H(+) + methanol; Xref=Rhea:RHEA:32919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30854, ChEBI:CHEBI:72782; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32920; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol; Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373; Evidence={ECO:0000269|PubMed:18467465}; CATALYTIC ACTIVITY: Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate; Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832; Evidence={ECO:0000269|PubMed:18467465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612; Evidence={ECO:0000269|PubMed:18467465};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=1.77 nmol/min/ug enzyme with methyl salicylate (MeSA) as substrate {ECO:0000269|PubMed:18643994};
|
PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.; PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:18467465}.
| null | null |
FUNCTION: Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro. {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:18643994}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80501
|
RAH1B_ARATH
|
MAPVSALAKYKLVFLGDQSVGKTSIITRFMYDKFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAVIVYDVASRQSFLNTTKWIDEVRTERGSDVIVVLVGNKTDLVDKRQVSIEEAEAKARELNVMFIETSAKAGFNIKALFRKIAAALPGMETLSSTKQEDMVDVNLKSSNANASLAQQQSGGCSC
| null | null |
exocytosis [GO:0006887]; plant-type cell wall cellulose biosynthetic process [GO:0052324]; protein transport [GO:0015031]; regulation of cell growth [GO:0001558]
|
cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; trans-Golgi network [GO:0005802]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:19454595}; Lipid-anchor {ECO:0000305|PubMed:19454595}. Cytoplasm, cytosol {ECO:0000269|PubMed:19454595}.
| null | null | null | null | null |
FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Binds GTP and GDP and possesses intrinsic GTPase activity (By similarity). {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80507
|
CSK2E_ARATH
|
MYKDRSGGGIMGGGGSSRSEILGGAIDRKRINDALDKHLKKSSPSTSRVFTSKDKDSVPSTSTAKSQLHSRSPDVESDTDSEGSDVSGSEGDDTSWISWFCNLRGNEFFCEVDEDYIQDDFNLCGLSGQVPYYDYALDLILDVESSNGDMFTEEQHEMVESAAEMLYGLIHVRYILTTKGMAAMMEKYKNYDFGRCPRVFCCGQSCLPVGQSDIPRSSTVKIYCPKCEDIYYPRSKYQGNIDGAYFGTTFPHLFLMAYGNMKPQKPAQNYVPKIFGFKVHNKQ
| null | null |
circadian rhythm [GO:0007623]; photoperiodism, flowering [GO:0048573]; positive regulation of circadian rhythm [GO:0042753]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]
|
protein kinase regulator activity [GO:0019887]; protein serine/threonine kinase activity [GO:0004674]
|
PF01214;
|
2.20.25.20;1.10.1820.10;
|
Casein kinase 2 subunit beta family
|
PTM: Phosphorylated by alpha subunit. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}.
| null | null | null | null | null |
FUNCTION: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis (PubMed:21330376). CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation (PubMed:19509278). {ECO:0000269|PubMed:19509278, ECO:0000269|PubMed:21330376}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80528
|
HASP_ARATH
|
MGQRVDLWSEVIKSEEEDGDIPKIEAVFQRRKKPDKSSEAVNFGWLVKGARTSSVNGPKRDSWARSLSTRGRESIAVRAYVNNQPQKKAAGRKKPPIPKGKVVKAPDFQKEKEYFRDIDAFELLEESPSPNKSSTWTMGEQVVPEMPHLSTRLEKWLISKKLNHTCGPSSTLSKILENSAIHQESVCDNDAFDSLSLKTPDKSSAGNTSVFRLIPSCDENLAAEDVPVRKIKMESIDLEDELKRLSLTSDLIPTHQDFDQPILDLLSACGQMRPSNFIEAFSKFCEPESIVKIGEGTYGEAFRAGSSVCKIVPIDGDFRVNGEVQKRADELLEEVILSWTLNQLRECETTAQNLCPTYIKTQDIKLCQGPYDPILIKAWEEWDAKHGSENDHPDFPEKQCYVMFVLEHGGKDLESFVLLNFDEARSLLVQATAGLAVAEAAFEFEHRDLHWGNILLSRNNSDTLPFILEGKQVCIKTFGVQISIIDFTLSRINTGEKILFLDLTSDPYLFKGPKGDKQSETYRKMKAVTEDYWEGSFARTNVLWLIYLVDILLTKKSFERSSKHERELRSLKKRMEKYESAKEAVSDPFFSDMLMDQIS
|
2.7.11.1
| null |
intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; phosphorylation [GO:0016310]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; phragmoplast [GO:0009524]
|
ATP binding [GO:0005524]; histone H3T11 kinase activity [GO:0035402]; histone H3T3 kinase activity [GO:0072354]; protein serine kinase activity [GO:0106310]
|
PF12330;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Haspin subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21527018}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21527018}. Nucleus {ECO:0000269|PubMed:21527018}. Chromosome {ECO:0000269|PubMed:21527018}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21527018}. Note=During interphase, localized in the cytoplasm and at the nuclear periphery. During prometaphase and metaphase, localized on chromosomes, and around the cell plate during cytokinesis. {ECO:0000269|PubMed:21527018}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph) and 'Thr-11' (H3T11ph), but not at 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Plays a role in mitotic cell division during plant growth (PubMed:21527018). Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph), but not at 'Thr-11' (H3T11ph), 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Involved in histone H3 phosphorylation in mitotic cells. Contributes to organ and plant development, as well as embryonic patterning (PubMed:21749502). {ECO:0000269|PubMed:21527018, ECO:0000269|PubMed:21749502}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80536
|
PIF3_ARATH
|
MPLFELFRLTKAKLESAQDRNPSPPVDEVVELVWENGQISTQSQSSRSRNIPPPQANSSRAREIGNGSKTTMVDEIPMSVPSLMTGLSQDDDFVPWLNHHPSLDGYCSDFLRDVSSPVTVNEQESDMAVNQTAFPLFQRRKDGNESAPAASSSQYNGFQSHSLYGSDRARDLPSQQTNPDRFTQTQEPLITSNKPSLVNFSHFLRPATFAKTTNNNLHDTKEKSPQSPPNVFQTRVLGAKDSEDKVLNESVASATPKDNQKACLISEDSCRKDQESEKAVVCSSVGSGNSLDGPSESPSLSLKRKHSNIQDIDCHSEDVEEESGDGRKEAGPSRTGLGSKRSRSAEVHNLSERRRRDRINEKMRALQELIPNCNKVDKASMLDEAIEYLKSLQLQVQIMSMASGYYLPPAVMFPPGMGHYPAAAAAMAMGMGMPYAMGLPDLSRGGSSVNHGPQFQVSGMQQQPVAMGIPRVSGGGIFAGSSTIGNGSTRDLSGSKDQTTTNNNSNLKPIKRKQGSSDQFCGSS
| null | null |
de-etiolation [GO:0009704]; gibberellic acid mediated signaling pathway [GO:0009740]; positive regulation of anthocyanin metabolic process [GO:0031539]; red or far-red light signaling pathway [GO:0010017]; red, far-red light phototransduction [GO:0009585]; regulation of DNA-templated transcription [GO:0006355]; regulation of photosynthesis, light reaction [GO:0042548]; regulation of plant organ morphogenesis [GO:1905421]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to cold [GO:0009409]; response to ethylene [GO:0009723]; response to heat [GO:0009408]; response to red or far red light [GO:0009639]; response to salt [GO:1902074]; response to water-immersion restraint stress [GO:1990785]; unidimensional cell growth [GO:0009826]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00010;
|
4.10.280.10;
| null |
PTM: Phosphorylated by PHYA; this phosphorylation is repressed by PIA2. {ECO:0000269|PubMed:27143545}.; PTM: Dephosphorylated by TOPP4 during photomorphogenesis, leading to subsequent degradation of PIF3 by the proteasomal pathway. {ECO:0000269|PubMed:26704640}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23548744}.
| null | null | null | null | null |
FUNCTION: Transcription factor acting in the phytochrome signaling pathway (PubMed:10466729, PubMed:14508006). Activates transcription by binding to the G box (5'-CACGTG-3'), particularly in the dark but barely in far-red light (PubMed:10797009, PubMed:31732705). Acts as a negative regulator of phytochrome B signaling (PubMed:14508006). Represses chlorophyll biosynthesis and photosynthesis in the dark (PubMed:23548744). Recruits the histone deacetylase HDA15 to the promoters of chlorophyll biosynthetic and photosynthetic genes (PubMed:23548744). HDA15 represses their transcription by histone deacetylation (PubMed:23548744). Promotes the expression of MDP60 to modulate hypocotyl cell elongation in response to light and ethylene signaling (PubMed:29167353). Required for submergence-induced and ethylene-dependent underwater hypocotyl elongation (PubMed:31638649). {ECO:0000269|PubMed:10466729, ECO:0000269|PubMed:10797009, ECO:0000269|PubMed:14508006, ECO:0000269|PubMed:23548744, ECO:0000269|PubMed:29167353, ECO:0000269|PubMed:31638649, ECO:0000269|PubMed:31732705}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80548
|
MRF2_ARATH
|
MEHQDLTDSRKDPLCISQLKISSSSLDPLPQANMAEDLTKSRRHSPIKVEGSEETWGVEDDDDLTDPIFDTIEGNGHSDPTSCFDADLSEYKKKATVIVEEYFGTNDVVSVVNELKELGMAEYRYYFVKKLVSMAMDRHDKEKEMAAFLLSTLYADVIDPPEVYRGFNKLVASADDLSVDIPDAVDVLAVFVARAIVDDILPPAFLKKQMKLLPDNSKGVEVLRKAEKSYLATPLHAEVVEKRWGGTDNWTAEDVKARINDLLKEYVMSGDKKEAFRCIKGLKVPFFHHEIVKRALIMAMERRKAQVRLLDLLKETIEVGLINSTQVTKGFSRIIDSIEDLSLDIPDARRILQSFISKAASEGWLCASSLKSLSADAGEKLLENSSANVFKDKAKSIIREYFLSGDTSEVVHCLDTELNASSSQLRAIFVKYLITLAMDRKKREKEMACVLVSTLGFPPKDVRSAFSMLIESADDTALDNPVVVEDLAMFLARAVVDEVLAPRDLEEVLNQTPEAGSSVGEKVIQMAKTLLKARLSGERILRCWGGGGIETNSPGSTVKEVKEKIQILLEEYVSGGDLREASRCVKELGMPFFHHEVVKKSVVRIIEEKENEERLWKLLKVCFDSGLVTIYQMTKGFKRVDESLEDLSLDVPDAAKKFSSCVERGKLEGFLDESFASEDSQSKKQNGSSSSSG
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; regulation of translation [GO:0006417]; response to absence of light [GO:0009646]; response to carbon starvation [GO:0090549]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
ribosome binding [GO:0043022]
|
PF02847;
|
1.25.40.180;
|
PDCD4 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytosol {ECO:0000269|PubMed:29084871}.
| null | null | null | null | null |
FUNCTION: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions. {ECO:0000269|PubMed:29084871}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80560
|
IP5PC_ARATH
|
MDIINNNHRDENDDDEEEALSAMSSVPPPRKIHSYSHQLRATGQKGHHRQRQHSLDDIPKITEIVSGCGISGDSSDDEFYPYATTTNSSSFPFTGGDTGDSDDYLHQPEIGEDFQPLPEFVGSGGGVGMFKVPTRSPLHSARPPCLELRPHPLKETQVGRFLRNIACTETQLWAGQESGVRFWNFDDAFEPGCGLSGRVQRGDEDAAPFQESASTSPTTCLMVDNGNRLVWSGHKDGKIRSWKMDYVLDDGDDSPFKEGLAWQAHKGPVNSVIMSSYGDLWSCSEGGVIKIWTWESMEKSLSLRLEEKHMAALLVERSGIDLRAQVTVNGTCNISSSEVKCLLADNVRSKVWAAQLQTFSLWDGRTKELLKVFNSEGQTENRVDMPLGQDQPAAEDEMKAKIASTSKKEKPHGFLQRSRNAIMGAADAVRRVATRGGGAYEDAKRTEAMVLAGDGMIWTGCTNGLLIQWDGNGNRLQDFRHHQCAVLCFCTFGERIYIGYVSGHIQIIDLEGNLIAGWVAHNNAVIKMAAADGYIFSLATHGGIRGWPVISPGPLDGIIRSELAEKERTYAQTDSVRILTGSWNVGQGKASHDALMSWLGSVASDVGILVVGLQEVEMGAGFLAMSAAKESVGGNEGSTIGQYWIDTIGKTLDEKAVFERMGSRQLAGLLISLWVRKNLRTHVGDIDVAAVPCGFGRAIGNKGGVGLRIRVFDRIMCFINCHLAAHLEAVNRRNADFDHIYKTMSFTRSSNAHNAPAAGVSTGSHTTKSANNANVNTEETKQDLAEADMVVFFGDFNYRLFGISYDEARDFVSQRSFDWLREKDQLRAEMKAGRVFQGMREAIITFPPTYKFERHRPGLGGYDSGEKKRIPAWCDRVIFRDTRTSPESECSLDCPVVASIMLYDACMDVTESDHKPVRCKFHVKIEHVDRSVRRQEFGRIIKTNEKVRALLNDLRYVPETIVSSNSIVLQNQDTFVLRITNKCVKENAVFRILCEGQSTVREDEDTLELHPLGSFGFPRWLEVMPAAGTIKPDSSVEVSVHHEEFHTLEEFVDGIPQNWWCEDTRDKEAILVVNVQGGCSTETVCHRVHVRHCFSAKNLRIDSNPSNSKSQSLKKNEGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSNSKSSKKSDGDSCSKSQKKSDGDTNSKSQKKGDGDSSSKSHKKNDGDSSSKSHKKNDGDSSSKSHKKSDGDSSSKSHKKSEGDSSSKSHKKNDGDSSSSYKSQSGKKNSNSSTVEESRNNHNKR
|
3.1.3.56
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15574849};
|
phosphatidylinositol dephosphorylation [GO:0046856]; pollen germination [GO:0009846]
| null |
inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; metal ion binding [GO:0046872]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]
| null |
3.60.10.10;2.130.10.10;
|
Inositol polyphosphate 5-phosphatase family
| null | null |
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:203600; EC=3.1.3.56; Evidence={ECO:0000269|PubMed:15574849};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=223 uM for Ins(1,4,5)P3 {ECO:0000269|PubMed:15574849};
| null | null | null |
FUNCTION: Has phosphatase activity toward Ins(1,4,5)P3 (PubMed:15574849). Controls Ins(1,4,5)P3/Ca(2+) levels that is crucial for maintaining pollen dormancy and regulating early germination of pollen (PubMed:22573619). {ECO:0000269|PubMed:15574849, ECO:0000269|PubMed:22573619}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80562
|
HOL2_ARATH
|
MAEEQQNSSYSIGGNILPTPEEAATFQPQVVAEGGWDKCWEDGVTPWDQGRATPLILHLLDSSALPLGRTLVPGCGGGHDVVAMASPERFVVGLDISDKALNKANETYGSSPKAEYFSFVKEDVFTWRPNELFDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGELITLMYPMTDHEGGAPYKVALSSYEDVLVPVGFKAVSVEENPDSIPTRKGKEKLARWKKIN
|
2.1.1.9
| null |
methylation [GO:0032259]
|
cytosol [GO:0005829]
|
thiol S-methyltransferase activity [GO:0018708]
|
PF05724;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, TPMT family
| null | null |
CATALYTIC ACTIVITY: Reaction=a thiol + S-adenosyl-L-methionine = a methyl thioether + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18277, ChEBI:CHEBI:15378, ChEBI:CHEBI:29256, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:86315; EC=2.1.1.9; Evidence={ECO:0000269|PubMed:19419967};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for KSCN {ECO:0000269|PubMed:19419967}; KM=36 mM for KCL {ECO:0000269|PubMed:19419967}; KM=1.1 mM for ammonium sulfide {ECO:0000269|PubMed:19419967}; KM=49 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19419967}; Vmax=260 nmol/sec/mg enzyme toward KSCN {ECO:0000269|PubMed:19419967}; Vmax=200 nmol/sec/mg enzyme toward KCL {ECO:0000269|PubMed:19419967}; Vmax=520 nmol/sec/mg enzyme toward ammonium sulfide {ECO:0000269|PubMed:19419967}; Vmax=200 nmol/sec/mg enzyme toward S-adenosyl-L-methionine {ECO:0000269|PubMed:19419967};
| null | null | null |
FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase. Involved in glucosinolate metabolism and defense against phytopathogens (By similarity). {ECO:0000250, ECO:0000269|Ref.5}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80565
|
OEP37_ARATH
|
MADPSSQNPNLATPPPPSSPSPTHQIQSGTSELSPPSRPPCSTLSFLKTANRPKLRVTSEFDSDSLLFLNKVSCKLFDNLAKLKLSFQNNSQREISQPQVSFTSKHVSVLYDVEEKNTFIKSTLDVHPRLQLRALHNVKAQQGEVAMEANLTEPGYSLELSSPVPIGYPRATLKFPLGEISLQEKDEEEEEKQKRTLSVNGILKRQVMNGVCTALYTDEELRLRYAYKDDALSFIPSISLPSNAASFAFKRRFSPSDKLSYWYNFDSNMWSAVYKRTYGKDYKLKAGYDSDVRLGWASLWVGDEAGKVKTTPMKMKVQFMLQVPQDDIKSSVLMFRVKKRWDI
| null | null |
monoatomic cation transport [GO:0006812]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; chloroplast outer membrane [GO:0009707]; cytosol [GO:0005829]; plastid [GO:0009536]; pore complex [GO:0046930]
|
identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; porin activity [GO:0015288]
| null | null |
Plastid outer envelope porin OEP37 (TC 1.B.47) family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:16624824}; Multi-pass membrane protein {ECO:0000269|PubMed:16624824}.
| null | null | null | null | null |
FUNCTION: Voltage-dependent peptide-sensitive high conductance rectifying cation channel with a strong affinity for TIC32 that is imported into the chloroplast. Conductance is pH-dependent decreasing with decreasing pH values. {ECO:0000269|PubMed:16624824}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80568
|
ITPK4_ARATH
|
MKGVLLDESVLFSPESEDSSPSLRESVPSLLRLLRYSMIRTGISYGLDLPENKVDLLRKTAAEYSINCLPLETSLTSVTFGDTLKAWYSDGSILYVASSRKEEILRELSPSQLVVLLDVEGDSLEDPNIIHIHSLEELPMTICCINKKAMGDGAAIVAYIMKPSRVEDFAKRGALPMYPTSCGLIFLPLMFEFPLASQLKHADIIFHKATDEILSIELNCSDSKSSVAVTFSTGMEKLKKYMEDQNACAIVDPIRNIYPVVDRLKMQHILLGLEGLGAAGRKIRGACFLKIDSYDEPDLAQNLSRAGLSLPCIVKPQVACGVADAHSMAIVFRVEDFKNLNTPVPAIIQEYVDHSSRIFKFYVLGETIFHAVKKSIPSSSSLRKSAEENGLKPILFDSLKSLPVDSANQNPVSEIDLELVTEAATWLRKKLDLTIFGFDVVIQEGTGDHVIVDLNYLPSFKEVPDNIAVPAFWEAIRNRFDQHVQEKH
|
2.7.1.159
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572};
|
inositol trisphosphate metabolic process [GO:0032957]; myo-inositol hexakisphosphate biosynthetic process [GO:0010264]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; magnesium ion binding [GO:0000287]
|
PF05770;
|
3.30.470.20;
|
ITPK1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:17698066}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:17698066};
| null | null | null | null |
FUNCTION: Kinase that can phosphorylate the inositol polyphosphate Ins(1,3,4)P3 to form InsP4. Also phosphorylates a racemic mixture of Ins(1,4,6)P3 and Ins(3,4,6)P3 to form InsP4. Does not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity, but possesses inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity (PubMed:17698066). Ins(1,3,4,6)P4 is an essential molecule in the hexakisphosphate (InsP6) pathway (By similarity). {ECO:0000250|UniProtKB:Q13572, ECO:0000269|PubMed:17698066}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80575
|
RISB_ARATH
|
MKSLASPPCLRLIPTAHRQLNSRQSSSACYIHGGSSVNKSNNLSFSSSTSGFASPLAVEKELRSSFVQTAAVRHVTGSLIRGEGLRFAIVVARFNEVVTKLLLEGAIETFKKYSVREEDIEVIWVPGSFEIGVVAQNLGKSGKFHAVLCIGAVIRGDTTHYDAVANSAASGVLSASINSGVPCIFGVLTCEDMDQALNRSGGKAGNKGAETALTALEMASLFEHHLK
|
2.5.1.78
| null |
riboflavin biosynthetic process [GO:0009231]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; riboflavin synthase complex [GO:0009349]
|
6,7-dimethyl-8-ribityllumazine synthase activity [GO:0000906]; identical protein binding [GO:0042802]
|
PF00885;
|
3.40.50.960;
|
DMRL synthase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
| null |
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
| null | null |
FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin (By similarity). {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80588
|
EDE1_ARATH
|
MEARIGRSMEHPSTPAINAPAPVPPPSTRRPRVREVSSRFMSPISSSSSSSSSSSAGDLHQLTSNSPRHHHQHQNQRSTSAQRMRRQLKMQEGDENRPSETARSLDSPFPLQQVDGGKNPKQHIRSKPLKENGHRLDTPTTAMLPPPSRSRLNQQRLLTASAATRLLRSSGISLSSSTDGEEDNNNREIFKSNGPDLLPTIRTQAKAFNTPTASPLSRSLSSDDASMFRDVRASLSLKNGVGLSLPPVAPNSKIQADTKKQKKALGQQADVHSLKLLHNRYLQWRFANANAEVKTQSQKAQAERMFYSLGLKMSELSDSVQRKRIELQHLQRVKAVTEIVESQTPSLEQWAVLEDEFSTSLLETTEALLNASLRLPLDSKIKVETKELAEALVVASKSMEGIVQNIGNLVPKTQEMETLMSELARVSGIEKASVEDCRVALLKTHSSQMEECYLRSQLIQHQKKCHQQECTTSV
| null | null |
cell division [GO:0051301]; endosperm cellularization [GO:0010342]; endosperm development [GO:0009960]; microtubule cytoskeleton organization [GO:0000226]; seed development [GO:0048316]; spindle assembly [GO:0051225]
|
cytoplasm [GO:0005737]; nuclear microtubule [GO:0005880]; nucleus [GO:0005634]
|
microtubule binding [GO:0008017]
|
PF04484;
| null |
QWRF family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:21558460}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19151224}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19151224}. Note=Microtubule-associated.
| null | null | null | null | null |
FUNCTION: Microtubule-associated protein required for seed development and for microtubule function in the endosperm. Associates with nuclear microtubules during mitosis. Binds to microtubules of the spindle and spindle-poles and to midzone microtubules out of which the phragmoplast emerges. Not associated with cortical microtubules. Required for endosperm cellularization. May be bound and sequestered by GRF5 in an inactive soluble form during the early stages of mitosis. {ECO:0000269|PubMed:19151224, ECO:0000269|PubMed:22535409}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O80605
|
SUC3_ARATH
|
MSDSVSISVPYRNLRKEIELETVTKHRQNESGSSSFSESASPSNHSDSADGESVSKNCSLVTLVLSCTVAAGVQFGWALQLSLLTPYIQTLGISHAFSSFIWLCGPITGLVVQPFVGIWSDKCTSKYGRRRPFILVGSFMISIAVIIIGFSADIGYLLGDSKEHCSTFKGTRTRAAVVFIIGFWLLDLANNTVQGPARALLADLSGPDQRNTANAVFCLWMAIGNILGFSAGASGKWQEWFPFLTSRACCAACGNLKAAFLLAVVFLTICTLVTIYFAKEIPFTSNKPTRIQDSAPLLDDLQSKGLEHSKLNNGTANGIKYERVERDTDEQFGNSENEHQDETYVDGPGSVLVNLLTSLRHLPPAMHSVLIVMALTWLSWFPFFLFDTDWMGREVYHGDPTGDSLHMELYDQGVREGALGLLLNSVVLGISSFLIEPMCQRMGARVVWALSNFTVFACMAGTAVISLMSLSDDKNGIEYIMRGNETTRTAAVIVFALLGFPLAITYSVPFSVTAEVTADSGGGQGLAIGVLNLAIVIPQMIVSLGAGPWDQLFGGGNLPAFVLASVAAFAAGVIALQRLPTLSSSFKSTGFHIG
| null | null |
response to wounding [GO:0009611]; sucrose metabolic process [GO:0005985]; sucrose transport [GO:0015770]
|
Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; pollen tube [GO:0090406]
|
sucrose transmembrane transporter activity [GO:0008515]; sucrose:proton symporter activity [GO:0008506]
|
PF07690;
|
1.20.1250.20;
|
Glycoside-pentoside-hexuronide (GPH) cation symporter transporter (TC 2.A.2.4) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + sucrose(out) = H(+)(in) + sucrose(in); Xref=Rhea:RHEA:72187, ChEBI:CHEBI:15378, ChEBI:CHEBI:17992; Evidence={ECO:0000269|PubMed:11135120}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72188; Evidence={ECO:0000269|PubMed:11135120};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for sucrose {ECO:0000269|PubMed:11135120}; KM=1.6 mM for maltose {ECO:0000269|PubMed:11135120};
|
PATHWAY: Glycan biosynthesis; sucrose metabolism.
| null | null |
FUNCTION: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport maltose at a lesser rate. May also transport biotin. Probably involved in carpel maturation that leads to pod shatter and seed dispersal. {ECO:0000269|PubMed:11135120}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.