entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
A4IHB9
|
SL9B2_XENTR
|
Sodium/hydrogen exchanger 9B2 (Na(+)/H(+) exchanger NHA2) (Na(+)/H(+) exchanger-like domain-containing protein 2) (NHE domain-containing protein 2) (Sodium/hydrogen exchanger-like domain-containing protein 2) (Solute carrier family 9 subfamily B member 2)
|
MEDSLFSVDKAGPGKDASAASADCNHMVAEDGIITEQHKEIPLVALKVPDGHAPIDECELLNSDDQLPKGSQNQTNICMRIRAFACPPQGCFSLAITNVTMVILIWAVVWSITGPECLPGGNLFGILALLFSAALGGKLISLIKIPSLPPLPPLLGMLLAGFLIRNIPVITDQVQIHHKWSAALRNIALAIILVRAGLGLDPKALRKLKAVCLRLSFGPCVVESCTAAVVSHFIMGFPLTWGFMLGFVLGAVSPAVVVPSMLILQKEGFGVDKGIPTLLMAAGSFDDVLAITGFNTCLGMAFSSGSTLNTIVRGVLEVVVGIAAGLLFGFFLHYFPSKDQENLKGKRSYLILALSVFAVFGSLYFGFPGSGGLCTLVMAFLAGIGWSTDKTVVEDIIAVSWDIFQPLLFGLIGAEISVASLKPETVGLCTATLIIALIIRICISFLMVCFSGFSLKEKIFISLAWMPKATVQAAIGSVALDTARTLENKQFEDYGMDVLTVAFLGILVTAPIGALVIGLTGPKMLEKSESRTVTEEGSV
|
Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (By similarity). Uses the proton gradient/membrane potential to extrude sodium (By similarity). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity). Also able to mediate Na(+)/Li(+) antiporter activity in kidney (By similarity).
|
A4IID1
|
MGT4A_XENTR
|
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa) (GlcNAc-T IVa) (GnT-IVa) (N-acetylglucosaminyltransferase IVa) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa) [Cleaved into: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]
|
MRLRNGTVATALVFITTFLSLSWYTAWQNGKEKLMAYQREFHALKERLRIAEHRTLQRSSELHAILDHFRRMIKEANGSRDALNHFSDETQKLIKDLTNRKALQVPNIYYHMPHLLNHDGSLQPAVQVGLGRTGVSVVMGIPTVKRRVKSYLKETLHSLIDKLSPEEKLDCVIIVFVGETDLEYVNSVVASLQKEFATEISSGLVEVISPPATYYPDLNNLKETFGDSKERVRWRTKQNLDYCFLMMYAQRKGIYYIQLEDDIVAKQNYFSTIKNFALQLSSEDWMILEFSQLGFIGKMFQAPDITLIVEFILMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKSNLRIRFRPSLFQHVGLHSSLAGKIQKLTDKDFLKPLLHKIHVNPPAEVSTSLKVYQGHTLEKTYLGEDFFWAITPVAGDYILFKFDKPVNVERYLFRSGNPEHPGDQLWNTTVEVLPYRKDIVELRSDTKDKRLSDGFFRIGKFEDGLAEGPVNSYLNPISALRLSVLQNSAVWVILNEIHIKRNPAD
|
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 (By similarity). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity).
|
A4IIN5
|
TISD_XENTR
|
mRNA decay activator protein ZFP36L2 (Zinc finger protein 36, C3H1 type-like 2)
|
MSTTLLSAFYDIDLLYKNEKVLNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSASNLQALSGNTNPAKFCPNNNQLKEPAAGSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQKAGAQVNSTRYKTELCRPFEESGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSSSLYCQELLQLNNNNNPCANNAFTFSGQELGLIAPLAIHTQNPPYCRQPSSSPPLSFQPLRRVSESPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSDSPTLDSNRRLPIFSRLSISDD
|
Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (By similarity). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs (By similarity). Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Required for tubulogenesis during pronephros development (By similarity).
|
A4IU28
|
LADA_GEOTN
|
Long-chain alkane monooxygenase (EC 1.14.14.28) (Long-chain alkane degradation protein A)
|
MTKKIHINAFEMNCVGHIAHGLWRHPENQRHRYTDLNYWTELAQLLEKGKFDALFLADVVGIYDVYRQSRDTAVREAVQIPVNDPLMLISAMAYVTKHLAFAVTFSTTYEHPYGHARRMSTLDHLTKGRIAWNVVTSHLPSADKNFGIKKILEHDERYDLADEYLEVCYKLWEGSWEDNAVIRDIENNIYTDPSKVHEINHSGKYFEVPGPHLCEPSPQRTPVIYQAGMSERGREFAAKHAECVFLGGKDVETLKFFVDDIRKRAKKYGRNPDHIKMFAGICVIVGKTHDEAMEKLNSFQKYWSLEGHLAHYGGGTGYDLSKYSSNDYIGSISVGEIINNMSKLDGKWFKLSVGTPKKVADEMQYLVEEAGIDGFNLVQYVSPGTFVDFIELVVPELQKRGLYRVDYEEGTYREKLFGKGNYRLPDDHIAARYRNISSNV
|
Involved in the degradation of long-chain alkanes. Converts alkanes ranging from C(15) to C(36) into their corresponding primary alcohols.
|
A4K144
|
M2_I54A2
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLIIAASVVGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4K2Q5
|
STK4_OTOGA
|
Serine/threonine-protein kinase 4 (EC 2.7.11.1) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)]
|
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVRQCLVKSPDQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENSEEDELDSGTMVRAVGDEMGTVRVASTMSDGANTMIEHDDTLPSQLGTMVINADDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKVPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
|
Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes.
|
A4K2T0
|
STK4_MACMU
|
Serine/threonine-protein kinase 4 (EC 2.7.11.1) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)]
|
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGASTMIEHDDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
|
Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes.
|
A4K436
|
RTEL1_BOVIN
|
Regulator of telomere elongation helicase 1 (EC 3.6.4.12)
|
MPKITLKGVTVDFPFQPYKCQEEYMSKVLECLQEKVNGILESPTGTGKTLCLLCSTLAWREHLRDAVSARRIAERASGELFPDRTLASWGNAIPEGDVPACYTDIPKIIYASRTHSQLTQVISELRNTSYRPRVCVLGSREQLCIHPEVKKQESNHMQVHLCRRKVASRSCHFYNNVEEKSLEQELATPILDIEDLVRSGTKHKLCPYYLSRNLKQQADIIFMPYNYLLDAKSRRAHGIDLKGTVVIFDEAHNVEKMCEEAASFDLTPHDVASELDVIDRVLEERTKVAQQAELHPEFSADSARSGLNLEPEDLAKLKMILLRLEGAIDAVELPGDNSGVTKPGSYIFELFAEAQITFQTKGCILDSLDQLIQHLAGRAGLFTNTAGLQKLVDIIQIVFSVDSAEGDPGPMVGLASQSYKVHIHLDAGHRRTAQRSDVWNTTAARKPGKVLSYWCFSPGHSMRELVRQGVRTLILTSGTLAPMASFSLEMQIPFPVCLENPHVINQHQIWVGVIPKGPDGAQLSSAFDRRFSDECLSSLGKVLSNISRVVPHGLLVFFPSYPVMEKSLEFWRARDFTRKLEVRKPLFVEPRSKGGFSEVMEAFYARVAAPESSGAIFLAVCRGKASEGLDFADVNGRGVIVTGLPYPPRMDPRVLLKMQFLDEMKAQSGAGGQFLSGHDWYRQQASRAVNQAIGRVIRHRHDYGAVFLCDHRFAHADTRAQLPSWVRPHVKVYDSFGHVIRDVAQFFRVAQKTMPEPAPRAAAPSLGEGGGIVSVSVSPGPLPTRKAMSLDVHVPSLRQRHTGSPVTKDTEGSLCVEYEQEPVRAQRRPAGLLAALGHNEQLAEGPGDEALPVEEACGCPTLLGPREKRPAEEQRGRRRKVRLVGSSEVPAASTDTGRAKLFMVAVKQALSQASFDTFTQALRDYKSSDDLEALVARLSPLFAEDPKKHSLLQGFYQFVRPHHKQQFEEVCLQLTGQGCSSPHKHGHPQRQGAQLALDSSGRKESDPKLTVSQGATRQLDPCEQLNQGRPHLASGPFPAGDLNCSLHKGSRAPGAEKQHPSTVSAYLADVRRTLGAAGYSQLLTALTTYKQDDDFEKVVAVVAALTTEKPEDLPLLQRFGMFVRPHHKQRFRQMCVDLSGPGTQAPGPQEGGPAMPSDPVCEAPSPGPRKTQSKISSFLRCQACWRQHLQVSRKCPGCCAATRKQTLAQVFWPEPQ
|
ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-Rule:MF_03065}.
|
A4KZ49
|
POLG_TRMVU
|
Genome polyprotein [Cleaved into: P1 proteinase (N-terminal protein) (EC 3.4.-.-); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
|
MSSKKMMWVPKSAHKAPVVSREPVIRKKEWVARQIPKYIPVSNPSDCRDEISQTLLHFDSEEAVYDFVWRFPMGSIFWDTNGRIKPVVNCLLRATRMNLDYDVAADVYVCRDCLSCASSYMYFSNYHYDCRELRENHEAVVSCKYEQHIVSTFDVFPRYCTQEIEQNVVNWMTETLERYDNEPLRIEKQLQFYNHKTEQMESRVQEVQVTTAEYAVSDTYVPQQLSRKGSVSAKLTQRRANKIIMRTHEVENLIRETIDLCDERQIPITFVDVKHKRCLPRIPLRHMQAKPDISEIVEQGDMYNEVGQFIEQYQNLAEPFRVIRDYEVTRGWSGVILHRDDLALDPQTQARCLNNLFVVMGRCEHGHLQNALRPDCLEGLTYYSDTFGKVFNESLVKHHPGKHQFRIGSRTDYEWEELAMWVNAVCPVSFRCADCRPPQSLNEYIENIRMSKAMAELAGRQDALSKTLHKWTTMLISSVLTTEIRARDNLEPIQERIFTRNMPLGPLYDVAGAMNRAVIDIQTAVQNMQLSIGNSNMNEQQRNQTLLNEINKIKQHSFMQTKEMLSRFENIAQTYQNIISSASQPLSIHSMRQLMMDSRMDESFEFDIMRKKGSIASIAPMAFRTFEDIYSQPGVYNQKWLNLTPSGRFQTDIDYLRLDLPIDVIQKKKHVVNRNEIKEETCYVIVGQVNVSFCEVVARCFVPIPHVLRVGSPQNPTMIKIQDQEGGKTLVPKSGFCYVLQLVLMLGYVPDQLTAAFVKDVGIVVESLGPWPLFVDYLGAIKNLIIRYPTTIKAPTALHIVDHVDTVIHVMTTLGCVNKGEHYLTLQSVAQLHDAAMTVNIETFKDYRIGGVVPQLKHMLQSEEHMLEVLEAKPQWLVHLLLSPTQIWALSQSVVKYQVIHKVMTSNPDLAVALAQLVAISSNFSIFKNTEHVIQKYFEVSKQLQNVSGVILGEHNEYFETAFAQYSALRFSTDVVLLMDQFSTRKKTLDDLEDYYRKTIPSILIECGLLGPSDFGWRKRLVRGVVDRGSGLKSTVKSLGSFSTKEKWISWSGLGSGTITCVKFPFVCLQRSGSWLYSSTKTTAFNAVWMAGIKCVKSNVRSILLDSALYGAITLALLCAIKLIRKAFRFVEGLIKEDTSDDEDYVLHAKAASDSLYIQCLAWLALVVGCFNSGLANDIYFSTTKYRTLLDMVKTAHSDSFVFHAGDEEEGEIVELITRDNFVDYVYNHSDPLMEFDSETLLGWYTRISYQGRVLEHPLRVGTNCHLTRENVDEIAKNIATGAGNEFIVVGDVGSGKSTKLPIAVSTYGPVLILVPSRELVNNLCSSIWHVGKKQASTYMMNCITRGTSNISIMTYGYALALFSHCPIELQKYRFIQMDECHEFSSHMITFYSWWRESGKFTKLFKTTATPPGTVIKGGCVPTNHKVDVIEIRDVSVEEFCRRSIDSHAEGLRSLMPNGGRVIMFVPSRRECELARSSLISIPGARTWVVYRAAATQATKLVAELADDKHYFQIIITTTVLQNGVNLDPDCVVDFGQTFEAAYDRDSRQLGVRRRNINPGELIQRVGRVGRNKPGKFIQVGKRLEHEVVPNSCCVTDAILMSFTLELAPFISSHLIDEVNFVTREQVRTAMKFSAPLLFMIHYVRRDGRMLNGYYQQLKGLLLQTSDVALCDTLVGDAETNSFLTLRQYQLRGIIEAQEVLPDLPIPFYSSEFALPFYLEIGQITKEAIRARSFTLRIKTPDVKKAVMRLSTSATQIDQTIGILRTRLQLTRERLSKFSELKATAHNLRLTPIFNTCFDMGAAKSESTLRASLTAGEELLSALELARTEKSDKALEKLILDNPVLGDCLVFHGGPEEYFDQTLFQTSTGLINKYTVGIACLTVGLGCTIWYYLKKREKYVMHGKVHTRETGLTTNHLFVPGMKEHIQEWTGGDHEIGNRFGEAYKRRFIGRQPTEEQKLSKEKWDKREGQQTSVYKTLYDLDPTKFKYVVVECPDFDLKKKLNRQEKKQLDTTIVEACRTRMLDKGQHDFKDVERATVYLFNDNGVGHKVQLTPHNPLAVSRTTTHPVGFPAEAGRLRQTGQAMEMTPEELEKALDDNYVPHSRCQIDISHLHRHLAIVNTGGMSTQCFITQTMCVAPYHLAMGFKDNTKLTIYCSNGVYVMPVPKVEKMENMDLVVFRMPQDFPPLKRCATIREPKSSDEVTLITGKRTTHGIQLQFSKVVSIDRKSDTVWKYMIDSVPGVCGGMVMCVEDGCVVGFHSAAAIRNKVSNGSIFTPVTPQLLDSLQSSEGHLFDWYFNDDLISWKGVPTNMDPRNFPVSETISEFIFHNDSKGHGTDKYYGENLTIEGRVLQSFNTRHVVKGLDDAFAEYVNKFGEPPADTFTHLPSDLSSDAFYKDFMKYSTPVEVGTVNIENFEKAVQAVVELLEQQGFEQGEFSPEMDFYKILNSFNLDTAMGALYQCKKKDVLPMASHEQLATWFWNSLENLATGKLGLWKASLKAELRPKEKVLEKKTRVFTAAPFDVSFGAKAFVDDFNNKFYATQAGSNWTVGINKFNCGWDELARRFNPDWKFIDADGSRYDSSLTPLLFNAVLRIRQHFLRANGFERRMLSNFYTQLVWTPISTITGQIVKKNKGGPSGQPSTVVDNTMMLMIAVEYAKLQYGVTDLKYVCNGDDLILNAPQGVCETIRANFSHSFKELGLTYEFEQEVDSIDQVEYMSHKWIDCGGVLIPKLKPERIVSVLQWNKSLDLASQANKINAAWIESFGYGDLSKFIREYANWWGERNGQVGFLCSEEKVASLYLTNDVTIHTEEHDEFVFHSGADQSGVVKDQTGDKAEGSGTKTEDPPNQTTDPVNNPSNGGNKDAPQNLNATVVTKSYTYIPPIMKSLVTIDTAKKMADYTPPDALISTQACTLEQFGRWANAAANGLGLSMQAFQTDVVPYWIYWCIVNSASDEHKKLSSWTKVNMTIDDATGQINLNEGEAQTIYEMSPMFDEAKPTLRAVMRHFGALAYRWVKFSIAKRKPIIPHNAIKAGLMDVTYFPCCIDFVTVDQLSPQEQNVRNQVINARVSDTPRALFKHAQRAGAGEEDTNLRRDDDANYGRTRVGGAMFGTR
|
[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
|
A4L691
|
PINX1_RAT
|
PIN2/TERF1-interacting telomerase inhibitor 1 (Pin2-interacting protein X1)
|
MSMLAERRRKQKWAVDPRNTAWSNDDSKFGQKMLEKMGWSKGKGLGAQEQGATEHIKVKVKNNHLGLGATNNNEDNWIAHQDDFNQLLAALNTCHGQETADSSDNKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSETDLDCIFGKRRNKKLAQDGCSNSTADEADTSLTTTTTTTSAFTIQEYFAKRMAQLKSKSQAAAPGSDLSETPIEWKKGKKKTKEAAGTDIENSPQHKAKRHKKKKRVEAERGPAAKKRDQVELQPGGPSGDECSDASVEAAEDRVQTPDTQDDVPKPRKRRAKKTLQRPGGVAVDTAPDSAPVKKKKKVSR
|
Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor (By similarity). {ECO:0000250, ECO:0000269|PubMed:17624691}.
|
A4L7N3
|
FOXO1_PIG
|
Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)
|
MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDAAAGLPSASAAAVNADFMSNLSLLEESEDFPQAPGSVAAAAAAAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQQPPPPGPLSQHPPVPPAAAGSLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGNGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTIMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPMQTLQDSKSSYGGMAQYNCAAGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVLMGPSSVMPAYGGQASHNKMMNPSSHSHPGHAQSTSAVNGRALPHAVNTMPHASGMNRLTQEKTALQVPLPHPMQMNALGGYSPASTCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG
|
Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (By similarity). Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).
|
A4L9P5
|
HIPK1_RAT
|
Homeodomain-interacting protein kinase 1 (EC 2.7.11.1)
|
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQASSSHQVANFNIPAYDQGLLLQAPAVEHIVVTAADSSGSAATATFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRVTPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNMEICKRRVHMYDTVSQIKSPFTTHVAPSTSTNLTMSFSNQLSTVHNQASVLASSSTAAAATLSLANSDVSLLNYQSALYPPSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPLVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVQQAWPGGTQQILLPSAWQQLPGVALHNSVQPTAVIPEAMGSSQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSRKNKQSAPVSSTSSLEVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKFKPSSSSLKARSNVISYVTVNDSPDSDSSLSSPYPTDTLSALRGNSGTLLEGPGRTAADGIGTRTIIVPPLKTQLGDCTGATQASGLLSSSKTKPVASVSGQSSGCCITPTGYRAQRGGASAVQPLNLSQNQQSSSASTSQERSSNPAPRRQQAFVAPLSQAPYAFQHGSPLHSTGHPHLAPAPAHLPSQPHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
|
Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation (By similarity). Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity).
|
A4PBQ9
|
VM3VA_CROAT
|
Zinc metalloproteinase-disintegrin-like VAP2A (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP) (Vascular apoptosis-inducing protein 2A) (VAP2A)
|
MIQVLLVTICLAAFPYQGSSIILESGNVNDYEIVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEHQKYNPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYELANTVNDIYRYMYIHVALVGLEIWSNEDKITVKPEADYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSPINLVVAVIMAHEMGHNLGINHDRGYCSCGDYACIMRPEISPEPSTFFSNCSYFDCWDFITNHNPECIVNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNSCKMFYSNEDEHKGMVLPGTKCADGKVCSNGHCVDVATAY
|
Heterodimeric zinc metalloprotease VAP2 that induces apoptosis in endothelial cells, without triggering cell detachment.
|
A4PES0
|
WEE2_PIG
|
Wee1-like protein kinase 2 (EC 2.7.10.2) (Wee1-like protein kinase 1B) (Wee1B kinase) (pWee1B) (pigWee1B)
|
MGDNGDNKELKQKLNFSYSEEEQEDEGQKEAQESKKVQYHTPERCGHQDSEAKFTPPRTPLNHVCELSTPQVKDRASPDQGLRTPVSRPHTRPETPAPPDKSKPPPHCESPFTPRGHSSQSVISTGKLPSRGSKHLRLTPGPLTDEMTSLALVNINPFTPESYRRQFLKSNGKRKTRRDLEEAGPEEGKVEKGLPAKRCVLRETNMACRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPVSGLSDENLAMHEVYAHSVLGHHPHVVRYYSSWAEDDHMMIQNEYCNGGSLQAAISENAKSGNHFQEPKLKDILLQISLGLKYIHNYGMVHMDIKPSNIFICHKIPSDSPVVPEEAENEADWFLSANVTYKIGDLGHVTSISEPQVEEGDSRFLAKEILQENYQHLPKADIFALGLTIAVAAGAEALPTNGTSWHHIREGQLPNIPQDLSKEFYNLLKDMIDPDPVARPSAAALTRSRVLCPSLGRTEELQQQLNLEKFKTATLERELKEVQRAQSSKEGQSSPGVTGTHTGSRSTRRLVGGKSAKSSSFTWGQSSP
|
Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation.
|
A4Q998
|
PNPH_ANOGA
|
Purine nucleoside phosphorylase (EC 2.4.2.1) (AgPNP) (Inosine phosphorylase) (Inosine-guanosine phosphorylase)
|
MSKFSYLQNGKASTNGVPHANGHHQQHQNGHSNGVARNGGTATDTLPVAYQQKAATSGPFHMPRTEHVGYTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIPHFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMHLIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDERFGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVAEVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEEHCHDSIVGVGKNREKTLGEFVSRIVKHIHYEAKK
|
As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Preferentially acts on 2'-deoxyinosine and inosine, and to a lesser extent on 2'-deoxyguanosine and guanosine. Has no activity towards adenosine or 2'-deoxyadenosine.
|
A4Q9E5
|
TTLL3_MOUSE
|
Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3)
|
MQGVSSALLLSAGQLGPGAAWYRQEGSSECSWLRRSQPSELRTNFSSRWPWPRNSESRRSERLQWPGPASAKPEVASCGDSRRDYSSLPARHLSSARESSMPGALGTVNPQPVRTLVPPTLDEPLPDALRPPDDSLLLWRGLTKGPNHMGRLRNAKIHVERAVKQKKIFMIHGRYPVIRCLLRQRGWVEKKMVHPPGTALPAPQKDLDSSMLGDSDATEDEDEEENEMFRESQLLDLDGFLEFDDLDGIHALMSRMVRNETPYLIWTTRRDVLDCRFLSKDQMINHYARAGSFTTKVGLCLNLRNLPWFDEADADSFFPRCYRLGAEDDKKAFIEDFWLTAARNVLKLVVKLEEKSQSISIQAREEEAPEDTQPKKQEKKLVTVSSDFVDEALSACQEHLSSIAHKDIDKDPNSPLYLSPDDWSQFLQRYYQIVHEGAELRYLEVQVQRCEDILQQLQNVVPQLDMEGDRNIWIVKPGAKSRGRGIMCMNRLDEMLKLVDCNPMLMKDGKWIVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQRHLEASCHRHPMLPPDNMWSSQRFQAHLQEVDAPKAWSSVIVPGMKAAVIHALQTSQDNVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRRLDRSCDTGAFELIYKQPAVEVPQYVGIRLLVEGSTIKKPVPVGHRRTGVRSSLPHLLTQQGSGESKDSGSPTHRSASRKNARAESLEHTEKPEPAAVASVSGKGKKAPFHFPSLHSKAWLPSPRVHRPQGRVLRLQHDQLVGSKALSTTGKALMTLPTAKVLMSFPPHPDLKLAPSMLKPGKVGFELCCTTWRVVLSGGIGEEGHRQRAAPRPSSAPGKGLSSTEPCSKTET
|
Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction. Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions. Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development. Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility.
|
A4Q9E8
|
TTLL6_MOUSE
|
Tubulin polyglutamylase TTLL6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin--tyrosine ligase-like protein 6)
|
MLQCLTSESEEGAEEREESSTEDLEELKEFVTLAFVRENTQKRLQNAQQHGKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKTYICKPDSGCQGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPLRVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFNSYMKTHGYDVEQIWRGIEDVIIKTLISAHPVIKHNYHTCFPSHTLNSACFEILGFDILLDRKLKPWLLEVNHSPSFSTDSKLDKEVKDSLLYDALVLINLGNCDKKKVLEEERQRGRFLQQCPNREIRLEEVKGFQAMRLQKTEEYEKKNCGGFRLIYPGLNLEKYDKFFQDNSSLFQNTVASRARELYARQLIQELRQKQEKKVFLKKARKEETQGESAGEQARDKVVRLQRQRQQPKCKTVATCPPKQSLHPVTLVSCTSGLLLNIRGLKKGEISESLEQKDTKEAMLIPCKPVSARNYSSVPDLRSANPSCFEPEFHVPNAKVKEVKSAFMVNIESTAQPITSVESSRDATAPISTSLESLASMSLSTSPECSSPESVHMVSYNHKQQKASFHKPMQEKKSKPLMFSKSRHLDLNCTSMKNDINRQYLMSEILQKVQMKKKRPLFPAPKSQYPTLSKERCPHSRSSSRKKEMNSPSVFVLQASHSRAESLNDLLVVATQARLDPRPSRSHSGTTTRDSSTQDPKHTATA
|
Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins. Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions. Mediates microtubule polyglutamylation in primary cilia axoneme which is important for ciliary structural formation and motility. Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating. Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response.
|
A4Q9F0
|
TTLL7_MOUSE
|
Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 7) (mTTLL7)
|
MPSLPQDGVIQGSSPVDLGTELPYQCTMKRKVRKKKKKGIITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDAAVQQEKITDLQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKVPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQANQHDVTKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRKNLAKQKAEAQRRLYGQNPVRRLSPGSSDWEQQRHQLERRKEELKERLLQVRKQVSQEEHENRHMGNYRRIYPPEDKALLEKYEGLLAVAFQTFLSGRAASFQREMNNPLKKMREEDLLDLLEQCEIDDEKLMGKTGRVRGPKPLCCMPECAEVTKKQKYYGSSDSSYDSSSSSSNSELDENEKELCQKRLDQVPYSLKHTSHCKIIQQPSGSHNLIYSESPVYLTTLVFLSEFPDSMRRSVSCPRSISAHLPSRGDVRPFSSQQVIPLARPTSASRSHSLNRASSYARHLPHGSDTGSTNTLNESLRQLKTKEQEDDLTSQTLFVLKDMRIRFPGKSDAESELLIEDIMDNWKHYKTKVASYWLIKLDSVKQRKVLDIVKSSIRTVLPRIWRVPDAEELSLYRIFNRVFNRLLWSHGQGLWSCFCDSGSSWESIFSKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYTTETRGPISGIGPDWGNSRYLLPGSTQFLMRSPLYNMKYNSPGMTRSNVLFTSRYGRL
|
Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation.
|
A4Q9F1
|
TTLL8_MOUSE
|
Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8)
|
MSCPPTPNPPFRPPSHTRVLRTPPLPPWVCLNSKSLSTGVGGQKNQLREASMENGERKKLSSTLSDGDHKEENKLKQGIPQDLSSSPKLDRYKIARQLTEKAIKERKIFSIYGHYPVIRATLRRKGWVEKKFNFFPKALQNLGSEDKSAETKENQEIALERFDDIHDVMSRLVKNEIPYLLWTIKRDVVDYHSLTCDQMLNHYGKTASFTTKIGLCLNMRSLPWYVQANPNTFFPRCYGLCTESEKQEFLDDFRRTVAASILKWVVLHQNYCSKVKGKSKKEEAKNSDPSPKKDPENPDLKLPSLSGQVVDTACKVCQAYLGQLEHEDIDVSEASTEALSEEEWNDLTQQYYLLVHGNASITDSKSYFAQCQALLSKISSVNPQTEIDGIRNIWIIKPAAKSRGRDIVCMDRVENILSLVAADSQTTKDNKWVVQKYIETPMLIYDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNSIQRRLKNDKERSPLLPCHNMWTSTRFQEYLQKRGRGGTWGSIIYPSMKRAVTNAMRVAQDHVEARKNSFELYGADFILGRDFKPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVVVDRKLDRNCDIGNFELLWRQPAVELPPFNGSDLCVEGISVKKAKKQMPPIASVGLSESLLDAPPKVRSARALMETVIRPPRTTVRQDWKREEAKVLSTTWSMPVMDAEVRGRAKPIYAFEVNDYQHVDNKSHKSGYTRVQSSKVPGVTLTSAQHPALFAQTMKPTQMTSSPPPTASGNHRDSSPFCPIVFEELWLHPNSQRRPSSCILQSRAQGWIRGIP
|
Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferentially monoglycylates alpha-tubulin over beta-tubulin. Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility. Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1.
|
A4Q9F3
|
TTL10_MOUSE
|
Protein polyglycylase TTLL10 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 10)
|
MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEAAALQAKTQSIEDDPIYRKMPFRAPQARVVQRYVQNPLLLDGKKFDVRSYMLIACAMPYMVFFGHGYARLTLSLYNPHSSDLSGHLTNQFMQKKSPLYTLLKESTVWTMEHLNRYINDKFRKTKGLPRDWVFTTFTKRMQQIMSHCFLAVKSKLECKLGYFDLIGCDFLIDENFKVWLLEMNANPALHTNCEVLKAVIPGVVIETLDLALETCQKSLHSQKMLPLLSQRRFVLLYNGETTDLWPRLASSRPLNRLPNPNPNPNPNANPHPHPHPNPHPHPNPHPNANPHPPRPTCEAASSALSSARAAISERPGARKSMPSRGAPVCTPRKSRLSDSSGSSIAESEPSLCSGSLEGSRDTAREPSLGPPEEEREEEQRSTSHRGS
|
Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins. Involved in the elongation step rather than the initiation step of the polyglycylation reaction. Polyglycylates alpha-tubulin and beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1.
|
A4Q9F4
|
TTL11_MOUSE
|
Tubulin polyglutamylase TTLL11 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 11)
|
MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFCTEPYQEPNPQNLHHVFMHLTNYSLNIHSGKFVHSDSASTGSKRTFSSILCRLSSKGVDIKKVWSDIISLVIKTVIALTPELKVFYQSDIPTGRPGPTCFQILGFDILLMKNLKPMLLEVNANPSMRIEHEYELSPGVFENIPSLVDEEVKVAVIRDTLRLMDPLKKKKEIHFPDIYMDRKHRIPPVSDRMSSWKHKGSSLSIVRSQQMEKSFTSKEDLNCDPTGGDSEPNPEAHLPSICLKQVFPKYAKQFNYLRLVDRMANLFIRFLGIKGTMKLGPTGFRTFIRNCKLSSSSLSMAAVDILYIDITRRWNSVTVDQRDSGMCLQAFVEAFFFLAQRKFKLQPLHEQVASLIDLCEYHLSVLDEKRLLCHRGRPLQRNPPQMNRPEHSATGSSAPRVIGASKLSQS
|
Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Preferentially mediates ATP-dependent polyglutamate long side-chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions.
|
A4QB65
|
AROE_CORGB
|
Quinate/shikimate dehydrogenase (NAD(+)) (QSDH) (EC 1.1.1.-) (EC 1.1.1.24)
|
MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDANGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHPGTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFLSL
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively.
|
A4QPC6
|
BT2A2_MOUSE
|
Butyrophilin subfamily 2 member A2
|
MEPTTSLRSCPIASLLFFLVLSLFVLVSAQFTVIGPAEPILAMVGENTTLHCHLSPERNAEEMEVRWFRWRFFPAVLVYRGHQERPEEQMVAYRGRTTFMRTDISKGRVALIIHNVTAYDNGIYCCYFQEGRSYDQATMKLMVASLGSEPLIKMKTLEDGSILLECTSEGWYPEPRAVWRDPYDEVVPALEEEYTADREGLFTVTMTIIIRDCSVRNMTCSVNNTLLSQEVESVILIPESFVPSLPLWMVAVAVTLPVVMLILLTSGSICLVKKHRRKKSILSAEKEAEYEEKEAARQLQEELRWRRTLLHAADVVLDPDTAHPELFLSDDQRSVIRGSSRQSVPDNPERFDCRPCVLGRESFSSGKHYWEVEVENVMVWAIGVCRDSVERKGEALLVPQNGFWTLEMFGSQYRALSSPEKIIPLKERLHRIAVFLDCEGGDISFYNMRDRSHIYTCPPVTFTGPLRPFFRLGSDDSPLFICPAFTGAQGVTIPEGGLFLYKTRPISQSLVRKP
|
Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion.
|
A4QUT2
|
KATG2_MAGO7
|
Catalase-peroxidase 2 (CP 2) (EC 1.11.1.21) (Peroxidase/catalase 2)
|
MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVGDGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEAVNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELADAFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVDKLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNWVSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAKDAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTEEIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDFFVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRAIAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKVKK
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575, ECO:0000269|PubMed:21971530}.
|
A4QXX4
|
SSN3_MAGO7
|
Serine/threonine-protein kinase SSN3 (EC 2.7.11.22) (EC 2.7.11.23) (Cyclin-dependent kinase 8)
|
MSHSNPPTGASGGPGSASASAAPARGYYSLKRSIQTAFNDPLDRGLGPPAYQSKVRVMDKYQVIGFISSGTYGRVYKARGRQGQPGEFAIKKFKPDKEGEQITYTGISQSAIREMALCSELRHPNVIRLVETILEDKAIFMVFEYAEHDLLQIIHHHTQQPKHPIPPQTIKSIMFQLLNGCQYLHTNWVLHRDLKPANIMVTSSGEVKVGDLGLARIFWKPVRTLMQGDKVVVTIWYRAPELLMGSHHYTPAVDMWAVGCIFAELLSLRPIFKGEEAKMDNTKKGGSRDMPFQRHQMQKIVDIMGMPTKERWPLLTSMPDYDKLPLLQPPLSASGYSQQPAHSHHHHQHYNQGPQYGGRAGGPTSSSSANSSSAAAAASQSHLDKWYYHTVSQGQTAGPMPHAPPGSLASLGVEGYKLLAGLLEYDPEKRLTAAAALQHNFFSTGDRVSANCFEGCKAEYPHRRVSQEDNDIRTGSVPGTKRSGMPDDSMGRPGKRVKE
|
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
|
A4R5S9
|
KATG1_MAGO7
|
Catalase-peroxidase 1 (CP 1) (EC 1.11.1.21) (Peroxidase/catalase 1)
|
MGECPLRTANVAGGGTRNRDWWPNTLKLNILRQHTEATNPYDPNFDYAEAFKSLDYEGLKKDLRALMTDSQEYWPADFGHYGGLFVRMAWHSAGTYRVMDGRGGGGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLMLLTGNVALEDMGFKTFGFAGGRPDTWEADESTYWGGETTWLGNEVRYSSGNEGHKESGVIDGSESKKGHKDIHTRDLEKPVSAAHMGLIYVNPEGPDGIPDPVAAARDIRTTFSRMAMNDEETVALIAGGHTVGKTHGAAPSDNVGPEPEAAPIENQGLGWSNKHGSGKGPDTITSGLEVIWTKEPAKFTMNYLEYLFKYEWELTKSPAGANQWVAKNAEEFIPDAFDPSKKHKPRMLTTDLSLRFDPEYEKISRRFLENPEQFKDAFARAWFKLLHRDMGPRSRWLGPEVPKETLLWEDPIPTPDHPIIDGSDVDSLKKAILATGVAPSKLIQTAWASASTFRGGDKRGGANGARIRLEPQNKWEVNNPQQLAEVLKALEGVKADFEKSGKKVSIADLIVLAGVAAVEQAAGVPVPFTPGRGDATQEQTDVESFTHLEPAADAFRNYGKGTSRVTTEQIMVDRAQQLTLTAPELTVLVGGLRVLGANYDGSSHGVWTDKPGKLTNDFFVTLLDPYTSWKSVDGEVFEGTNSKSGKKLTGTRADLVFGSHSELRALAEVYGSADGQQKFTKDFVAAWDKVMNLDRFDVRRGIYDETRLKSKL
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}.
|
A4RD09
|
ARO1_MAGO7
|
Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MSTANGSSPTRISILGEESIIVDYGLWLNYVTHDLLNNIPSSTYVLITDTNLHSLYVPQFETAFTSASAAATSNSSATPPPPRAPRLLTYAIPPGEGSKSRDTKAEIEDWLLEQQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLNTLPAREFINGMAEVIKTAAIWDAEEFSALEQNAPAILSAVRTPASAAADPNARLLPISDILKRIVLGSARVKAHIVSADEKEGGLRNLLNFGHSIGHAFEAILTPQVLHGEAVAVGMVKEAELARHLGILRPAAVARLVKCIASYDLPISLEDKRLVRMTGGKSCPVDIVLAKMAVDKKNEGKQKKIVLLSAIGKTHEPKASSVDDRAIRVVLSAAVRVQPGVRPGLKVDVTPPGSKSISNRALILAALGKGPCRIKNLLHSDDTEHMLNAIGKLRGASFSWEDDGEILVVEGRGGQLFAPSEGELYLGNAGTASRFLTTVAALCSPSSDGDATSTVLTGNARMKLRPIGALVDALRSNGINIEYMGKESSLPIRVDAAGGFGGGVIELAATVSSQYVSSLLMAAPYAKEPVTLRLVGGKPISQPYIDMTIAMMRSFGIDVQRSTTEADTYHIPQGIYTNPAEYTVESDASSATYPLAVAAITGTTCTIPNIGSASLQGDARFAVEVLRPMGCTVEQSASSTTVTGPPLGQLKGIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDQLAKFGVHCNELDDGIEVTGNSWTELTEPREIYCYDDHRVAMSFSVLSVISPHPVLILERECTGKTWPGWWDVLSGVFGVAMDGEEPLSHSTVTGSGPNNRSVFVIGMRGAGKSTAGKWMASTLGRTFMDLDTELERRHNTTIPDMVKSEVGWEGFRKFEVELLREMMETKPEGYIFSCGGGIVETPEAREALISYCRAGGAVLLVHRDTTHVLEYLNRDKSRPAWSEEIEKVYIRRKPWYQECSNFEYHSPHLGVEESAVEMPVDFARFVSLICGKSSHLREVKAKPHSFFVSLTVPNITAHTATIPKAVVGSDAVELRVDLLQDHSPEFVVRQVALLRSLCKMPIIFTVRTVSQGGRFPDADHAGALALYRVALRMGVEYVDVEMTMPEDVIETVTKAKGYTSIIASHHDPKGTLSWRNGAWMQYYNKALHYGDVIKLVGWCRTDEDNFSLLTFKTRMLAAHESTPIIALNMGEQGKLSRVLNGFMTPVTHAALPAAAAPGQLTAAEIRQALSLLSKIPKRKFYLFGKPISKSRSPILHNTLFQQTGLPHTYSRLETDKVAEVETTIRASDFGGASVTIPLKLDIMPMLDEITDAAKTIGAVNTIIPVPVQAGKQRLRGDNTDWCGMVHSLRMAGVTGKRACPASGVVVGSGGTTRAAIFALHSLGFSPIYIIARNATSVETIASSFPAEYDIRNLQGTLAYTEGMARPEVVISTIPATGDVDEGILMAVDSVLTLPMGTSNTGAARVLLEMAYTPTFTNMMARAKDAGWGTVPGFEVLAAQGWFQFQLWTDIKPVYSTASSIVMNGTSDSS
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
A4RPM5
|
UBA4_MAGO7
|
Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]
|
MEEADKRAEELRAQIAECEATLQSLKEQLAAAEAAKTPPYSDSTETDRGSSSSTWKWPLAEAEYERYGRQLILPSVGIQGQLRLKAASVLIVGAGGLGCPASAYFAGAGVGTIGLVDGDTVEASNLHRQVAHGTSRVGMLKVDSAISYLRELNPLVKYNAHQSHLTPENAESIVSGYDLVLDCTDHPTSRYLISDVCVLLRKPLVSASALRTDGQLIVLNTPAAPQADLSGGPCYRCVFPKPPPPDAVTSCGEGGILGPVVGVMGVLQALEGIRLLAAGRHLSPSPEQQQTAISPSLLLFSAPPDGSPAGFRSVRMRGRRKDCFACGEKSALSLATLREGGLDYVQFCGGSRKPVALLKSEERVSAEQLNALLQQQAGEHGKPVLLDVREREHFEIANIPGAINIPFSKTQNPGARHNAEDTPKLDWLPDGVADGHSPVYVVCRVGNDSQTVARQLKEFGLDNQGKRFIGDVKGGMLAWKREVDSTLPFM
|
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}.
|
A4STF2
|
FADB_AERS4
|
Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
|
MIYQGETLSVSYLENGIAELRFDAPGSVNKLDRATLLSLSEAIAALQQQADLKGLILTSGKDAFIVGADITEFLELFDLPQEDLLGWLKKANDIFSAIEDLPVPTLSAIKGHALGGGCETILSTDFRLADTSAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITTGKDYRADDALKVGAIDAVVAPDALHSAAVQMMKDAIAGKLNWQSRRAAKKAPLRLSKLEAMMSFSTAAGMVAAVAGKHYPAPMTAVKTVEAAAGMSRDEALVVEAQGFIKLAKTDVAKALVGIFLNDQHIKALAKKAAKQAAKATRHAAVLGAGIMGGGIAYQSASKGIPAVMKDINEKALALGMGEATKLLNGQLEKGRIDGIKMGQVLSAITPTLSYDNVKHVDLVVEAVVENPKVKAAVLGEVEGIIGDDAVLASNTSTIPISLLAKGLKRPQNFCGMHFFNPVHRMPLVEIIRGEQTSDETINRVVAYAAAMGKSPVVVNDCPGFFVNRVLFPYFFGFNKLVADGADFAAVDKVMEKEFGWPMGPAYLLDVVGIDTGHHAGDVMAQGFPARMSKEGRTAIDVMYDASRFGQKNGKGFYAYEQDKKGKPKKVADVAAYELLAPIAKPKQDFDKEAIIAGMMIPMINEVVLCLEEGIVATPAEADIALVYGLGFPPFRGGVFRYLDTIGLDRYVAMADQYADLGPLYRVSDRLREMAAQGKTFY
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
|
A4U6V3
|
M2_I45A0
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAANIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4U7A7
|
M2_I51A0
|
Matrix protein 2 (Proton channel protein M2)
|
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
|
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
A4UGR9
|
XIRP2_HUMAN
|
Xin actin-binding repeat-containing protein 2 (Beta-xin) (Cardiomyopathy-associated protein 3) (Xeplin)
|
MSPESGHSRIFEATAGPNKPESGFAEDSAARGEGVSDLHEVVSLKERMARYQAAVSRGDCRSFSANMMEESEMCAVPGGLAKVKKQFEDEITSSRNTFAQYQYQHQNRSEQEAIHSSQVGTSRSSQEMARNEQEGSKVQKIDVHGTEMVSHLEKHTEEVNQASQFHQYVQETVIDTPEDEEIPKVSTKLLKEQFEKSAQEKILYSDKEMTTPAKQIKTESEYEETFKPSSVVSTSSTSCVSTSQRKETSTTRYSDHSVTSSTLAQINATSSGMTEEFPPPPPDVLQTSVDVTAFSQSPELPSPPRRLPVPKDVYSKQRNLYELNRLYKHIHPELRKNLEKDYISEVSEIVSSQMNSGSSVSADVQQARYVFENTNDSSQKDLNSEREYLEWDEILKGEVQSIRWIFENQPLDSINNGSPDEGDISRGIADQEIIAGGDVKYTTWMFETQPIDTLGAYSSDTVENAEKIPELARGDVCTARWMFETRPLDSMNKMHQSQEESAVTISKDITGGDVKTVRYMFETQHLDQLGQLHSVDEVHLLQLRSELKEIKGNVKRSIKCFETQPLYVIRDGSGQMLEIKTVHREDVEKGDVRTARWMFETQPLDTINKDITEIKVVRGISMEENVKGGVSKAKWLFETQPLEKIKESEEVIIEKEKIIGTDVSRKCWMFETQPLDILKEVPDADSLQREEIIGGDVQTTKHLFETLPIEALKDSPDIGKLQKITASEEEKGDVRHQKWIFETQPLEDIRKDKKEYTRTVKLEEVDRGDVKNYTHIFESNNLIKFDASHKIEVEGVTRGAVELNKSLFETTPLYAIQDPLGKYHQVKTVQQEEIVRGDVRSCRWLFETRPIDQFDESIHKFQIIRGISAQEIQTGNVKSAKWLFETQPLDSIKYFSDVEETESKTEQTRDIVKGDVKTCKWLFETQPMESLYEKVSLMTSSEEIHKGDVKTCTWLFETQPLDTIKDDSETAVKLQTVKQEEIQGGDVRTACFLFETENLDSIQGEEVKEIKPVEMDIQAGDVSSMRYKFENQSLDSISSSSEEVLKKIKTLKTEDIQKGNVLNCRWLFENQPIDKIKESQEGDECVKTVTDIQGGDVRKGCFIFETFSLDEIKEESDYISTKKTITEEVIQGDVKSYRMLFETQPLYAIQDREGSYHEVTTVKKEEVIHGDVRGTRWLFETKPLDSINKSETVYVIKSVTQEDIQKGDVSSVRYRFETQPLDQISEESHNIMPSIDHIQGGNVKTSRQFFESENFDKNNYIRTVSVNEIQKGNVKTSTWLFETHTMDELRGEGLEYENIKTVTQEDVQKGDVKQAVWLFENRTFDSIMEAHKGITKMTKEEIPPSDVKTTTWLFETTPLHEFNETRVEKIEIIGKSIKETLEDLYSQKVIQAPGIIIEADEIGDVRMAKYKLMNQASPEIQKEEIIRADLRNIMVNLLSKRDCTEREILISEEEKGNVNLTKTQLLNRSTEFHAEKEEIVKGDVQQAIKNLFSEERSVKKGILIQEDEKGDINMTIYCLLHENDGDTIEREEVIGGDVKRTIHNLLSSTSNNKISERAKIDASERGNVQFFTTCIEAGALDYLKQLHTESNETLTAKKQEGEKEIIGGDVEGTKLLLKKRQSLVERTVSETDIIPGDVHNTVKVFMTEPQSTFGKIPKEEIIKGDLTSTLNSLSQAVNQKTVTKTEEIIKGNMLATLKSLKESSHRWKESKQPDAIPGDIEKAIECLEKATNTKTEILKKELLKDDLETSLRSLKEAQRSFKEVHKEGVIKKDAKAVMAGSSGEQKTDIHQVAVQRNKNSLLQPKPGPFEPAAKWQGGADTLSQTMGKSCHGNLVEERTEVNLPKAPKGTVKIVIDREQNNDALEKSLRRLSNSHHKSNVLESGDKTGVWTDTTGEQHLRDEYMSRQLTSTVSVKNNLTTKESDRAVRELKKDDVFNSIQSAGKTVGKQQTYELRNDHQKMEGFHIKSPKKTKNIKILTDTQSSKPSPTQHPVSMPVGGTYDLSGDFQKQTLLKQETKYSNKDIKKKNINLQPMWQLLPVEQDTSNVTEMKVSEKSHNTFKATNKKRETDVHLKSQDFLMKTNTSTGLKMAMERSLNPINFNPENNVKESECPLPPPSPPPPPPSNASSEIEFPLPPPPPLMMFPEKNGFLPSLSTEKIKAEFESFPGLPLPPPPVDEKSERESSSMFLPPPPPPTPSQKPAHLLSSSAPEKHSGDFMQQYSQKEASNSQNSQAKIITGKTGVLPPPTLPKPKLPKHIKDNKNDFSPKVELATSLSDMECKITTSKDQKKVMVMTSSEHTETKQNVISKSLDERKQLSIDSANCLSHTVPGTSAPRKKQIAPLIKSHSFPESSGQQNPKPYMRKFKTPLMIAEEKYRQQKEEIEKQKQESSYYNIVKTQSQNQHITEVEKEMPLQKTNEEVSLSGIDSECTVVQPSPGSQSNARILGVCSDNQLSTTSPETVAAKRLHHVLAASEDKDKMKKEVLQSSRDIMQSKSACEIKQSHQECSTQQTQQKKYLEQLHLPQSKPISPNFKVKTIKLPTLDHTLNETDHSYESHKQQSEIDVQTFTKKQYLKTKKTEASTECSHKQSLAERHYQLPKKEKRVTVQLPTESIQKNQEDKLKMVPRKQREFSGSDRGKLPGSEEKNQGPSMIGRKEERLITERKHEHLKNKSAPKVVKQKVIDAHLDSQTQNFQQTQIQTAESKAEHKKLPQPYNSLQEEKCLEVKGIQEKQVFSNTKDSKQEITQNKSFFSSVKESQRDDGKGALNIVEFLRKREELQQILSRVKQFEAEPNKSGLKTFQTLLNTIPGWLISEDKREYAVHIAMENNLEKVKEEITHIKTQAEDMLVSYENIIQTAMMSSKTGKPGNKPTSLDETSSKVSNVHVSNNKNSEQKENKIAKEKTVQHQVAAHHEATVRSHVKTHQEIKLDDSNIPPPSLKTRPPSPTFITIESTARRTENPTKNELSQSPKKDSYVEPPPRRPMSQKSEIHRANTSPSPPRSRSEQLVRLKDTTAKLSKGAIPCPAATPVPIVEKRSEIIMSPATLRRQIKIETRGRDSPPTITIPVNINHAASGSFRESVDAQEEIRKVEKRATYVHKDGLNSTDHMVPDTESYDAVEIIRKVAVPPRLSEHTQRYEAANRTVQMAENFVNDPENEINRWFREFEHGPVSEAKSNRRVYAKGETNHNIQQESRTFCKEEFGLTSLGNTSFTDFSCKHPRELREKIPVKQPRICSETRSLSEHFSGMDAFESQIVESKMKTSSSHSSEAGKSGCDFKHAPPTYEDVIAGHILDISDSPKEVRKNFQKTWQESGRVFKGLGYATADASATEMRTTFQEESAFISEAAAPRQGNMYTLSKDSLSNGVPSGRQAEFS
|
Protects actin filaments from depolymerization.
|
A4UHT7
|
SALR_PAPBR
|
Salutaridine reductase (EC 1.1.1.248)
|
MPETCPNTVTKMRCAVVTGGNKGIGFEICKQLSSSGIMVVLTCRDVTRGLEAVEKLKNSNHENVVFHQLDVTDPITTMSSLADFIKARFGKLDILVNNAGVAGFSVDADRFKAMISDIGEDSEEVVKIYEKPEAQELMSETYELAEECLKINYYGVKSVTEVLLPLLQLSDSPRIVNVSSSTGSLKYVSNETALEILGDGDALTEERIDMVVNMLLKDFKENLIETNGWPSFGAAYTTSKACLNAYTRVLAKKIPKFQVNCVCPGLVKTEMNYGIGNYTADEGAKHVVRIALFPDDGPSGFFYDCSELSAF
|
Involved in biosynthesis of morphinan-type benzylisoquinoline alkaloids. Catalyzes the stereospecific conversion of salutaridine to salutaridinol.
|
A4UTP7
|
MEF2C_PIG
|
Myocyte-specific enhancer factor 2C
|
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIPAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNFLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
|
Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity).
|
A4UUI3
|
GBP4_MOUSE
|
Guanylate-binding protein 4 (EC 3.6.5.-) (GTP-binding protein 4) (GBP-4) (Guanine nucleotide-binding protein 4)
|
MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGWSHTGKSYLMNCLAGQNHVSGTLPTSQRFPSGLHRAVSDQGHLDVVHAPPHQARALVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFVYNSMNTINHQALEQLHYVTELTELIRAKSSPNPHGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPGNNPRIQASNSARECIRRFFPNRKCFVFEWPTHDIELIKQLETISEDQLDPTFKESAMAFASYIFTYAKIKTLREGIKVTGNGLGTLVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTDTIQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELLREKNGLFLLKNEEASDKYCQEELDRLSKDLMDNISTFSVPGGHRLYMDMREKIEHDYWQVPRKGVKASEVFQNFLQSQAIIESSILQADTALTAGQKAIAEKHTKKEAAEKEQDLLRQKQKEHQEYMEAQEKRNKENLEQLRRKLEQEREQLIKDHNMMLEKLTKEQKTFREEGYKTQAEELRREIHQLGHNIKEMKQNGDSLVESILRSWFSFISPPSESEKAISSVLSLLRKKDRL
|
Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens. Negatively regulates the antiviral response by inhibiting activation of IRF7 transcription factor.
|
A4UVI1
|
FADS1_PAPAN
|
Acyl-CoA (8-3)-desaturase (EC 1.14.19.44) (Delta(5) fatty acid desaturase) (D5D) (Delta(5) desaturase) (Delta-5 desaturase) (Fatty acid desaturase 1)
|
MAPDPVAAKTPVQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYDISEFTRRHPGGSRVISHYAGQDATDPFVAFHSNKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVEQMGLMKANHVFFLLYLLHILLLDGAAWLTLWIFGTSFLPFLLCAVLLTAAQIQAGWLQHDLGHLSVFSTSKWNHLVHHFVIGHLKGVPASWWNHMHFQHHAKPNCFGKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALVPFFFQWYVFYFVIQRKKWVDLAWMITFYIRLLLTYVPLLGLKAFLGLYFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPMMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQLWLDAYLHQ
|
[Isoform 1]: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively (Probable). As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity). [Isoform 2]: Does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity.
|
A4VBF0
|
PA2H_VIPBN
|
Acidic phospholipase A2 inhibitor chain HPD-1I (svPLA2 homolog) (Heterodimeric neurotoxic phospholipases A2 acidic subunit)
|
MRTLWIVAVCLIGVEGNLFQFGDMILQKTGKEAVHSYAIYGCYCGWGGQGRAQDATDRCCFAQDCCYGRVNDCNPKTATYTYSFENGDIVCGDNDLCLRAVCECDRAAAICLGENVNTYDKNYEYYSISHCTEESEQC
|
Heterodimer: slightly affects neuromuscular transmission acting presynaptically. It has a low catalytic activity, a low anticoagulant activity and weakly inhibits ADP-induced platelet aggregation. Monomer: has no activity (neurotoxic, catalytic, anticoagulant and a ADP-induced platelet aggregation), but inhibits phospholipase A2.
|
A4VCL2
|
FA20C_DROME
|
Extracellular serine/threonine protein CG31145 (EC 2.7.11.1) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK)
|
MAVLRTMKLKERLVISLGATLVLLTLLLIVDVQMDFGVANRHLLQQQHQKIRLGNDYDGGTGGGGMLHEFKRKFLQKSNASGSKEASTQAGASQSGGATSGQDAAAGASGGAAGPGTSRSTSTRKPTPHDRYADLQKHLLSDEYSHVIVDNAPDVSRDNPTLAEMLHRKASANASNLERFQLRITKKELYGEQDTLVDAVLRDMIKLPIQHVVQKEGGTQLKLIIEYPNDIKALMKPMRFPREQQTLPNHFYFTDYERHNAEIAAFHLDRILGFRRAMPVAGRTLNITTEIYQLAEENLLKTFFVSPSLNLCFHGKCSYYCDTSHAICGNPDMLEGSFAAFLPNFESGNRKLWRHPWRRSYHKRKKAQWETDANYCALVRDIPPYDDGRRLYDLMDMAVFDFLTGNMDRHHYETFKVYGNETFPLHLDHGRGFGRPFHDELSILAPVLQCCLIRKSTLVKLLDFHNGPKPLSQLMSESLSQDPVSPVLWQPHLEALDRRTGIILQSIRDCIKRNPPGDVDGSETDVSS
|
Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs.
|
A4VFY3
|
AKECT_STUS1
|
Aspartate kinase Ask_Ect (EC 2.7.2.4) (Aspartokinase)
|
MHTVEKIGGTSMSRFEEVLDNIFIGRREGAALYQRIFVVSAYSGMTNLLLEHKKTGEPGVYQRFADAQSEGAWREALEGVRQRMLAKNAELFSSEYELHAANQFINSRIDDASECMHSLQKLCAYGHFQLSEHLMKVREMLASLGEAHSAFNSVLALKQRGVNARLADLTGWQQEAPLPFEEMISSHFAGFDFSRELVVATGYTHCAEGLMNTFDRGYSEITFAQIAAATGAREAIIHKEFHLSSADPNLVGADKVVTIGRTNYDVADQLSNLGMEAIHPRAAKTLRRAGVELRIKNAFEPEHGGTLISQDYKSEKPCVEIIAGRKDVFGIEVFDQDMLGDIGYDMEISKLLKQLKLYVVNKDSDANSITYYASGSRKLINRAARLIEEQYPAAEVTVHNLAIVSAIGSDLKVKGILAKTVAALAEAGISIQAIHQSIRQVEMQCVVNEEDYDAAIAALHRALIEPENHGDVIAAA
|
Involved in the biosynthesis of L-aspartate-beta-semialdehyde, which is an intermediate in the biosynthesis of ectoine, a highly soluble organic osmolyte, called compatible solute. Ectoine is used to avoid excessive water efflux, plasmolysis, molecular crowding of the cytoplasm, and cessation of growth in high salinity environments. Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.
|
A4VGK4
|
D2HDH_STUS1
|
D-2-hydroxyglutarate dehydrogenase (D-2-HG dehydrogenase) (D2HGDH) (EC 1.1.99.39) (D-malate dehydrogenase) (EC 1.1.99.-)
|
MTDPALIDELKTLVEPGKVLTDADSLNAYGKDWTKHFAPAPSAIVFPKSIEQVQAIVRWANAHKVALVPSGGRTGLSAAAVAANGEVVVSFDYMNQILEFNEMDRTAVCQPGVVTAQLQQFAEDKGLYYPVDFASAGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDLRQLFIGAEGTLGFVVEATMRLERQPTNLTALVLGTPDFDSIMPVLHAFQDKLDLTAFEFFSDKALAKVLGRGDVPAPFETDCPFYALLEFEATTEERAEQALATFEHCVEQGWVLDGVMSQSEQQLQNLWKLREYISETISHWTPYKNDISVTVGKVPAFLKEIDAIVGEHYPDFEIVWFGHIGDGNLHLNILKPDAMDKDEFFGKCATVNKWVFETVQKYNGSISAEHGVGMTKRDYLEYSRSPAEIEYMKAVKAVFDPNGIMNPGKIFAA
|
Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate or D-2-HG) to 2-oxoglutarate and of (R)-malate (D-malate) to oxaloacetate. Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the adjacent gene in the locus. Is required for the utilization of D-2-hydroxyglutarate as well as D-malate as the sole carbon source for growth of P.stutzeri. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol (DCPIP) and appears to couple with electron transfer flavoprotein (ETF) for efficient oxidation of both D-2-hydroxyglutarate and D-malate in vivo. Cannot catalyze the oxidation of L-2-hydroxyglutarate, D-lactate, D-tartrate, D-2-hydroxybutanoate, D-mandelate, D-glycerate and D-phenyllactate.
|
A4VKA3
|
FADB_STUS1
|
Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
|
MIYEGKAITVKALESGIVELNFDLKGESVNKFNRLTLNDLRQAVDAIKADASVKGVIVTSGKDVFIVGADITEFVDNFKLPDEELVAGNLEANKIFSDFEDLGVPTVVAINGIALGGGFEMCMAADYRVMSTTAKVGLPEVKLGIYPGFGGTVRLPRLIGVDNAVEWIASGKENRAEDALKVHAVDAVVAPEKLQEAALDLVKRAISGELDYKAKRQPKLDKLKLNAIEQMMAFETSKAFVAGQAGPNYPAPVEAIKTIQKAANFGRDKAIEVEAAGFVKLAKTSVAQSLVGLFLSDQELKKKAKAYDKQARDVKLAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEGIQMGLDEASKLLGKRVEKGRLTPEKMAQALNAIRPTMSYGDFGNVDIVVEAVVENPKVKHAVLAEVEGHVREDAIIASNTSTISISYLAQALKRPENFCGMHFFNPVHMMPLVEVIRGEKTSETAIATTVAYAKKMGKSPVVVNDCPGFLVNRVLFPYFGGFARAIAHGVDFVRADKVMEKFGWPMGPAYLMDVVGMDTGHHGRDVMAEGFPDRMKDDTRTAVDVMYDANRLGQKNGKGFYAYEMDKKGKPKKVVDPQAYELLKPIVAETRELSDEDIINYMMIPLCLETVRCLEDGIVETAAEADMGLIYGIGFPPFRGGALRYIDSIGVAEFVAMADKYADLGPLYHPTAKLREMAANGQRFYG
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
|
A4VLU6
|
CYSG_STUS1
|
Siroheme synthase [Includes: Uroporphyrinogen-III C-methyltransferase (Urogen III methylase) (EC 2.1.1.107) (SUMT) (Uroporphyrinogen III methylase) (UROM); Precorrin-2 dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase (EC 4.99.1.4)]
|
MEYLPLFHNLKGRTVLIVGGGEIALRKARLLSEAGARLRVVAPSIEAQLVELVQAGAGECLDRGYARQDLQGCVLAIAATDDEPLNATVSQHANALGVPVNVVDSPQLCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRARIETWIPAAYGQLAGLAKQFRAQVKARFANVQQRRVFWEEVFQGPIAEQALAGRTAEAERLLAEKLAGVAPKALGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPAIIDLCRRDADRIYVGKQRADHAVPQEQINQQLVTLAKQGKRVLRLKGGDPFIFGRGGEEIEELAAHGVPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGSCDLPWSELAAPAQTLVFYMGLVGLPVICQQLIAHGRSAETPAALVQQGTTSNQRVFTATLGTLAGRIAQEDVQAPTLLIVGEVVQLREKLAWFEGAQAAGR
|
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. {ECO:0000255|HAMAP-Rule:MF_01646}.
|
A4WFX4
|
FADB_ENT38
|
Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
|
MLYKGDTLYVDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFQVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLIDGIVKAEKLRDGAISILRQAINGDLDWKAKRQRKLEPLKLSKIEATMSFTIAKGMVMQTAGKHYPAPITAVKTIEAAARLGREEALKLENQSFVPLAHTNEARALVGIFLNDQFVKGKAKQLTKNVEMPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLSGVISTIHPTLEYSGFDRVDVVVEAVVENPKIKKAVLAETEDKVRPDTVLASNTSTIPIGELASVLKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEDDTAVESLLADVSQPTRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQQLGPLYEVPDGLRNKARHNEPYYPPVEPARPVGALKTA
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
|
A4WYU7
|
AGO_CERS5
|
Protein argonaute (RsAgo)
|
MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARNVRLAPKVEYVFDRTGAKSAEYAWRGLSQFGPFDRPSFANRSPRILVVYPSSTQGKVENFLSAFRDGMGSNYSGFSKGFVDLMGLTKVEFVMCPVEVSSADRNGAHTKYNSAIEDKLAGAGEVHAGIVVLFEDHARLPDDRNPYIHTKSLLLTLGVPTQQVRMPTVLLEPKSLQYTLQNFSIATYAKLNGTPWTVNHDKAINDELVVGMGLAELSGSRTEKRQRFVGITTVFAGDGSYLLGNVSKECEYEGYSDAIRESMTGILRELKKRNNWRPGDTVRVVFHAHRPLKRVDVASIVFECTREIGSDQNIQMAFVTVSHDHPFVLIDRSERGLEAYKGSTARKGVFAPPRGAISRVGRLTRLLAVNSPQLIKRANTPLPTPLLVSLHPDSTFKDVDYLAEQALKFTSLSWRSTLPAATPVTIFYSERIAELLGRLKSIPNWSSANLNIKLKWSRWFL
|
A catalytically inactive argonaute protein. Binds 5'-phosphorylated RNA as the guide (gRNA) and short DNA as target DNA (tDNA) does not bind other nucleic acid combinations, does not bind tDNA alone. Has highest affinity for gRNA that begins with 5'-phospho-U and poor affinity for gRNA with 5'-OH. Upon expression in E.coli, plasmid sequences are found in RsAgo, its induction leads to plasmid degradation and suppression of genes encoded on foreign plasmids, suggesting it may also interfere with transcription. Does not interact with preformed gRNA:tDNA duplexes. Mismatches and nt bulges are tolerated in the ternary complex, however, they significantly reduce the affinity of RsAgo:gRNA for tDNA. Mismatched tDNA can cause dissociation of gRNA from RsAgo. In situ binds 2 populations of RNA (15-19 and 45 nucleotides, nt) and a population of ssDNA 22-24 nt in length. The small sense RNA is probably derived from mRNA degradation and strongly enriched for U in the first and U/C in the second positions. The small DNA is enriched for sequences complementary to the RNA, with 3 nt overhangs on both ends another nuclease may trim the ends. The sequences are largely derived from exogenous plasmids or genome-encoded foreign elements such as prophages and transposons. Forms a ternary complex with gRNA and double-stranded tDNA only when the tDNA is open.
|
A4X3Q0
|
SALL_SALTO
|
Adenosyl-chloride synthase (EC 2.5.1.94) (5'-chloro-5'-deoxyadenosine synthase) (Chlorinase SalL)
|
MQHNLIAFLSDVGSADEAHALCKGVMYGVAPAATIVDITHDVAPFDVREGALFLADVPHSFPAHTVICAYVYPETGTATHTIAVRNEKGQLLVGPNNGLLSFALDASPAVECHEVLSPDVMNQPVTPTWYGKDIVAACAAHLAAGTDLAAVGPRIDPKQIVRLPYASASEVEGGIRGEVVRIDRAFGNVWTNIPTHLIGSMLQDGERLEVKIEALSDTVLELPFCKTFGEVDEGQPLLYLNSRGRLALGLNQSNFIEKWPVVPGDSITVSPRVPDSNLGPVLG
|
Involved in the biosynthesis of the proteosome inhibitor salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine (5'-CIDA) and L-methionine. It can also use bromide and iodide, producing halogenated 5'-deoxyadenosine (5'-XDA) and L-methionine, however no halogenase activity is detected in the presence of fluoride.
|
A4XF23
|
MAND_NOVAD
|
D-mannonate dehydratase (ManD) (EC 4.2.1.8) (RspA homolog)
|
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRGKLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLSPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
|
Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
|
A4XSM8
|
FADB_PSEMY
|
Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
|
MIYEGKAITVKALESGIVELNFDLKGESVNKFNRLTLNELRASVDAIKADGSIKGVIVTSGKDVFIVGADITEFVDNFKLPDEELVAGNLEANKIFSDFEDLAVPTVVAINGIALGGGFEMCLAGDYRVMSETAKIGLPEVKLGIYPGFGGTVRLPRVIGTDNAVEWIASGKENKAADALKVGAVDAVVAPAKLKEAALDLVKRAISGELDYKAKRQPKLEKLKLNAIEQMMCFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFVKLAKTSVAESLIGLFLNDQELKKKAKHHDEIARDVKLAAVLGAGIMGGGIAYQSASKGTPILMKDIREEGIQMGLTEASKLLGKRVEKGRMTPAKMAEALNAIRPTMSYGDFGNVDIVVEAVVENPKVKQIVLAEVEDVVREDAILASNTSTISISLLAQALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSEVAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFSKLLGFGVDFVRIDKVMEKFGWPMGPAYLSDVVGIDTGHHGRDVMAEGFPDRMAVEGKTAVDVMYEANRLGQKNGKGFYAYETDKRGKPKKVSDPEAYELLKSIVVEEREVTDEDIINFMMIPLCLETVRCLEDGIVDTAAEADMGLIYGIGFPPFRGGALRYIDSIGVAEFVALADKYADLGALYHPTAKLREMAAKGQKFFG
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
|
A4YDR9
|
HBCL2_METS5
|
4-hydroxybutyrate--CoA ligase 2 (EC 6.2.1.40) (Acetate--CoA ligase) (EC 6.2.1.1) (Butyrate--CoA ligase) (EC 6.2.1.2) (Propionate--CoA ligase) (EC 6.2.1.17) (acyl-activating enzyme)
|
MGGFKIPNYEGVDPTGSWYSVLTPLLFLERAGKYFKDKTAVVYRDSRYTYSTFYDNVMVQASALMRRGFSREDKLSFISRNRPEFLESFFGVPYAGGVLVPINFRLSPKEMAYIINHSDSKFVVVDEPYLNSLLEVKDQIKAEIILLEDPDNPSASETARKEVRMTYRELVKGGSRDPLPIPAKEEYSMITLYYTSGTTGLPKGVMHHHRGAFLNAMAEVLEHQMDLNSVYLWTLPMFHAASWGFSWATVAVGATNVCLDKVDYPLIYRLVEKERVTHMCAAPTVYVNLADYMKRNNLKFSNRVHMLVAGAAPAPATLKAMQEIGGYMCHVYGLTETYGPHSICEWRREWDSLPLEEQAKLKARQGIPYVSFEMDVFDANGKPVPWDGKTIGEVVMRGHNVALGYYKNPEKTAESFRDGWFHSGDAAVVHPDGYIEIVDRFKDLINTGGEKVSSILVEKTLMEIPGVKAVAVYGTPDEKWGEVVTARIELQEGVKLTEEEVIKFCKERLAHFECPKIVEFGPIPMTATGKMQKYVLRNEAKAKANKEKS
|
Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.
|
A4YDT1
|
HBCL1_METS5
|
4-hydroxybutyrate--CoA ligase 1 (EC 6.2.1.40) (Acetate--CoA ligase) (EC 6.2.1.1) (Butyrate--CoA ligase) (EC 6.2.1.2) (Propionate--CoA ligase) (EC 6.2.1.17)
|
MVTVQDFFRKFIEFQNSPNEKSLQEIVKLVGQLDLRRFNWVRDVFEDIHVKERGSKTALIWRDINTGEEAKLSYHELSLMSNRVLSTLRKHGLKKGDVVYLMTKVHPMHWAVFLAVIKGGFVMVPSATNLTVAEMKYRFSDLKPSAIISDSLRASVMEEALGSLKVEKFLIDGKRETWNSLEDESSNAEPEDTRGEDVIINYFTSGTTGMPKRVIHTAVSYPVGSITTASIVGVRESDLHLNLSATGWAKFAWSSFFSPLLVGATVVGINYEGKLDTRRYLGEVENLGVTSFCAPPTAWRQFITLDLDQFRFERLRSVVSAGEPLNPEVIKIWKDKFNLTIRDFYGQTETTAMVGNFPFLKVKPGSMGKPHPLYDIRLLDDEGKEITKPYEVGHITVKLNPRPIGLFLGYSDEKKNMESFREGYYYTGDKAYFDEEGYFYFVGRGDDVIKTSDYRVGPFEVESALLEHPAVAEAAVVGVPDTVRWQLVKAYIVLKKGYMPSKELAEEIREKMKTLLSPYKVPRIIEFVDELPKTISGKIRRVELRKREEEKRKKGEVGQNEYVF
|
Involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle which incorporates carbon dioxide into cellular carbon. Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.
|
A4ZDL6
|
GNK2_GINBI
|
Antifungal protein ginkbilobin-2 (Antimicrobial protein Gnk2-1)
|
MKTMRMNSAFILAFALAAAMLILTEAANTAFVSSACNTQKIPSGSPFNRNLRAMLADLRQNTAFSGYDYKTSRAGSGGAPTAYGRATCKQSISQSDCTACLSNLVNRIFSICNNAIGARVQLVDCFIQYEQRSF
|
Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity. Exerts antifungal activity against S.cerevisiae and F.culmorum through its carbohydrate-binding specificity. Acts as a lectin that stricly recognizes alpha-1,2-linked mannose moieties and interacts with the yeast cell wall mannan polysaccharide. Can interfere with the fungal actin remodeling resulting to the activation of an actin-dependent cell death.
|
A5A616
|
MGTS_ECOLI
|
Small protein MgtS
|
MLGNMNVFMAVLGIILFSGFLAAYFSHKWDD
|
Modulates intracellular Mg(2+) levels to maintain cellular integrity upon Mg(2+) limitation. Acts by binding and stabilizing the Mg(2+) transporter MgtA, thereby leading to increased intracellular level of Mg(2+). May inhibit FtsH proteolysis of MgtA.
|
A5A6H8
|
ITM2B_PANTR
|
Integral membrane protein 2B (Immature BRI2) (imBRI2) (Transmembrane protein BRI) (Bri) [Cleaved into: BRI2, membrane form (Mature BRI2) (mBRI2); BRI2 intracellular domain (BRI2 ICD); BRI2C, soluble form; Bri23 peptide (Bri2-23) (ABri23) (C-terminal peptide) (P23 peptide)]
|
MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS
|
Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites (By similarity). Mature BRI2 (mBRI2) functions as a modulator of the amyloid-beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers.
|
A5A6I5
|
ALDOA_PANTR
|
Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Muscle-type aldolase)
|
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIVGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIAEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY
|
Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04075}.
|
A5A6I6
|
TRFE_PANTR
|
Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin)
|
MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEATTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKNDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGPNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVKEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
|
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation (By similarity).
|
A5A6J1
|
TBA1A_PANTR
|
Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
|
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
A5A6J2
|
DDX5_PANTR
|
Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5)
|
MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVENCIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQASFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ
|
Involved in the alternative regulation of pre-mRNA splicing its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity).
|
A5A6J8
|
AT1B1_PANTR
|
Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1)
|
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKIGNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
|
This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1.
|
A5A6K9
|
HS90A_PANTR
|
Heat shock protein HSP 90-alpha
|
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVIPHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD
|
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes.
|
A5A6L1
|
CCN1_PANTR
|
CCN family member 1 (Cellular communication network factor 1) (Cysteine-rich angiogenic inducer 61) (Protein CYR61)
|
MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVSGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD
|
Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5 (By similarity). CCN1-mediated gene regulation is dependent on heparin-binding (By similarity). Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1 (By similarity). Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-1/beta-5 and cell proliferation through integrin alpha-v/beta-3 (By similarity).
|
A5A6M2
|
ANXA1_PANTR
|
Annexin A1 (Annexin-1) [Cleaved into: Annexin Ac2-26]
|
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTRRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
|
Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2.
|
A5A6M3
|
RBMX_PANTR
|
RNA-binding motif protein, X chromosome (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]
|
MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY
|
RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment (By similarity).
|
A5A6N6
|
EMP2_PANTR
|
Epithelial membrane protein 2 (EMP-2)
|
MLVLLAFIIAFHITSAALLFIATIDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFFIFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHHKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMYLILRKRK
|
Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (By similarity). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (By similarity). Also regulates many processes through PTK2 (By similarity). Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation. Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (By similarity). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity).
|
A5A6P2
|
ASAH1_PANTR
|
Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylethanolamine hydrolase ASAH1) (EC 3.5.1.-) (N-acylsphingosine amidohydrolase) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta]
|
MPGRSRVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMLDKAPMLKVIVNSLKNMINTFVPSGKIVQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLSLNERFSINGGYLGILEWILGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
|
Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity).
|
A5A6P7
|
GPC3_PANTR
|
Glypican-3 (GTR2-2) (Intestinal protein OCI-5) (MXR7) [Cleaved into: Glypican-3 alpha subunit; Glypican-3 beta subunit]
|
MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASKELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVARVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSVPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMMKVKNQLRFLAELAYDLDVDDAPGSNQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH
|
Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (By similarity). Positively regulates the non-canonical Wnt signaling pathway (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (By similarity). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (By similarity).
|
A5A7I8
|
CDPK5_SOLTU
|
Calcium-dependent protein kinase 5 (CDPK 5) (StCDPK5) (EC 2.7.11.1)
|
MGNACRGSFGGKTFQGYPQPQDHSESNSNPKHNSDSPKPKKEQQPLVTMNRTSTNQSYYVLGHKTPNIRDLYTLGRKLGQGQFGTTYLCTELSSGIDYACKSIAKRKLISKEDVEDVRREIQIMHHLAGHKNIVSIKGAYEDPLYVHIVMELCGGGELFDRIIQRGHYTERKAADLTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKHYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGHIDFDSDPWPLLSESAKDLIRKMLCMRPSERLTAHEVLCHPWICENGVAPDRALDPAVLSRLKHFSAMNKLKKMALRVIAESLSEEEIAGLKEMFKAMDTDNSGAITFDELKAGLRKYGSTLKDIEIRELMDAADVDNSGTIDYGEFIAATIHLNKLDREEHLMAAFQYFDKDGSGYITVDELQQACADHNITDVFFEDIIREVDQDNDGRIDYGEFVAMMQKGNPCIGRRTMRNSLNFSMRDAPGAH
|
Regulates the production of reactive oxygen species (ROS) by NADPH oxidase.
|
A5CAL1
|
2KGR_VITVI
|
Glyoxylate/hydroxypyruvate/pyruvate reductase 2KGR (EC 1.1.1.26) (EC 1.1.1.28) (EC 1.1.1.79) (2-keto-L-gulonate reductase) (Vv2KGR) (EC 1.1.1.-)
|
MESIGVLLTCPMNPYLEQELDKRFKLFRFWDFPSANDLFREHSNSIRAVVGNSFIGADAQMIEALPKMEIVSSFSVGLDKIDLVRCKEKGIRVTNTPDVLTEDVADLALALILATLRRICESDRYVRSGSWKKGDFKLTTKFTGKSVGIIGLGRIGSAIAKRAEGFSCPISYHSRTEKPGTNYKYYPSVVELASNCQILVVACALTPETRHIINREVINALGPKGVVINIGRGLHVDEPELVSALVEGRLGGAGLDVFENEPNVPEELLAMDNVVLLPHVGSGTVETRKDMADLVLGNLEAHFLNKPLLTPVV
|
Involved in the biosynthesis of L-tartarate from L-ascorbate. Catalyzes the NAD(P)H-dependent reduction of 2-dehydro-L-idonate (2-keto-L-gulonate) to L-idonate. Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate. Prefers NADPH to NADH as proton donor.
|
A5D7B7
|
SEPR_BOVIN
|
Prolyl endopeptidase FAP (EC 3.4.21.26) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) (Z-Pro-prolinal insensitive peptidase) (ZIP) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]
|
MKTWLKIVFGVATSAVLALLVMCIVLRPSRVHNSEESTTRALTLKDILNGTFSYKTFFPNWISGQEYLHQSTDNNVVFYNIETGESYTILSNTTMKSVNASNYGLSPDRQFAYLESDYSKLWRYSYTATYHIYDLTNGEFIRRNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPEDPPFQITYNGKENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTEIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDATYPEHIGPREVPVPAMIASSDYYFSWLTWVTDDRICLQWLKRIQNVSVLSTCDFREDWQTWNCPKTQEHIEESRTGWAGGFFVSTPVFSHDTISYYKIFSDKDGYKHIHYIRDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGSHSPSKKCITCHLRKKRCQYYTASFSDYAKYYALVCYGPGLPISTLHDGRTDQEIKILEDNKELENALKNIQLPKEEIKKLKVDDITLWYKMILPPQFDKSKKYPLLIQVYGGPCSQSVRSIFAVSWISYLASKEGIVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYTERFMGLPTKDDNLKHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTKHLYTHMTHFLKQCFSLSD
|
Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.
|
A5D7D1
|
ACTN4_BOVIN
|
Alpha-actinin-4 (Non-muscle alpha-actinin 4)
|
MVDYHAANQSYQYGPSSGSNGAGGGGTMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANIVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
|
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.
|
A5D7E9
|
NF2L1_BOVIN
|
Endoplasmic reticulum membrane sensor NFE2L1 (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1]
|
MLSLKKYLTEGLLQFTILLSLIGVRVDVDTYLTSQLPPLREIILGPSSAYTQTQFHNLRNTLDGYGIHPKSIDLDNYFTARRLLNQVRALDRFQVPTTEVNAWLVHRDPEGSVSGSQPSSGLALESSSGLQDVTGPDNGVRESETEQGFSEDLEDLGAVAPPVSGDLTKEDIDLGAGREIFDYSHRQKEQDVDKELRDGAEQEDTWPGEGAEALARNLLVDGETGESFPAQVPGGEDQTALSLEECLRLLEATCPFGENAEFPADISSITEAVPSESEPPGLQNNLLSPLLTGTESPFDLEQQWQDLMSIMEMQAMEVNTSTSEVLYNAPPGDPLSTNYSLAPNTPINQNVSLHQASLGGCSQDFSLFSPEVESLPVASSSTLLPLVPSNSTSLNSTFGSTNLAGLFFPPQLNGTANDTAGPELPDPLGGLLDEAMLDEISLMDLAIEEGFNPVQASQLEEEFDSDSGLSLDSSHSPSSLSSSEGSSSSSSSSSSSSSSSASSSASSSFSEEGAVGYSSDSETLDLEEAEGAVGYQPEYSKFCRMSYQDPSQLSCLPYLEHVGHNHTYNMAPSALDSADLPPPSTLKKGSKEKQADFLDKQMSRDEHRARAMKIPFTNDKIINLPVEEFNELLSKYQLSEAQLSLIRDIRRRGKNKMAAQNCRKRKLDTILNLERDVEDLQRDKARLLREKVEFLRSLRQMKQKVQSLYQEVFGRLRDENGRPYSPSQYALQYAGDGSVLLIPRTLADQQARRQERKPKDRRK
|
[Endoplasmic reticulum membrane sensor NFE2L1]: Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (By similarity). Constitutes a precursor of the transcription factor NRF1 (By similarity). Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (By similarity). In response to stress, it is released from the endoplasmic reticulum membrane following cleavage by the protease DDI2 and translocates into the nucleus to form the transcription factor NRF1 (By similarity). Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal, such as CD36 (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (By similarity). [Transcription factor NRF1]: CNC-type bZIP family transcription factor that translocates to the nucleus and regulates expression of target genes in response to various stresses. Heterodimerizes with small-Maf proteins (MAFF, MAFG or MAFK) and binds DNA motifs including the antioxidant response elements (AREs), which regulate expression of genes involved in oxidative stress response. Activates or represses expression of target genes, depending on the context (By similarity). Plays a key role in cholesterol homeostasis by acting as a sensor of cholesterol excess: in low cholesterol conditions, translocates into the nucleus and represses expression of genes involved in defense against cholesterol excess, such as CD36 (By similarity). In excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal (By similarity). Critical for redox balance in response to oxidative stress: acts by binding the AREs motifs on promoters and mediating activation of oxidative stress response genes, such as GCLC, GCLM, GSS, MT1 and MT2 (By similarity). Plays an essential role during fetal liver hematopoiesis: probably has a protective function against oxidative stress and is involved in lipid homeostasis in the liver (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, mediates the 'bounce-back' of proteasome subunits by translocating into the nucleus and activating expression of genes encoding proteasome subunits (By similarity). Also involved in regulating glucose flux (By similarity). Together with CEBPB represses expression of DSPP during odontoblast differentiation. In response to ascorbic acid induction, activates expression of SP7/Osterix in osteoblasts (By similarity).
|
A5D7F8
|
SH3R1_BOVIN
|
E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1)
|
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRPWKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQRHSMEISPPVLISSSNPAAAARIGELAGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPAEAPYPAALATLNPPLPPPPLQAATPTGTAVAAAAGMGPRPTAGPTDQTTHPRPQPRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTSASQGKVPMLTTGPASRGGVLANPPSTGGPAQKPPGNGVAGGPGVPTAVVSAAHVQTSPQAKVLLHASGQMTVNQARSAARTVSAHSQERPTAAVTPIQVQSTPGQSHHPLVSPQPPAPLGPPAHAAASGLGRVGGPLACATAPASIPAASLEPEPSSRPATLLPGTPTSPDSGSAARPDKDGKKEKKGLLKLLSGASTKRKPRGSPPASPTLDAELGAELSCGPPGPPCACPGPCDGDTMAPGPQRRASSLDSAPVAPPPRQPCSSLGPAASEVRPAVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
|
Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly.
|
A5D7I4
|
EXT1_BOVIN
|
Exostosin-1 (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostoses protein 1 homolog)
|
MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPDALRPFVPWDQLENEDSSVHVSPRQKREANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYPQQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSLHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKDHPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKHGKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVMLSNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVEKIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKFTAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATSVPVIVIEGESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWDNSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYTHYLPASLKNMVDQLANCEDILMNFLVSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHSQMRLDPVLFKDQVSILRKKYRDIERL
|
Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
|
A5D7L5
|
S39AE_BOVIN
|
Metal cation symporter ZIP14 (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14)
|
MELLRPALPSYFLLTLLSIWTAASEARAVSTGMPTISAASFLQNLMHRYGEGDSLTLQQLKALLNHLDVGVGRGNISQPVQGPRNLSTCFSSGELFAAHNLSHQSQIGEREFQEFCPTILQQLDSRACSSENQENEENEQTEEGRPSSVEVWGYGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPMEDYYVSKSAVVFGGFYLFFFTEKILKMLLKQKNEHHHGHSHYTSETLPSQKDQEEGVTEKLQNGDLDHMIPQHCSGELDGKTPVVDEKVIVGSLSVQDLQASQSACHWLKGVRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGISTSVAILCEEFPHELGDFVILLNAGMSLQQALFFNFLSACCCYVGLGFGILAGSHFSANWIFALAGGMFLYISLADMFPEMNEVSQEDERKGSALIPFVIQNLGLLTGFGIMLVLTMYSGHIQIG
|
Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (By similarity).
|
A5D7U4
|
SCNNB_BOVIN
|
Amiloride-sensitive sodium channel subunit beta (Beta-NaCH) (Epithelial Na(+) channel subunit beta) (Beta-ENaC) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB)
|
MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFVLTLLFTSLVCWQWGLFIKTYLNWEVSVSLSIGFKTMDFPAVTICNASPFQYSKVQHLLKDLDELMEAVLGRILGPELSQVNDTRALNLSIWHHTPLVFINEQNPHHPVVLDLFEDNFNGSASNSPAPGRPCSAHRCKVAMRLCSHNGTTCTFRNFSSATQAVTEWYTLQATNIFAQVPNQELVAMGYPAERLILACLFGAEPCNYRNFTPIFHPDYGNCYIFNWGMTEKALPSANPGTEFGLKLILDMGQEDYVPFLTSTAGARLMLHEQRSYPFIKEEGIYAMAGMETSIGVLVDKLQRKGEPYSQCTKNGSDVPIQNLYSNYNTTYSIQACIRSCFQEHMIRECGCGHYLYPLPHKRKYCNNQEFPDWAHCYSALRISLAQRETCIYACKESCNDTQYKMTISMAVWPSEASEDWIFHVLSQERDQSSNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEFGEIIIDFVWITIIKLVALAKSVRQKRAQARYEGPPPTVAELVEAHTNFGFQPDLATPGPDVEAYPHEQNPPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
|
Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.
|
A5D8Q0
|
XIAP_XENLA
|
E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP) (xXIAP)
|
MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS
|
Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of ripk2 downstream of NOD1 and NOD2, thereby transforming ripk2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (By similarity). A key apoptotic suppressor in eggs. Acts as a positive regulator of Wnt signaling.
|
A5D8S5
|
SH3R1_DANRE
|
E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1)
|
MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRPRRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIIILRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPPPQRHSMEISGPVLISSSNPTAAARIGELSGGLSSSAPSQVHICTTGLIVTPPPSSPVTTATVFTFPPETSYASIPVDALPPPPPPPPQSQSSVVGAAALNAGQRPSPAAGDQSGRQRPTVYVAMFPYSPRKEDELELRKGEMFLVLERCQDGWFKGTSMHTGKIGVFPGNYMSPVSRTVSGSSQPKVPLTLCSQAGRGVTIVSPSSALGSMDLSKPLPVCPNATPSCSLPAAVVTAAHLPTGQHPKVLMHVTSQMTVNQARNAVRTAVSHSQDRPTAAVTPIQSHNPVAYLPSTAVVLQASPVLNSSSGCSSARVGVALGCAAASLTPPNVSAASLDTDAMRPVPMVALPVNAGSTKPLGAASNHGVACRLDKDCKREKKGLLKLLSNKKKLRPSPPSSPTLEAEQSVSMELPQGAVGPEMALSGSAGHNGRIGACPMDSELSMSSSSSNTDAVTHRSSPQDNTAPIAPPPRQPCSSLLSMQHDGRPIVCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGRTGLFPGSFVDSI
|
Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway.
|
A5D8T8
|
CL18A_HUMAN
|
C-type lectin domain family 18 member A (Mannose receptor-like protein 2)
|
MLHPETSPGRGHLLAVLLALLGTAWAEVWPPQLQEQAPMAGALNRKESFLLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSPRGNWEVNGKTIVPYKKGAWCSLCTASVSGCFKAWDHAGGLCEVPRNPCRMSCQNHGRLNISTCHCHCPPGYTGRYCQVRCSLQCVHGRFREEECSCVCDIGYGGAQCATKVHFPFHTCDLRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDSDFETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQFAQEHISRWGPGS
|
Binds polysaccharides in a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans.
|
A5D8V6
|
VP37C_HUMAN
|
Vacuolar protein sorting-associated protein 37C (hVps37C) (ESCRT-I complex subunit VPS37C)
|
METLKDKTLQELEELQNDSEAIDQLALESPEVQDLQLEREMALATNRSLAERNLEFQGPLEISRSNLSDRYQELRKLVERCQEQKAKLEKFSSALQPGTLLDLLQVEGMKIEEESEAMAEKFLEGEVPLETFLENFSSMRMLSHLRRVRVEKLQEVVRKPRASQELAGDAPPPRPPPPVRPVPQGTPPVVEEQPQPPLAMPPYPLPYSPSPSLPVGPTAHGALPPAPFPVVSQPSFYSGPLGPTYPAAQLGPRGAAGYSWSPQRSMPPRPGYPGTPMGASGPGYPLRGGRAPSPGYPQQSPYPATGGKPPYPIQPQLPSFPGQPQPSVPLQPPYPPGPAPPYGFPPPPGPAWPGY
|
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
|
A5D8V7
|
ODAD3_HUMAN
|
Outer dynein arm-docking complex subunit 3 (Coiled-coil domain-containing protein 151)
|
MTSPLCRAASANALPPQDQASTPSSRVKGREASGKPSHLRGKGTAQAWTPGRSKGGSFHRGAGKPSVHSQVAELHKKIQLLEGDRKAFFESSQWNIKKNQETISQLRKETKALELKLLDLLKGDEKVVQAVIREWKWEKPYLKNRTGQALEHLDHRLREKVKQQNALRHQVVLRQRRLEELQLQHSLRLLEMAEAQNRHTEVAKTMRNLENRLEKAQMKAQEAEHITSVYLQLKAYLMDESLNLENRLDSMEAEVVRTKHELEALHVVNQEALNARDIAKNQLQYLEETLVRERKKRERYISECKKRAEEKKLENERMERKTHREHLLLQSDDTIQDSLHAKEEELRQRWSMYQMEVIFGKVKDATGTDETHSLVRRFLAQGDTFAQLETLKSENEQTLVRLKQEKQQLQRELEDLKYSGEATLVSQQKLQAEAQERLKKEERRHAEAKDQLERALRAMQVAKDSLEHLASKLIHITVEDGRFAGKELDPQADNYVPNLLGLVEEKLLKLQAQLQGHDVQEMLCHIANREFLASLEGRLPEYNTRIALPLATSKDKFFDEESEEEDNEVVTRASLKIRSQKLIESHKKHRRSRRS
|
Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
|
A5D8W1
|
CFA69_HUMAN
|
Cilia- and flagella-associated protein 69
|
MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDVFKPMDLNRVIKLLEETDKDGLEEKQLKFVKKLVQCYQNGLPLRDLAQIFKILNLCSGKIKNQPRFIESAYDIIKLCGLPFLKKKVSDEITYAEDTANSIALLGDLMKIPSSELRIQICKCIVDFYHAEPPKKHIPGYQQASSSYKIQMAEVGGLAKTMVQSMTLLENQLVEKLWVLKVLQHLSTSEVNCTIMMKAQAASGICTHLNDPDPSGQLLFRSSEILWNLLEKSSKEEVIQQLSNLECLLALKEVFKNLFMRGFSHYDRQLRNDILVITTIIAQNPEAPMIECGFTKDLILFATFNEVKSQNLLVKGLKLSNSYEDFELKKLLFNVIVILCKDLPTVQLLIDGKVILALFTYVKKPEKQKIIDWSAAQHEELQLHAIATLSSVAPLLIEEYMSCQGNARVLAFLEWCESEDPFFSHGNSFHGTGGRGNKFAQMRYSLRLLRAVVYLEDETVNKDLCEKGTIQQMIGIFKNIISKPNEKEEAIVLEIQSDILLILSGLCENHIQRKEIFGTEGVDIVLHVMKTDPRKLQSGLGYNVLLFSTLDSIWCCILGCYPSEDYFLEKEGIFLLLDLLALNQKKFCNLILGIMVEFCDNPKTAAHVNAWQGKKDQTAASLLIKLWRKEEKELGVKRDKNGKIIDTKKPLFTSFQEEQKIIPLPANCPSIAVMDVSENIRAKIYAILGKLDFENLPGLSAEDFVTLCIIHRYLDFKIGEIWNEIYEEIKLEKLRPVTTDKKALEAITTASENIGKMVASLQSDIIESQACQDMQNEQKVYAKIQATHKQRELANKSWEDFLARTSNAKTLKKAKSLQEKAIEASRYHKRPQNAIFHQTHIKGLNTTVPSGGVVTVESTPARLVGGPLVDTDIALKKLPIRGGALQRVKAVKIVDAPKKSIPT
|
Cilium- and flagellum-associated protein. In the olfactory epithelium, regulates the speed of activation and termination of the odor response and thus contributes to the robustness of olfactory transduction pathways (By similarity). Required for sperm flagellum assembly and stability.
|
A5D979
|
SPRTN_BOVIN
|
DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)
|
MDEDLVLALQLQEEWNLQVSEREPAQEPLSLVDASWELVDPTPDLQGLFVLFNDRFFWGQLEAVEVKWSVRMTLCAGICSYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINRLTGANITVYHTFHDEVDEYRRHWWRCNGPCQNSKPYYGYVKRATNRAPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKTKLRKQPVSEAENKDKPNRGEKQLLIPFTGKGYVLGETSNFSSGKCITSHAINESQEPLSQDHSANALRPHSKTEVKFEQNGPSKKTSVASPVLSTSHQNVLSNYFSKVSVASSKAFRSVSGSPVKSLTVGDSTTKSVSAGSQRRVTSSRTSLRNSLKAMESTYVTVPQDAGGPEGKLPSKRPRIEDKTFFDLFFIKKEQAQSGGGDVTSSSHPPAAAQSPSGASGQSRVVHCPVCQDEVSETQINEHLDWCLERDSTQVKS
|
DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity).
|
A5D9M6
|
BAG6_PIG
|
Large proline-rich protein BAG6 (BCL2-associated athanogene 6) (HLA-B-associated transcript 3)
|
MEPNDSTSTTMEEPESLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQLPSGASSGTGSASATHGGGPPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMECRGGSQAQHSQPPSQMPTVAPEPVALSSQTSESVESEVPPREPMAAEEVEERASAQSPGLSPSGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNQEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSLAPSSTTVESSTEGAPPPGPAPPPAASHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPTGHGQTLGQQVPGFPTAPTRVVIARPTPPQSRPSHPGGPPVSGALPGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPPQPSASDLQFSQLLGNLLGPAGPGAGGPGMTSPTITVAMPGVPAFLQGMTDFLQATQTAAPPAPPPPPPPPPPAPEQQTAPPPGSPPGGAGSPGGLGPESLPLEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPGNIRTATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVMHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGSERTSPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGAAAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRADIQKRLQEDPNYSPQRFPNAHRAFAEDP
|
ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).
|
A5F120
|
NHAD_VIBC3
|
Na(+)/H(+) antiporter NhaD (Sodium/proton antiporter NhaD)
|
MTGRIALLSLTLFSPLSLASTPDGQALDFTHSTIGYAALLIFAIAYTLVMLEEYLQLRKSKPVLLAAGLIWAMIGYVYQQTGSTEVARQALEHNLLEYAELLLFLLVAMTYISAMEERRLFDALKAWMINRGFNFHTLFWITGWLAFFISPIADNLTTALLMCAVVMKVGGENPKFVSLACINIVIAANAGGAFSPFGDITTLMVWQAGHVSFLEFMDLFLPSLANYLVPALVMSLFVPHQTPSSIQEVVELKRGAKRIVVLFLFTILSAIGFHAFFHFPPVIGMMMGLAYLQFFGYFLRKTLARSLAKKTAIAMAKNDEAALKRIGSVVPFDVFRSISHAEWDTLLFFYGVVMCVGGLSLLGYLGLVSEILYTEWNPIWANVLVGLLSSVVDNIPVMFAVLSMQPEMSLGNWLLVTLTAGVGGSLLSIGSAAGVALMGAAHGKYTFLSHLKWTPVILLGYVVSIVLHLLLNHQSFT
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium.
|
A5F465
|
FADB_VIBC3
|
Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
|
MIYQAKTLQVKQLANGIAELSFCAPASVNKLDLHTLESLDKALDALAADSSVKGLLLSSDKEAFIVGADITEFLGLFAKPEAELDEWLQFANRIFNKLEDLPFPTLSALKGHTLGGGCECVLATDFRIGDATTSIGLPETKLGIMPGFGGTVRLPRLIGADSAMEIITQGKACRAEEALKVGLLDAIVDSDKLIDSAITTLTQAIEEKLDWQKRRQQKTSALTLSKLEAMMSFTMAKGMVAQVAGKHYPAPMTSVVTIEEAARLPRDAALDIERKHFIKLAKSTEAQALVGIFLNDQYIKGLAKQSAKAASQDTQHAAVLGAGIMGGGIAYQSALKGVPVLMKDIAPHSLELGMTEAAKLLNKQLERGKIDGFKMAGILASITPSLHYAGIDQADVIVEAVVENPKVKAAVLSEVEGLVDAETILTSNTSTIPINLLAKSLKRPQNFCGMHFFNPVHRMPLVEIIRGEHTSEDTINRVVAYAAKMGKSPIVVNDCPGFFVNRVLFPYFAGFSLLMRDGANFTEIDKVMERQFGWPMGPAYLLDVVGIDTAHHAQAVMAEGFPTRMAKSGREAIDALYEAKKFGQKNGSGFYQYTVDKKGKPKKAFSDDVLAILAPVCGAPQNFDPQTLIERTMIPMINEVVLCLEEGIIASAQEADMALVYGLGFPPFRGGVFRYLDTIGIANYVAMAEKYADLGALYQVPQLLKNMAQQGTSFYSAQQASAL
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
|
A5F5X0
|
NQRB_VIBC3
|
Na(+)-translocating NADH-quinone reductase subunit B (Na(+)-NQR subunit B) (Na(+)-translocating NQR subunit B) (EC 7.2.1.1) (NQR complex subunit B) (NQR-1 subunit B)
|
MGLKKFLEDIEHHFEPGGKHEKWFALYEAAATLFYTPGLVTKRSSHVRDSVDLKRIMIMVWLAVFPAMFWGMYNAGGQAIAALNHLYSGDQLAAIVAGNWHYWLTEMLGGTMSSDAGWGSKMLLGATYFLPIYATVFIVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEVFGGTGRNFLNPALAGRAFLFFAYPAQISGDLVWTAADGYSGATALSQWAQGGAGALINNATGQTITWMDAFIGNIPGSIGEVSTLALMIGAAFIVYMGIASWRIIGGVMIGMILLSTLFNVIGSDTNAMFNMPWHWHLVLGGFAFGMFFMATDPVSASFTNSGKWAYGILIGVMCVLIRVVNPAYPEGMMLAILFANLFAPLFDHVVVERNIKRRLARYGKQ
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00426}.
|
A5F5Y4
|
NQRF_VIBC3
|
Na(+)-translocating NADH-quinone reductase subunit F (Na(+)-NQR subunit F) (Na(+)-translocating NQR subunit F) (EC 7.2.1.1) (NQR complex subunit F) (NQR-1 subunit F)
|
MSTIIFGVVMFTLIILALVLVILFAKSKLVPTGDITISINGDPEKAIVTQPGGKLLTALAGAGVFVSSACGGGGSCGQCRVKIKSGGGDILPTELDHISKGEAREGERLACQVAVKADMDLELPEEIFGVKKWECTVISNDNKATFIKELKLAIPDGESVPFRAGGYIQIEAPAHHVKYADFDVPEKYRGDWDKFNLFRYESKVDEPIIRAYSMANYPEEFGIIMLNVRIATPPPNNPNVPPGQMSSYIWSLKAGDKCTISGPFGEFFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLKSKRKMSYWYGARSKREMFYVEDFDGLAAENDNFVWHCALSDPQPEDNWTGYTGFIHNVLYENYLKDHEAPEDCEYYMCGPPMMNAAVINMLKNLGVEEENILLDDFGG
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. {ECO:0000255|HAMAP-Rule:MF_00430}.
|
A5FB63
|
CHIA_FLAJ1
|
Chitinase ChiA (EC 3.2.1.14)
|
MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAANSTNGLFVAAPRYIVPGCTNPQNPTGTWDGSGACEKSGSIEICDLVGNPVTNSHAYLDPNTMMVTPSAASAGWVRYFDNTTKVPYLYNSTLKQFISYEDKQSMDLKVQYIKSRNLAGGMIWELSQDTRGSIPNSLLNQVDTSFGSVVPGTVSISGSVKNGSALVTDVTVELRNASNAVIQTVVSANGNFAFNNLTSGQNYSLTALKATYTFTPVTLVNVTVNQTAVVINGTQPTYTVSGTVLDGSTPVSGVTVTAVSGSTTLTAVSNASGVYSIAGLTAGLNFTVTAAKSGFSYAPASTVYNAIDSNKTLNFTQGAPVVNYTVSGTVLNSTTPVSGVTVTASFTGGSYAAVTNASGTYSLSLPSGGNYTVTAALTGQTFTPASTVYSNLNANKTLNFTQDVVVSTSKISGTVKNGTNPVAGAKVELVLPWTDNTHNWKSVIATTDAQGKYSFDNSVVDGYTQVLSLKLNSWQNGEVAYYPNNLANFAVPANPTVYNFNTSSTAKSALAAAANLISGTVKNGTTPVAGAKVEIVLPWTDNTHNWKSVLATTDASGNYSFDNSVVAGYTQILSLKLNGWENGDVTYYPNNLANFAVPTTPTIYNFNRQAVVATKPVVTITAPTASAIAINLGSAINFVASVGLSAVDATTISSVVFSLDGQSLSTANSSGTYTAAWTPAANQFSLSHTLTVTATASNGTTDSKTYSFTLTCSGANCPNALPVITWNSPSNTTVYQNTFQVVPISVTAVDSDGTVSGVTITINGGTFNMTAGTNNTYTYNFTPSAYQDYPVVIKATDNKSGVTTLNNTIKIATVSTNRFIPLPSKIILGYAHSWENAGAPFLYFSQMVGSKFNVVDYSFVETVNRDGYTPILTTNDTRYLTNGVFNKQLLKNDIKSLRDSGVPVIVSIGGQNGHVVLDNVTQKNIFVNGLKAIIDEYQFDGVDIDFEGGSMNFNAGGLRDISYAGISAYPRLKNVVDAFKELKAYYGPGFLLTAAPETQYVQGGYTTYTDTFGSFLPIIQNLRNELDLLAVQLYNTGGENGLDGQYYGTAKKSNMVTALTDMVIKGYNIASTGMRFDGLPASKVLIALPACPSAAGSGYLTPTEGINAMHYLRTGTTFSGRTYTMQPGGPYPSLRGLMTWSVNWDASSCGNSSELSKAYAAYFASQTAAKTLVLDDISAKSNATIAYFKNNALSVTNENEDIAQVDVFNVLGQNLVSHRNVQNNKEVLLHNQSFSSKQLFLVVVTDKAGNKKSFKVMNFLN
|
Major extracellular chitinase, which is essential for chitin utilization.
|
A5GFW1
|
AURKA_PIG
|
Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)
|
MDKCKENCISGLKTTVPPGDGPKRVPVTQHFPAQHLPSANSGQAQRVLCPSNSSQRLPSHTQKLVSSHKPVQNLKQKQSQATSGPRPVSRPLSNTQQSEQPQPAAPGNNPEKEAASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKTQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVPEGARDLISRLLKHNPSHRPTLKEVLEHPWITANSKPASSHKKESTSKQP
|
Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (By similarity). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (By similarity). Required for initial activation of CDK1 at centrosomes (By similarity). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (By similarity). Regulates KIF2A tubulin depolymerase activity (By similarity). Required for normal axon formation (By similarity). Plays a role in microtubule remodeling during neurite extension (By similarity). Important for microtubule formation and/or stabilization (By similarity). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (By similarity). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (By similarity). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (By similarity).
|
A5GFZ6
|
MOCS3_PIG
|
Adenylyltransferase and sulfurtransferase MOCS3 (Molybdenum cofactor synthesis protein 3) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase MOCS3) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase MOCS3)]
|
MAAREEVLALQAEVARREEELSSLKHRLAAALLAEQESERLLPVSPLPPKAALSQDEILRYSRQLVLPELGVQGQLRLATASVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEVSNLARQVLHGEALAGQAKVFSAAASLRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYGGGPCYRCVFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGLFRRIQLRRRRPDCAACGERPTVTELQDYEGFCGSSATDKCRSLQLLSPEERVSVIDYKRLLDSGSPHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLGEAIREGKQGTQEGASLPIYVICKLGNDSQKAVKILQSLPDLDSLLVQDVVGGLMAWAAKVDGTFPQY
|
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}.
|
A5GZW8
|
DHSD_PIG
|
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (CII-4) (QPs3) (Succinate dehydrogenase complex subunit D) (Succinate-ubiquinone oxidoreductase cytochrome b small subunit) (Succinate-ubiquinone reductase membrane anchor subunit)
|
MATLWRLSVLCGARGGGALVLRTSVVRPAHVSAFLQDRHTPGWCGVQHIHLSPSHQASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKVAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL
|
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
|
A5H2P4
|
ARO12_LODEL
|
Pentafunctional AROM polypeptide 2 [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLEGFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPISVDEKIFSKIIGAKKNNLKIDSLIKKMLIDKKNDGSKIRCVLLESIGKCYESKAHQIFKEDIQVVMTDEVFVHPFANRHPESVSITPPGSKSISNRALILAALGEGTTRIKNLLHSDDTKHMLDAVVLMKGATVSFEDSGDTVVVQGHGGKLFACKEEIYLGNAGTASRFLTAVAALVNSTQDEKSVTLTGNARMQERPIAALVDALTTNGSKVDYLNKQGSLPLKIEAGNGFKGGRIELAATTSSQYVSAILMCAPYAEKEVTLSLVGGKPISQLYIDMTIAMMKDFGVDVTKSETEEYTYHIPKAVYQNPQEYVVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCTVEQTSKSTTVTGPPIGTLKALPEIDMEPMTDAFLTASVVAAVSQGTTTISGIANQRVKECNRIKAMVDELAKFGVSADETEDGISIHGVQLKDLKTPGGRGVKTYDDHRVAMSFSLLAGLCKDPVLIQERSTTGKTWPGWWDVLHSKFNAKLEGHEYIRQRSGSLRNGDRSIVIIGMRAAGKTTLSRWLAEHLNFKLLDLDQYLEKKLAVDIKLLVKEKGWDYFREKETEVLNECLEKFGKGHILATGGGIVEGEKPREALKNYTKSGGIVLHLHRDLKETVNFLSKDPTRPAYSDDIEEVWKRREKWYHECSNYHFYSTHCTSEAEFANLKLVFAKFVSKITGDDTFVLPATRSTFVTLTYPDLRKVPSLIKDVSETSNAVELRVDLLANQETAYIAEQIGLLRSVATDLPILYTVRTKSQCGQYPDEDEEGMRKLLMFGLKMGVDIIDLQLISSPSTIAEVISKRGHTKIIASHHDFTGDLKWDNVEWKNKYAQGVSIDADFVKLVGMAKTFDDNLLLENFRRQNTEKPLIGINMGPQGKLSRVLNKVLTPVTHELITDKPIGVGQLSLKEINQALFQIGGLLEKEFWVVGFPVSHSRSPALHNAAYAALGLPYKFDIFETDDAEKVYTQLMQKPTFGGLAVTIPLKLDIKKYCTELSESAKLIGAVNTVTPIADGRKGFLGDNTDWIGIANSFKKADFALASGVTNGLVVGGGGTSRAAIFALHSLGCQKIYLLNRTESKLQDLVDSFPDYDLEILLEKNASSVSIGLVVSCVPGDKALDETLMKKLDGVLSNNKGDKQTRPLLLEAAYKPRVTPIMELAKEKYDWTVIPGVEMLVNQGEAQFKLHTGYTAPYKVIHSAVLNE
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
A5H2Q8
|
ARO11_LODEL
|
Pentafunctional AROM polypeptide 1 [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
|
MSIEKVSILGKESIHVGYGIQSHIVEETIKCLASSTYVIISDTNMSKTPTYEKLQDSFQKELAKQRPQSRLLTYLIPPGENHKNRETKAEVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLSMVDSSVGGKTAIDTELGKNFIGAFHQPEFVFCDVSFLQTLPKRQLINGMAEVVKTAAIWDETEFTRLESFAKRFLAEISAPTPNLESIKDELIKTVLGSVRVKAFVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPSAVARLSKCLAAYGLPISVDEKIFSKIIGAKKNNLKIDSLIKKMLIDKKNDGSKIRCVLLESIGKCYESKAHQIFKEDIQVVMTDEVFVHPFANRHPESVSITPPGSKSISNRALILAALGEGTTRIKNLLHSDDTKHMLDAVVLMKGATVSFEDSGDTVVVQGHGGKLFACKEEIYLGNAGTASRFLTAVAALVNSTQDEKSVTLTGNARMQERPIAALVDALTTNGSKVDYLNKQGSLPLKIEAGNGFKGGRIELAATTSSQYVSAILMCAPYAEKEVTLSLVGGKPISQLYIDMTIAMMKDFGVDVTKSETEEYTYHIPKSVYQNPQEYVVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCTVEQTSKSTTVTGPPIGTLKALPEIDMEPMTDAFLTASVVAAVSQGTTTISGIANQRVKECNRIKAMVDELAKFGVSADETEDGIRIHGVQLRDLKTPGGRGVKTYDDHRVAMSFSLLAGLCKDPVLIQERSTTGKTWPGWWDVLHSKFNAKLEGHEYIRQRSGSLRNGDRSIVIIGMRAAGKTTLSRWLAEHLNFKLLDLDQYLEKKLAVDIKLLVKEKGWDYFREKETEVLNECLEKFGKGHILATGGGIVEGEKPREALKNYTKSGGIVLHLHRDLKETVNFLSKDPTRPAYSDDIEEVWKRREKWYHECSNYHFYSTHCTSEAEFANLKLVFAKFVSKITGDDTFVLPATRSTFVTLTYPDLRKVPSLIKDVSETSNAVELRVDLLANQETAYIAEQIGLLRSVATDLPILYTVRTKSQCGQYPDEDEEGMRKLLMFGLKMGVDIIDLQLISSPSTIAEVISKRGHTKIIASHHDFTGDLKWDNVEWKNKYAQGVSIDADFVKLVGMAKTFDDNLLLENFRRQNTEKPLIGINMGPQGKLSRVLNKVLTPVTHELITDKPIGVGQLSLKEINQALFQIGGLLEKEFWVVGSPVSHSRSPALHNAAYAALGLPYKFDIFETDDAEKVYSQLMQKPTFGGLAVTIPLKLDIKKYCTELSESAKLIGAVNTVTPIADGRKGFLGDNTDWIGIANSFKKADFALASGVSNGLVVGGGGTSRAAIFALHSLGCQKIYLLNRTESKLQDLVDSFPDYDLEILLEKNASSVSIGLVVSCVPGDKPLDETLMKKLDGVLSNNKGDKQTRPLLLEAAYKPRVTPIMELAKEKYDWTVIPGVEMLVNQGEAQFKLHTGYTAPYKVIHSAVLNE
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
A5H8G4
|
PER1_MAIZE
|
Peroxidase 1 (EC 1.11.1.7) (Plasma membrane-bound peroxidase 1) (pmPOX1)
|
MAKESKLTAGVAAALTVVAACALCLLLPATARAQLRVGFYDTSCPNAEALVRQAVAAAFAKDAGIAAGLIRLHFHDCFVRGCDGSVLLTVNPGGGQTERDALPNNPSLRGFDVIDAAKTAVEQSCPRTVSCADIVAFAARDSISLTGSVSYQVPAGRRDGRVSNATETVDLPPPTSTAQSLTDLFKAKELSVEDMVVLSGAHTVGRSFCASFFKRVWNTSTNPATAIVDAGLSPSYAQLLRALCPSNTTQTTPITTAMDPGTPNVLDNNYYKLLPRGMGLFFSDNQLRVNPQMAALVSSFASNETLWKEKFAAAMVKMGRIQVQTGTCGEVRLNCGVVNPSLYSSSSAVELGSSAPAAVGEEGYAAS
|
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12857829}.
|
A5HAK0
|
RNSL3_DANRE
|
Ribonuclease-like 3 (RNase ZF-3) (RNase-like 3) (ZF-RNase-3) (EC 3.1.27.-) (Dr-RNase 1) [Cleaved into: N-terminal peptide; LF-ZF3]
|
MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV
|
Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity.
|
A5HBE1
|
VP2_POVWU
|
Minor capsid protein VP2 (Minor structural protein VP2)
|
MGILLAVPEIIAASVAGGAEALSIAGSGAAIATGEGLAALGGLTESAALLGETVEISEAAATVLTKVPELVTVTQGVTAAVQGGAGLVGGIYTALAADRPGDLPASTPTGSPSGLHPPAGYNPQGGGLNIQSIHKPLHAPYPGMALAPIPEYNLETGIPGVPDWVFNFIASHLPELPSLQDVFNRIAYGIWTSYYNTGRTVVNRAVSEELQRLLGDLEYGFRTALATIGESDPVNAIVEQVRSFVSGGRQRELLQIAAGQPVDISEGVSRGTATISNAVEAVRDATQRLSQATYNFVYDASTLPRDGFNALSDGVHRLGQWISMPGATGGTPHYAAPDWILYVLEELNSDISKIPTQGIKRKLQQNGLHSKASLHSKTRKVTKKSTHKSAKPSKTSQKRRGRRAGRRTTVRRNRV
|
[Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity).
|
A5HC98
|
L_BUNLC
|
RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) [Includes: cap-snatching endonuclease (EC 3.1.-.-)]
|
MDYQEYQQFLARINTARDACVAKDIDVDLLMARHDYFGRELCKSLNIEYRNDVPFIDIILDIRPEVDPLTIDAPHITPDNYLYINNVLYIIDYKVSVSNESSVITYDKYYELTRDISDRLSIPIEIVIIRIDPVSRDLHINSDRFKELYPTIVVDINFNQFFDLKQLLYEKFGDDEEFLLKVAHGDFTLTAPWCKTGCPEFWKHPIYKEFKMSMPVPERRLFEESVKFNAYESERWNTNLVKIREYTKKDYSEHISKSAKNIFLASGFYKQPNKNEISEGWTLMVERVQDQREISKSLHDQKPSIHFIWGAHNPGNSNNATFKLILLSKSLQSIKGISTYTEAFKSLGKMMDIGDKAIEYEEFCMSLKSKARSSWKQIMNKKLEPKQINNALVLWEQQFMINNDLIDKSEKLKLFKNFCGIGKHKQFKNKMLEDLEVSKPKILDFDDANMYLASLTMMEQSKKILSKSNGLKPDNFILNEFGSRIKDANKETYDNMHKIFETGYWQCISDFSTLMKNILSVSQYNRHNTFRIAMCANNNVFAIVFPSADIKTKKATVVYSIIVLHKEEENIFNPGCLHGTFKCMNGYISISRAIRLDKERCQRIVSSPGLFLTTCLLFKHDNPTLVMSDIMNFSIYTSLSITKSVLSLTEPARYMIMNSLAISSNVKDYIAEKFSPYTKTLFSVYMTRLIKNACFDAYDQRQRVQLRDIYLSDYDITQKGIKDNRELTSIWFPGSVTLKEYLTQIYLPFYFNAKGLHEKHHVMVDLAKTILEIECEQRENIKEIWSTNCTKQTVNLKILIHSLCKNLLADTSRHNHLRNRIENRNNFRRSITTISTFTSSKSCLKIGDFRKEKELQSVKQKKILEVQSRKMRLANPMFVTDEQVCLEVGHCNYEMLRNAMPNYTDYISTKVFDRLYELLDKKVLTDKPVIEQIMDMMIDHKKFYFTFFNKGQKTSKDREIFVGEYEAKMCMYAVERIAKERCKLNPDEMISEPGDGKLKVLEQKSEQEIRFLVETTRQKNREIDEAIEALATEGYESNLGKIEKLSLGKAKGLKMEINADMSKWSAQDVFYKYFWLIALDPILYPQEKERILYFMCNYMDKELILPDELLFNLLDQKVAYQNDIIATMTNQLNSNTVLIKRNWLQGNFNYTSSYVHSCAMSVYKEILKEAITLLDGSILVNSLVHSDDNQTSITIVQDKMENDKIIDFAMKEFERACLTFGCQANMKKTYVTNCIKEFVSLFNLYGEPFSIYGRFLLTSVGDCAYIGPYEDLASRISSAQTAIKHGCPPSLAWVSIAISHWMTSLTYNMLPGQSNDPIDYFPAENRKDIPIELNGVLDAPLSMISTVGLESGNLYFLIKLLSKYTPVMQKRESVVNQIAEVKNWKVEDLTDNEIFRLKILRYLVLDAEMDPSDIMGETSDMRGRSILTPRKFTTAGSLRKLYSFSKYQDRLSSPGGMVELFTYLLEKPELLVTKGEDMKDYMESVIFRYNSKRFKESLSIQNPAQLFIEQILFSHKPVIDFSGIRDKYINLHDSRALEKEPDILGKVTFTEAYRLLMRDLSSLELTNDDIQVIYSYIILNDPMMITIANTHILSIYGSPQRRMGMSCSTMPEFRNLKLIHHSPALVLRAYSKNNPDIQGADPTEMARDLVHLKEFVENTNLEEKMKVRIAMNEAEKGQRDIVFELKEMTRFYQVCYEYVKSTEHKIKVFILPAKSYTTTDFCSLMQGNLIKDKEWYTVHYLKQILSGGHKAIMQHNATSEQNIAFECFKLITHFADSFIDSLSRSAFLQLIIDEFSYKDVKVSKLYDIIKNGYNRTDFIPLLFRTGDLRQADLDKYDAMKSHERVTWNDWQTSRHLDMGSINLTITGYNRSITIIGEDNKLTYAELCLTRKTPENITISGRKLLGSRHGLKFENMSKIQTYPGNYYITYRKKDRHQFVYQIHSHESITRRNEEHMAIRTRIYNEITPVCVVNVAEVDGDQRILIRSLDYLNNDIFSLSRIKVGLDEFATIKKAHFSKMVSFEGPPIKTGLLDLTELMKSQDLLNLNYDNIRNSNLISFSKLICCEGSDNINDGLEFLSDDPMNFTEGEAIHSTPIFNIYYSKRGERHMTYRNAIKLLIERETKIFEEAFTFSENGFISPENLGCLEAVVSLIKLLKTNEWSTVIDKCIHICLIKNGMDHMYHSFDVPKCFMGNPITRDINWVMFREFINSLPGTDIPPWNVMTENFKKKCIALINSKFETQRDFSEFTKLMKKEGGRSNIEFD
|
RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.
|
A5HEH4
|
GIF1_MAIZE
|
GRF-interacting factor 1 (ZmGIF1) (Protein ANGUSTIFOLIA 3 homolog)
|
MQQQHLMQMNQNMMGGYTSPAAVTTDLIQQYLDENKQLILAILDNQNNGKAEECERHQAKLQHNLMYLAAIADSQPPQTAPLSQYPSNLMMQPGPRYMPPQSGQMMNPQSLMAARSSMMYAHPSLSPLQQQQAAHGQLGMAPGGGGGGTTSGFSILHGEASMGGGGAGAGAGNNMMNAGMFSGFGRSGSGAKEGSTSLSVDVRGGTSSGAQSGDGEYLKVGTEEEGS
|
Transcription coactivator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences. Regulates shoot architecture and meristem determinacy. Binds to the inflorescence architecture gene UB3 (unbranched3). Regulates the expression of several genes involved in inflorescence architecture. Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (Probable). Associates with the core SWI/SNF chromatin-remodeling complex and specific GRFs to tightly regulate the transition between cell division and cell expansion in growing leaves.
|
A5HEI1
|
SCC2_ARATH
|
Sister chromatid cohesion protein SCC2 (Protein EMBRYO DEFECTIVE 2773) (Protein SISTER-CHROMATID COHESION 2) (AtSCC2)
|
MSNPSSSGLGSSSGLTHFGIGLANTVQSEVTPYLPLPSLPIFCGAAEPGEFKLFDEVGQGSGYRSLDRSEILAQSSRIANMLHETDVSYLDLRNEARAPDCNSGEHFQLYDLVLRCNPGAFEYVTPGPTCDPLFTNEGPQKIISEPSVPVKMQRQTDTHLARSIEPEPVKRVLRPNHVEDHSWQHETLTNQSPKDVTAYDSRPETITMNELSASKKPKGKKKRKDDLSSVQPDPSVLQESIVQNFCEMLEDFCGRAEVPGDDRDEAEWSSVPVDEVRVLINELMTIRSKMLLHMVPVDILSRLLRTLDHQIHRAEGLSIYSEHSDSDSVLLVLGALESIHASLAVMANSDMPKQLYKEEIIERILEFSRHQMMAVMSAYDPSYRTGSKPAENLAFEGDDDDDNPDHDMGSASKRRRIVKNSKVKKASVNRISGAVNTALQKLCTILGLLKDLLLVERLSDSCILQLLKTSITTFLVENIQILQLKAISLIGGIYNSYSQHRTYVIDEISQLLWKLPSSKRALRAYLLPDEEQRQIQMVTALLIQLVHNSTSLPETSRQAASGNSILETSVDVGYLTKCHEAATETCCLFWTRVLERFTSFKGQDASEIKLIIENLVMDLLTALNLPEYPSVSPILEVLCVILLHNAGLKSKDVSARIMAIELLGTIAARLKRDAVLCSKDRFWTLLESDSEISVDQVCTKDCTFCLGKRAGNLLVCQICQRRFHGDCLGLKELDISSRNWHCPLCVCKRQLLVLQSYCKTDTKGTGKLESEESIENPSMITKTEVVQQMLLNYLQDVGSADDVHTFICWFYLCLWYKDVPKSQNKFKYYIARLKAKSIIRNSGATTSFLTRDAIKQITLALGMNSSFSRGFDKILNMLLASLRENAPNIRAKALRAVSIIVEADPEVLCDKRVQLAVEGRFCDSAISVREAALELVGRHIASHPDVGIKYFEKVAERIKDTGVSVRKRAIKIIRDMCTSNPNFSEFTSACAEILSRISDDESSVQDLVCKTFYEFWFEEPPGHHTQFASDASSIPLELEKKTKQMVGLLSRTPNQQLLVTIIKRALALDFFPQAAKAAGINPVALASVRRRCELMCKCLLEKILQVEEMSREEGEVQVLPYVLVLHAFCLVDPGLCTPASDPTKFVITLQPYLKSQADSRTGAQLLESIIFIIDSVLPLIRKLPLSVTEDLEQDLKHMIVRHSFLTVVHACVRCLCSVSKLAGKGVSIVEHLLQFFFKRLEAQGSDNTQIAGRSLFCLGLLIRHGNSLISTSGGKNFNLSGCLNLFKRHLRTEDIALKVRSLQALGFILIARPEYMLEEDIGKIIETTLADEANGRMKMQALQNMYEYLLDAEKQLGSEKASDNTVNSVEQGGHNVPVAAGAGDTNICGGIVQLFWDKILGRCLDFDDQIRQTSLKIVEVVLRQGLVHPITCVPYLIALETDPQEANQKLAHHLLMNMHEKYPAFFESRLGDGLQMSFIFMQSISQVTSEPNQSLQQKGSTNMLGKNDHASSTLTQARLGVSRIYKLIRGNRVSRNKFMTSIVRKFDNPTWNGSVISFLKYCTETLALLPFTSPDEPLYLVYSINRVMQIRAGAVESNLKALLHKDSAKTQHGNGAYQQDPIPGHMNMMDLNTRIQEEPRHWNSYGHATLIDLNGSVYQDSRDQFTSYQVHNGKADVHKMTSSDPPELSTDDLQKIQVDCLAAIAIQLLLKLKRYLKVTYSLNDDRCQAYSPTEPLKPGDPLSRQSVAFDLSETRTDLPSTYQDLVQRYQEFKNAMREDTVDFTIYSTNVKRKRPTPRKTSRSAKKTVAYNEDDDDDDNDDRGWHGGGGRGAARRLNYSTRSSNRR
|
Essential protein required for cell fate determination during embryogenesis. Involved in sister chromatid cohesion during meiosis and mitosis. Forms a complex with SCC4, which is required for the association of the cohesin complex with chromosomes. Plays a structural role in chromatin, especially in centromere organization, chromosomal axis formation, and distribution of the cohesin subunit SCC3 on chromosomes.
|
A5HJM1
|
IL7RA_CALJA
|
Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127)
|
MTILGTTFGVFFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNTTNLEFEICGALVEVRCLNFRKLQEIYLIETKKFLLIGNSNICVKAGEKSLTCKNVNVATIVKPEAPFDLSVIYREGANDFLVTFNTSHLQKKYVKVLMHDVAYRHEKDENNWMHVNLSSTKLTLLQRKLQPKATYEIKVRSIPGDYFKGFWSEWSPSYYFRTPEINNHSGETNPTLLTISILSVLSVVLLVILACVLWKKRIKPIIWPSLPDHKKTLEHLCKKPSKNLIVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTVPPQLEESETQRPGGDVQSPSWPSENVVTTPETFGRDSPLRCLAGNVSAHDAPILSSSRSLDCRESATNGPHVNQDLLLSLGTTNSTLPPSFPPQSRILTLNPVAQGQPILTFLGSNKEEAYVTMSSFCQKR
|
Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP) (By similarity).
|
A5HNV6
|
DCAMP_TRYBB
|
Inactive S-adenosylmethionine decarboxylase prozyme (AdoMetDC prozyme)
|
MSVTRINQQTECPSSVHDLVSCWGGCTQSKTSTDSGLEKRFELNFAQPVDIGTVTVKQLASVMERAGESLRQNSAELGIHTLKFDRSLLVFTAKQIVVRSSVSVMLHEAVHPMLELMRSHNIIVDWASFMRVNYGSPWDMTSETSDIMAHEYAELKSAFPTGHPYLAGPVDRDHCFYFVYDGIDRDPSSCRRENDVQINVYMYNVQADDEYDLDGNTKEQQLLVSHCAGEYETLRVSTYGSTHPFASFETNAVSAASDITKIVNGLLKKFYPERVLLVLLQDRDAQGTTACGVMDRLEGFTVVHRGANHFGGGYVFHQATYARSA
|
Probably has no catalytic activity due to the loss of several residues required for processing and catalysis. Forms a complex with S-adenosylmethionine decarboxylase AdoMetDC which is essential to activate AdoMetDC. Required for the biosynthesis of the polyamine spermidine. Required for growth and survival during the bloodstream life cycle stage.
|
A5IQA5
|
HCHA_STAA9
|
Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
|
MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK
|
Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.