Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O02228 | SC5A7_CAEEL | MADLLGIVAIVFFYVLILVVGIWAGRKSKSSKELESEAGAATEEVMLAGRNIGTLVGIFTMTATWVGGAYINGTAEALYNGGLLGCQAPVGYAISLVMGGLLFAKKMREEGYITMLDPFQHKYGQRIGGLMYVPALLGETFWTAAILSALGATLSVILGIDMNASVTLSACIAVFYTFTGGYYAVAYTDVVQLFCIFVGLWVCVPAAMVHDGAKDISRNAGDWIGEIGGFKETSLWIDCMLLLVFGGIPWQVYFQRVLSSKTAHGAQTLSFVAGVGCILMAIPPALIGAIARNTDWRMTDYSPWNNGTKVESIPPDKRNM... | null | null | acetylcholine biosynthetic process [GO:0008292]; choline transport [GO:0015871] | axon [GO:0030424]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021] | choline transmembrane transporter activity [GO:0015220]; choline:sodium symporter activity [GO:0005307] | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion and chloride ion dependent. {ECO:0000269|PubMed:10649566}. | Caenorhabditis elegans |
O02274 | ZTF11_CAEEL | MSSISNNPDFSSIDPAVLMSLLMKSSGSLPTPPDTHSDGSESPDSTASDSSDKKRRRKPESKDIVRVAEEAEAAAATCSSIPSSSDTKENETEEDQNMTCDTTTNNAQKPTEQTATSADVVTSSVPSGLEGVPSFLFSQFMAPSFQKQLEIFTSGNMMSATHSDTSPSDVDSVLDGGVVTAEETSSSKSPMMTSSDTPKTPLTASSPPHSSGSESRVMSPITHTNISDELSISTTPTVAFTPNGSIPSPGTGYSWSIRREGKLACPTPGCDGSGHQTGLYTHHRSLSGCPRRPDKTVIQMLALRQDTVLRCTTAGCSGKG... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode larval development [GO:0002119]; neuron development [GO:0048666]; neuron fate determination [GO:0048664]; neuron fate specification [GO:0048665]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transdiffe... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF01530; | 4.10.320.30; | MYT1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31386623}. | null | null | null | null | null | FUNCTION: Transcriptional repressor which promotes neuronal differentiation during embryonic and postembryonic neurogenesis (PubMed:31386623). Together with components of the MuvB corepressor complex, negatively regulates the expression of non-neuronal genes during neurogenesis (PubMed:31386623). Required for the gener... | Caenorhabditis elegans |
O02279 | NHR62_CAEEL | MFSTLSPSAIDDILRHAVHFGQGTTAIAPSPVTFISTTTQQSLGATYPGVFNPTTPTFNHYQHQALPVTMHTSTSSAHHTTTGHGRGRRKNSTINLVCVVCGDQAFGKHYGVNACNGCKGFFRRSVWHNRQYLCRFEGRCAIAKEHRNVCRACRLKQCFVAGMNPRAVQSERVEREQNGSPNQIEEDDYKDLSSPDTCSVEIQTDVDEQKPSSNNSAPLPSMELEMAKLSEQIVEMHRAVCSYVDPVTKRENFDMKMETETTKIAFMNAFYNPEMIGPRTPLDITGRRVATVKDVMDEWKRNFVLFSDWLRALPEYNQMS... | null | null | autophagy [GO:0006914]; lipid metabolic process [GO:0006629]; regulation of DNA-templated transcription [GO:0006355]; response to starvation [GO:0042594]; triglyceride metabolic process [GO:0006641] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:23935515}. | null | null | null | null | null | FUNCTION: Orphan nuclear hormone receptor (PubMed:23935515). Required for metabolic and physiologic responses associated with dietary-restriction-induced longevity (PubMed:23935515). Modulates triglyceride and lipid metabolism and autophagy, associated with dietary-restriction, probably acting via regulation of transcr... | Caenorhabditis elegans |
O02298 | GCY35_CAEEL | MFGWIHESFRQLVTRKYGKDIWEKIVHMSKFELGTESEIAHYYNDDETLRLVNSMANVIGIPIEEIWEAYGGFLIQFTMETGWDELLRAMAPDLEGFLDSLDSLHYFIDHVVYKTKLRGPSFRCDVQADGTLLLHYYSKRSGLYPIVKGVVREVARRIYDTEVVMKVQERKQEHLDAFVTEHVVFVITQIENANSTQPKSISSKADSQIDLSTGIYEISSSDFSLAFPYHICFDPDLFVEHFGNFIKKTFPNAMRQETRVTDLLELVHPEVPFSYESIKYYKNSLFVFRLKGLGDIVHNANDEAKTVLLKGSMVFIDEGK... | 4.6.1.2 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305}; Note=Binds 1 or 2 heme groups per heterodimer. {ECO:0000305}; | aerotaxis [GO:0009454]; behavior [GO:0007610]; cGMP-mediated signaling [GO:0019934]; defense response to Gram-negative bacterium [GO:0050829]; response to hyperoxia [GO:0055093]; response to oxygen levels [GO:0070482] | dendrite [GO:0030425]; guanylate cyclase complex, soluble [GO:0008074]; neuronal cell body [GO:0043025] | carbon monoxide binding [GO:0070025]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitric oxide binding [GO:0070026]; oxygen binding [GO:0019825]; oxygen sensor activity [GO:0019826] | PF00211;PF07700;PF07701; | 6.10.250.780;3.90.1520.10;3.30.450.260;3.30.70.1230; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:29879119}. Note=Enriched localization at the URX dendrite ending. {ECO:0000269|PubMed:29879119}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; | null | null | null | null | FUNCTION: Plays a central role in social feeding behavior and oxygen sensation by synthesizing 3',5'-cyclic guanosine monophosphate (cGMP) from GTP. Oxygen, which binds to its heme-binding sites, probably regulates social behavior by modulating its activity. cGMP is a common second messenger in sensory transduction and... | Caenorhabditis elegans |
O02324 | FABP8_CAEEL | MVSMKEFIGRWKLVHSENFEEYLKEIGVGLLIRKAASLTSPTLEIKLDGDTWHFNQYSTFKNNKLAFKIREKFVEIAPDERSYNTLVTFENGKFISHQDKIKENHHSSVFTTWLENGKLLQTYQSGSVICRREFVKE | null | null | fatty acid transport [GO:0015908]; lipid transport [GO:0006869]; long-chain fatty acid transport [GO:0015909] | cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634] | fatty acid binding [GO:0005504]; lipid binding [GO:0008289]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:25554789}. Nucleus {ECO:0000269|PubMed:25554789}. | null | null | null | null | null | FUNCTION: Lysosomal lipid chaperone which binds to a wide range of unsaturated fatty acids, including high affinity binding to oleic acid and oleoylethanolamide, to transport them into the nucleus (PubMed:25554789, PubMed:31292465). As part of a lysosome-to-nucleus retrograde lipid signaling pathway, translocates into ... | Caenorhabditis elegans |
O02326 | CFI1_CAEEL | MSVRIDEPQLFVSMSKEPTQETVNVGGHHDDSSSNCDERVDDQTEEQKSPPASPDLTANLNVFDLESRQKVVQRLLNSQLNLSNLRAPLNLPPIFQALQGPFSIQQQLLGLASGLTAISPGLDDYDEENTNQGEPEDLTLGGFRKETSVKSEEPSESGINASGPAWSYEEQFKQLYELSDDVKRKEWLDDWLNFMHRIGKPVTRIPIMAKQVLDLYELYRLVVQHGGLVEIINKKLWREITKGLNLPSSITSAAFTLRTQYQKYLYDYECEKEKLSNQSDLQQAIDGNRREAPGRRTAPSFPLPFQLPHAASAAATMLNN... | null | null | cell fate commitment [GO:0045165]; cell fate specification [GO:0001708]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcriptio... | nucleus [GO:0005634] | DNA binding [GO:0003677]; sequence-specific DNA binding [GO:0043565] | PF01388; | 1.10.150.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:11959845}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:11959845, PubMed:28056346). Regulates neuronal subtype identity (PubMed:11959845, PubMed:28056346). Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor n... | Caenorhabditis elegans |
O02365 | IFA2_CAEEL | MTDPDSYRSSITSRPSFNRTVTSSSQNYGAPGSGNRVLKIVTETHSSSVSSGLSPYGQNAASTIRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQIMNGNRNDMESWYQLRVQEINTQSNRQNA... | null | null | cell-cell adhesion [GO:0098609]; heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | hemidesmosome [GO:0030056]; intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652] | structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Cell junction, hemidesmosome {ECO:0000269|PubMed:14597206}. Note=Colocalizes with myoactin. | null | null | null | null | null | FUNCTION: Cytoplasmic intermediate filaments provide mechanical strength to cells. Essential protein, involved in attachment structures in epidermal cells that connect muscles to the external cuticle. Probably acts by forming hypodermal hemidesmosome complexes that help mediate muscle-cuticle force transduction. Althou... | Caenorhabditis elegans |
O02372 | OB76A_DROME | MKHWKRRSSAVFAIVLQVLVLLLPDPAVAMTMEQFLTSLDMIRSGCAPKFKLKTEDLDRLRVGDFNFPPSQDLMCYTKCVSLMAGTVNKKGEFNAPKALAQLPHLVPPEMMEMSRKSVEACRDTHKQFKESCERVYQTAKCFSENADGQFMWP | null | null | courtship behavior [GO:0007619]; olfactory behavior [GO:0042048]; response to ethanol [GO:0045471]; response to pheromone [GO:0019236]; sensory perception of smell [GO:0007608] | extracellular region [GO:0005576] | dibutyl phthalate binding [GO:0035275]; diphenyl phthalate binding [GO:0035274]; odorant binding [GO:0005549]; pheromone binding [GO:0005550] | PF01395; | 1.10.238.20; | PBP/GOBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9755202}. | null | null | null | null | null | FUNCTION: Odorant-binding protein required for olfactory behavior and for activity of pheromone-sensitive neurons. Binds to alcohols and mediates avoidance behavior to high concentrations of alcohols, the alcohol-binding possibly resulting in activation of receptors on T2B neurons, the activation of these receptors inh... | Drosophila melanogaster (Fruit fly) |
O02373 | UGDH_DROME | MKVCCIGAGYVGGPTCAVMALKCPDIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADLIFISVNTPTKTCGNGKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRANQKPGIHYDILSNPEFLAEGTAINDLLNADRVLIGGEETPEGHQAVEKLSWIYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAYWQQVIDMNEYQKRRFSQKIIESLFN... | 1.1.1.22 | null | chondroitin sulfate biosynthetic process [GO:0030206]; epithelial cell migration, open tracheal system [GO:0007427]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic... | nucleus [GO:0005634] | NAD binding [GO:0051287]; UDP-glucose 6-dehydrogenase activity [GO:0003979] | PF00984;PF03720;PF03721; | 1.20.5.100;3.40.50.720; | UDP-glucose/GDP-mannose dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000269|PubMed:9217004}; | null | PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. {ECO:0000269|PubMed:9217004}. | null | null | FUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate and heparan sulfate. Required for wingless signaling in different tissues. {ECO:0000269|PubMed:9217004, ECO:0000269|PubMed:9272947, ECO:0000269|PubMed:9342049}. | Drosophila melanogaster (Fruit fly) |
O02466 | ILPR_BRALA | MRVVDKMAGLMWAALTLVIGLGLLVPSNGEEYICDSMDIRNRVSNLRQLENCTVIEGYLQILLIDFAEEQDYSGLAFPNLVEITDYFLLYRVRGLTNLSELFPNLAVIRGTNLFFNYALVVFEMLDMQKIGLYSLQNITRGSVRIEKNPNLCYLDTIDWSFIAESGYSNNFIVDNREEEECVNFCPGRCRIKHPVLQDLCWAEEHCQKVCPESCLGNCRDGISGCCHENCIGGCDGPTERDCVACKYFVHNGECLIQCPPDTYQYKDRRCITEEECPNTTNSVWKLHHRKCIPECPSGYTTDINNPRLCTECEGQCPKSC... | 2.7.10.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | glucose homeostasis [GO:0042593]; phosphorylation [GO:0016310]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897] | axon [GO:0030424]; insulin receptor complex [GO:0005899] | ATP binding [GO:0005524]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; metal ion binding [GO:0046872]; phosphatidylinositol 3-kinase binding [GO:0043548] | PF00041;PF00757;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This receptor binds to the insulin related peptide and has a tyrosine-protein kinase activity. | Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum) |
O02482 | UNC37_CAEEL | MKASYLETLDRIKDEHAEMSKHVNQQRSDIEKVALEKENMNRSYMTYAEVSNTLRSDLRKAEEINKRLQEFIMQSLAPQLSQDNQANCLAALEAFKTASPRENGNGAPALPPGFPPGAAGMLGMMPNMPFGMSPAMSQLFNQFASPHVNGGDGAGGSSGGASEAKKAKLEDPDDGELEIDVTNDDHPSTASNGGAANKNGRDSTNSVASSGASTPSIASNSRARQQQQPLAGLQGLEQMNFLAGFNPNLLRQASAAGGFNFLNDPHAQARLAAAIGQIGSRPAYSFKIVDGGVPTPTSFPPDAQKGPGIPTGLKKKMELN... | null | null | chemical synaptic transmission [GO:0007268]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of axonogenesis [GO:0050770]; regulation of synapse structure or activity [GO:0050803] | nucleus [GO:0005634]; synapse [GO:0045202]; transcription regulator complex [GO:0005667] | RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714] | PF03920;PF00400; | 2.130.10.10; | WD repeat Groucho/TLE family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional corepressor that functions with the neural specificity gene unc-4 to govern motor neuron identity (PubMed:10557206, PubMed:17289921, PubMed:9165118). In concert with unc-4, represses the expression of VB-specific genes such as ceh-12, thereby preventing the adoption of VB motor neuron fate (Pu... | Caenorhabditis elegans |
O02495 | SYB1_CAEEL | MDAQGDAGAQGGSQGGPRPSNKRLQQTQAQVDEVVGIMKVNVEKVLERDQKLSQLDDRADALQEGASQFEKSAATLKRKYWWKNIKMMIIMCAIVVILIIIIVLWAGGK | null | null | defecation [GO:0030421]; nematode larval development [GO:0002119]; regulation of hindgut contraction [GO:0043134]; regulation of nematode pharyngeal pumping [GO:0043051]; SNARE complex assembly [GO:0035493]; synaptic transmission, cholinergic [GO:0007271]; synaptic vesicle exocytosis [GO:0016079]; vesicle fusion [GO:00... | axon [GO:0030424]; cortical granule [GO:0060473]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905] | PF00957; | 1.20.5.110; | Synaptobrevin family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}. Cell membrane {EC... | null | null | null | null | null | FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Acts in neuronal exocytosis of synaptic transmission. Likely to have a role in cholinergic transmisson. Required for viability, coordinated movement and M3 pharynx motor neuron function. {ECO:0000269|PubMed:9412487}. | Caenorhabditis elegans |
O02604 | DRTS_PLAVI | MEDLSDVFDIYAICACCKVAPTSEGTKNEPFSPRTFRGLGNKGTLPWKCNSVDMKYFSSVTTYVDESKYEKLKWKRERYLRMEASQGGGDNTSGGDNTHGGDNADKLQNVVVMGRSSWESIPKQYKPLPNRINVVLSKTLTKEDVKEKVFIIDSIDDLLLLLKKLKYYKCFIIGGAQVYRECLSRNLIKQIYFTRINGAYPCDVFFPEFDESQFRVTSVSEVYNSKGTTLDFLVYSKVGGGVDGGASNGSTATALRRTAMRSTAMRRNVAPRTAAPPMGPHSRANGERAPPRARARRTTPRQRKTTSCTSALTTKWGRKT... | 1.5.1.3; 2.1.1.45 | null | dTMP biosynthetic process [GO:0006231]; methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate biosynthetic process [GO:0046654] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | dihydrofolate reductase activity [GO:0004146]; thymidylate synthase activity [GO:0004799] | PF00186;PF00303; | 3.40.430.10;3.30.572.10; | Dihydrofolate reductase family; Thymidylate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000269|PubMed:16135570}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methyle... | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. | null | null | FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. | Plasmodium vivax |
O02626 | MADD_CAEEL | MNDKEKEICPRLIDFLVVVGKRNRTRGASQSSPDATTDTTVTYPEILRRYPTDDHKDFILPTDVTVFCQPEGCTTTSARLRKNARNDPQFFVFMLTEKDSAKVRYGICLNFYQSFDRRSTPKDEIKKVPDDAHHKKRDSHVSLTSLCFISHHPFVSIFHQVLLLLKRIIDSSNHRAAQRTGLKDVVWAILTGHYNEPIVPEVMKEIKEIETWILMLLSSPVPVPGKTKVQIEVMPMDLSQVFEFALPDHTRFTLIDFPLHIPFEILGIDMALRVLTAAMLEFKIVIQSRNYNAVSMCILSIVALLYPLEYMFPVIPLLPA... | null | null | apoptotic process [GO:0006915]; chemical synaptic transmission [GO:0007268]; defecation [GO:0030421]; egg-laying behavior [GO:0018991]; lipid transport involved in lipid storage [GO:0010877]; mating [GO:0007618]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of ante... | cytosol [GO:0005829]; plasma membrane [GO:0005886]; synapse [GO:0045202] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF02141;PF03456; | 3.30.450.200;3.40.50.11500; | MADD family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}. | null | null | null | null | null | FUNCTION: Guanyl-nucleotide exchange factor that regulates small GTPases (By similarity). Converts GDP-bound inactive form of rab-3 and cab-1 to the GTP-bound active forms. Regulator of presynaptic activity that interacts with rab-3 to regulate synaptic vesicle release (PubMed:10970871, PubMed:9136770). Is also a regul... | Caenorhabditis elegans |
O02649 | CH60A_DROME | MFRLPVSLARSSISRQLAMRGYAKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIELKDKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKEGFEKISKGANPVEIRRGVMLAVETVKDNLKTMSRPVSTPEEIAQVATISANGDQAIGNLISEAMKKVGRDGVITVKDGKTLTDELEVIEGMKFDRGYISPYFINSSKGAKVEFQDALLLLSEKKISSVQSIIPALELANAQRKPLVIIAEDIDGEALSTLVVNRLKIGLQVAAVKAPGFGDNRKSTLTDMAIASGGIV... | null | null | apoptotic mitochondrial changes [GO:0008637]; cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; mitochondrion organization [GO:0007005]; positive regulation of interferon-alpha production [GO:0032727]; positive regu... | GroEL-GroES complex [GO:1990220]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
O02655 | DCAM_CAEEL | MSATSATNFAVQTHPVKAPDEEYFFEGAEKLLELWFCSSTQNETRSLRIIPREEIDAMLDIARCKILHSKHNESIDSYVLSESSLFISDNRVILKTCGTTRLLAALPVIMQLAGAYAGLDQVQSVYYSRKNFLRPDLQPSLHKNFDAEVEYLDSFFVDGHAYCLGSLKQDRWYLYTFHREVEFPAHKQPDHTLEILMSDLDEEVLHKFTKDYAVDGNDCFMRAGIDKIIPAGADVHDELFDPCGYSMNAYMNDTDQYATIHVTPEKAFSFASFETNQDLVCLYSQTRKVLQCFRPNKILMTVFANDISEKGKDAQQQLWD... | 4.1.1.50 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250|UniProtKB:P17707}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250|UniProtKB:P17707}; | spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597] | cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; putrescine binding [GO:0019810] | PF01536; | 3.60.90.10; | Eukaryotic AdoMetDC family | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | null | CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000269|PubMed:9841864, ECO:0000305|PubMed:19762559}; | null | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269|PubMed:9841864}. | null | null | FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. {ECO:0000269|PubMed:19762559}. | Caenorhabditis elegans |
O02658 | GLC7C_CAEEL | MTAPMDVDNLMSRLLNVGMSGGRLTTSVNEQELQTCCAVAKSVFASQASLLEVEPPIIVCGDIHGQYSDLLRIFDKNGFPPDVNFLFLGDYVDRGRQNIETICLMLCFKIKYPENFFMLRGNHECPAINRVYGFYEECNRRYKSTRLWSIFQDTFNWMPLCGLIGSRILCMHGGLSPHLQTLDQLRQLPRPQDPPNPSIGIDLLWADPDQWVKGWQANTRGVSYVFGQDVVADVCSRLDIDLVARAHQVVQDGYEFFASKKMVTIFSAPHYCGQFDNSAATMKVDENMVCTFVMYKPTPKSMRRG | 3.1.3.16 | null | amoeboid sperm motility [GO:0097723]; cell differentiation [GO:0030154]; egg-laying behavior [GO:0018991]; male meiosis chromosome segregation [GO:0007060]; regulation of pseudopodium assembly [GO:0031272]; reproduction [GO:0000003]; spermatogenesis [GO:0007283] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; pseudopodium [GO:0031143] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149;PF16891; | 3.60.21.10; | PPP phosphatase family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:16943775}. Cell projection, pseudopodium {ECO:0000269|PubMed:22042574}. Cytoplasm {ECO:0000269|PubMed:22042574}. Note=Co-localizes with MSP in oblong stripes in the cytoplasm of inactive sperm and in the pseudopodium in activated sperm. {ECO:0000269|PubMed:22042574}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|RuleBase:RU004273}; CATALYTIC ACTIVITY: Reaction... | null | null | null | null | FUNCTION: Probable phosphatase which plays a redundant role with gsp-4 in spermatogenesis by regulating sister chromatid segregation during meiosis (PubMed:16943775, PubMed:22042574). In addition, involved in sperm motility by controlling the dynamic disassembly of major sperm proteins (MSP) in the spermatozoan pseudop... | Caenorhabditis elegans |
O02662 | ADRB3_CANLF | MAPWPHGNGSVASWPAAPTPTPDAANTSGLPGAPWAVALAGALLALEVLATVGGNLLVIVAIARTPRLQTMTNVFVTSLATADLVVGLLVVPPGATLALTGRWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSKWWRVGADAEAQRCHSNPHCCAFASNIPYALLSSSVSFYLPLLVMLFVYARVFLVATRQLRLLRRELGRFPPAESPPAASRSRSPGPARRCASPAAVPSDRLRPARLLPLREHRALRTLGLIVGTFTLCWLPFFVANVMRALGGP... | null | null | activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting serotonin receptor signaling pathway [GO:0007198]; chemical synaptic transmission [GO:0007268]; G protein-coupled receptor signaling pathway, coupled to cy... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202] | beta-adrenergic receptor activity [GO:0004939]; beta3-adrenergic receptor activity [GO:0015052]; epinephrine binding [GO:0051379]; G protein-coupled serotonin receptor activity [GO:0004993]; neurotransmitter receptor activity [GO:0030594]; protein homodimerization activity [GO:0042803]; serotonin binding [GO:0051378] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB3 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis. | Canis lupus familiaris (Dog) (Canis familiaris) |
O02671 | LEPR_PIG | MTCPKFSVALLHWEFIYVITAFDLAYPITPWKFKLSCMPPNTTYDFLLPAGISKNTSTLNGHDEAVVETELNSSGTYLSNLSSKTTFHCCFWSEEDKNCSVHADNIAGKAFVSAVNSLVFQQTGANWNIQCWMKEDLKLFICYMESLFKNPFKNYDLKVHLLYVLLEVLEGSPLLPQKGSFQSVQCNCSARECCECHVPVSAAKLNYTLLMYLKITSGGAVFHSPLMSVQPINVVKPDPPLGLHMEITDTGNLKISWSSPTLVPFQLQYQVKYSENSTTNMREADEIVSDTSLLVDSVLPGSSYEVQVRGKRLDGPGIWS... | null | null | angiogenesis [GO:0001525]; bone growth [GO:0098868]; cytokine-mediated signaling pathway [GO:0019221]; energy homeostasis [GO:0097009]; glucose homeostasis [GO:0042593]; leptin-mediated signaling pathway [GO:0033210]; negative regulation of autophagy [GO:0010507]; phagocytosis [GO:0006909]; regulation of bone remodelin... | basolateral plasma membrane [GO:0016323]; external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; leptin receptor activity [GO:0038021] | PF06328;PF18589; | 2.60.40.10; | Type I cytokine receptor family, Type 2 subfamily | PTM: On ligand binding, phosphorylated on two conserved C-terminal tyrosine residues by JAK2. Tyr-986 is required for complete binding and activation of PTPN11, ERK/FOS activation,for interaction with SOCS3 and SOCS3 mediated inhibition of leptin signaling. Phosphorylation on Tyr-1141 is required for STAT3 binding/acti... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane {ECO:0000250|UniProtKB:P48357}. | null | null | null | null | null | FUNCTION: Receptor for hormone LEP/leptin (By similarity). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake ... | Sus scrofa (Pig) |
O02691 | HCD2_BOVIN | MAAACRSVKGLVALITGGASGLGLATAERLVGQGATAVLLDLPNSDGETQAKKLGKSCAFAPADVTSEKDVQAALTLAREKFGRVDVAVNCAGIAVASKTYNLKKSQAHTLEDFQRVINVNLIGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPMGIRVMTIAPGLFGTPLLTTLPDKVRNFLASQVPFPSRLGDPAEYAHLVQAIIENSFLNGEVIRLDGAIRMQP | 1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62 | null | androgen metabolic process [GO:0008209]; bile acid biosynthetic process [GO:0006699]; brexanolone metabolic process [GO:0062173]; C21-steroid hormone metabolic process [GO:0008207]; estrogen metabolic process [GO:0008210]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; isoleucine cat... | cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739] | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0044594]; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity [GO:010... | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q99714}. | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | null | PATHWAY: Amino-acid degradation; L-isoleucine degradation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:Q9971... | null | null | FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism. Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the... | Bos taurus (Bovine) |
O02695 | PTPR2_MACNE | MALPLLLLLLLLLPPRVLPAAPSSVPHGRQLPGRLGCLLEEGLCGASEACVNDGVFGRCQKVPAMDFYRYEVSPVALQRLRVALQKLSGTGFTWQDDYTQYVMDQELADLPKTYLRHPEASGPARPSKHSIGSERRYSQEGGAALAKAFRRHLPFLEALSQAPASDALARTRMAQDRPRAEGDDRFSKSILTYVAHTSVLTYPPGPQAQLPEDLLPRTLSQLQPDELSPKVDSSVERHHLMAALSAYAAQRPPAPPGKGSLEPQYLLRAPSRMPRPLLSPAVPQKWPSPLGDPEDPPSTGEGARIHTLLKDLQRQPAEAR... | 3.1.3.-; 3.1.3.48 | null | dephosphorylation [GO:0016311]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; lipid metabolic process [GO:0006629]; neurotransmitter secretion [GO:0007269]; regulation of secretion [GO:0051046] | secretory granule membrane [GO:0030667]; synaptic vesicle membrane [GO:0030672] | protein tyrosine phosphatase activity [GO:0004725] | PF11548;PF14948;PF00102; | 3.90.190.10;3.30.70.2470; | Protein-tyrosine phosphatase family, Receptor class 8 subfamily | PTM: Subject to proteolytic cleavage at multiple sites. {ECO:0000250|UniProtKB:P80560}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P80560}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P80560}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P80560}; Single-pass type I membrane protein {ECO:0000250|Uni... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in res... | Macaca nemestrina (Pig-tailed macaque) |
O02696 | PI3R5_PIG | MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLAPLALLFYSTVLCTPHFPPDSDLLLKAARTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLSTRSHRSSTVTVLLLNPVEVQAEFLDVADKLSTPGPSPHSAYITLLLHAFQATFGAHCDLSGLHRRLQSKTLAELEAIFTETAEAQELASGIGDAAEARQWLRTKLQAVGEKAGFPGVLDTAKPGKLRTIPIPVARCYTYSWNQDSFDILQEILLKEQELLQPEILDDE... | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897] | cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IB [GO:0005944]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; G-protein beta/gamma-subunit complex binding [GO:0031683] | PF10486; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}. Cytoplasm {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}. Cell membrane {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}; Peripheral membrane protein {ECO:0000305|PubMed:12507995}. Note=Predominantly localize... | null | null | null | null | null | FUNCTION: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG. {ECO:0000269|PubMed:12507995}. | Sus scrofa (Pig) |
O02697 | PK3CG_PIG | MELENYEQPVVLREDNRRRRRRMKPRSTAASLSSMELIPIEFVLPTSQRNTKTPETALLHVAGHGNVEQMKAQVWLRALETSVSADFYHRLGPDHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKVLHRSPGQIHVVQRHAPSEETLAFQRQLNALIGYDVTDVSNVHDDELEFTRRRLVTPRMAEVAGRDPKLYAMHPWVTSKPLPEYLLKKITNNCVFIVIHRSTTSQTIKVSADDTPGTILQSFFTKMAKKKSLMDIPESQNERDFVLRVCGRDEYLVGETPIKNFQWVRQCLKNGEEIHLVLDTPPDPALDEVRK... | 2.7.1.137; 2.7.1.153; 2.7.1.154; 2.7.11.1 | null | angiogenesis [GO:0001525]; cell migration [GO:0016477]; chemotaxis [GO:0006935]; endocytosis [GO:0006897]; immune system process [GO:0002376]; inflammatory response [GO:0006954]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phospha... | cytoplasm [GO:0005737]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; phosphatidylinositol 3-kinase complex, class IB [GO:0005944]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00454;PF00792;PF00794;PF00613;PF19710; | 3.10.20.770;2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | PTM: Autophosphorylation at Ser-1101 has no effect on the phosphatidylinositol-4,5-bisphosphate 3-kinase activity. {ECO:0000250|UniProtKB:P48736}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48736}. Cell membrane {ECO:0000250|UniProtKB:P48736}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.1... | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. | null | null | FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades inv... | Sus scrofa (Pig) |
O02703 | BAX_BOVIN | MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGETPELGLEQVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAAEMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic mitochondrial changes [GO:0008637]; apoptotic signaling pathway [GO:0097190]; B cell apoptotic process [... | BAX complex [GO:0097144]; Bcl-2 family protein complex [GO:0097136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; mitochondrial permeability transition pore complex [GO:0005757]; mitochondrion [G... | BH3 domain binding [GO:0051434]; channel activity [GO:0015267]; lipid binding [GO:0008289]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00452; | 1.10.437.10; | Bcl-2 family | PTM: Ubiquitinated on Lys-128 and Lys-190. 'Lys-63'-linked polyubiquitin chains on Lys-128 are removed by USP12. {ECO:0000250|UniProtKB:Q07812}. | SUBCELLULAR LOCATION: [Isoform Alpha]: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}. Nucleus {ECO:0000250|UniProtKB:Q07812}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a c... | null | null | null | null | null | FUNCTION: Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, u... | Bos taurus (Bovine) |
O02705 | HS90A_PIG | MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTND... | 3.6.4.10 | null | activation of innate immune response [GO:0002218]; cellular response to heat [GO:0034605]; cellular response to virus [GO:0098586]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of nitric oxide biosynthetic proc... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; nitric-oxide synthase regulator activity [GO:0030235]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: ISGylated. {ECO:0000250|UniProtKB:P07900}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000250|UniProtKB:P07900}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome {ECO:0000250|UniProtKB:P07900}. Cell membrane {ECO:0000250|UniProtKB:P07900}. Mitochondrion {ECO:0000250|UniProtKB:P07900}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P07900}; | null | null | null | null | FUNCTION: 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... | Sus scrofa (Pig) |
O02713 | S22A2_PIG | MLTVDDILEHTGEFNFFQKQTFFLLALLSAAFTPIYVGIVFLGFIPDHRCRSPGVAELSQRCGWSLAEELNYTVPGPGPAGQAFPRQCRRYEVDWNQSTLGCVDPLAGLAANSSHLPLGPCRYGWVYDTPGSSIVTEFDLVCANSWLLDLFQSAVNVGFFIGSVGIGYIADRFGRKLCLLLTILINAVSGVLMAISPTYTWMLVFRLIQGLVSKAGWMIGYILITEFVGLSYRRTVGIFYQVAFTFGLLVLAGVAYALPHWRWLQFTVTLPNFCFLFYYWCVPESPRWLISQNKNAKAMSIIKHIAKKNGKSLPASLQSL... | null | null | acetylcholine transport [GO:0015870]; dopamine transport [GO:0015872]; epinephrine transport [GO:0048241]; histamine transport [GO:0051608]; monoatomic ion transport [GO:0006811]; norepinephrine transport [GO:0015874]; organic cation transport [GO:0015695]; prostaglandin transport [GO:0015732]; putrescine transport [GO... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323] | acetylcholine transmembrane transporter activity [GO:0005277]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prost... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:O15244}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9R0W2}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000250|UniProtKB:Q9R0W2}; CATALYTI... | null | null | null | null | FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Functions as a Na(+)-independent, bidirectional uniporter. Cation cellular uptake or release is driven by the electrochemical potential, i... | Sus scrofa (Pig) |
O02718 | BCL2_BOVIN | MAHAGGTGYDNREIVMKYIHYKLSQRGYEWDAGDAGAAPPGAAPAPGILSSQPGRTPAPSRTSPPPPPAAAAGPAPSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARERFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDSIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKALLSLALVGACITLGAYLGHK | null | null | extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of cellular pH reduction [GO:0032848]; negative... | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965] | protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00452;PF02180; | 1.10.437.10; | Bcl-2 family | PTM: Phosphorylation/dephosphorylation on Ser-63 regulates anti-apoptotic activity. Growth factor-stimulated phosphorylation on Ser-63 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle (By similarity). In the absence of growth factors, BCL2 appears to be phosphorylate... | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:000... | null | null | null | null | null | FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the releas... | Bos taurus (Bovine) |
O02720 | LEP_CANLF | MRCGPLCRFLWLWPYLSCVEAVPIRKVQDDTKTLIKTIVARINDISHTQSVSSKQRVAGLDFIPGLQPVLSLSRMDQTLAIYQQILNSLHSRNVVQISNDLENLRDLLHLLASSKSCPLPRARGLETFESLGGVLEASLYSTEVVALNRLQAALQDMLRRLDLSPGC | null | null | activation of protein kinase C activity [GO:1990051]; adult feeding behavior [GO:0008343]; bone growth [GO:0098868]; cellular response to leptin stimulus [GO:0044320]; energy reserve metabolic process [GO:0006112]; intestinal absorption [GO:0050892]; leptin-mediated signaling pathway [GO:0033210]; lipid metabolic proce... | extracellular space [GO:0005615] | hormone activity [GO:0005179]; peptide hormone receptor binding [GO:0051428] | PF02024; | 1.20.1250.10; | Leptin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P41159}. | null | null | null | null | null | FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-r... | Canis lupus familiaris (Dog) (Canis familiaris) |
O02740 | GUC2F_BOVIN | MFLAPWPFSHLMLWFVTLGRQRGQHGLASFKLLWCLWLLVLMSLPLQVWAPPYKIGVVGPWTCDPLFSKALPEIAAQLATERINKDPALDLGHSLEYVIFNEDCQASRALSSFISHHQMASGFIGPANPGYCEAASLLGNSWDKGIFSWACVNYELDSKNSHPTFSRTLPSPIRVLLTVMKYFQWAHAGVISSDEDIWVHTAYRVASALRSRGLPVGVVLTTGQDSQSIQKALQQIRQADRIRIIIMCMHSTLIGGETQTHLLEWAHDLQMTDGTYVFVPYDTLLYSLPYKHTPYKVLRNNPKLREAYDAVLTITVESQE... | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; visual perception [GO:0007601] | plasma membrane [GO:0005886]; rod photoreceptor outer segment [GO:0120200] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07701;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | PTM: There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9175772}; Single-pass type I membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:Q5SDA5}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000269|PubMed:9175772, ECO:0000269|PubMed:9571173}; | null | null | null | null | FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors (PubMed:9175772, PubMed:9571173). Plays an essential role in phototransduction, by mediating cGMP replenishment (PubMed:9175772, PubMed:9571173). May also participate in the trafficking of membrane-asociated proteins to the... | Bos taurus (Bovine) |
O02741 | ISG15_BOVIN | MGGDLTVKMLGGQEILVPLRDSMTVSELKQFIAQKINVPAFQQRLAHLDSREVLQEGVPLVLQGLRAGSTVLLVVQNCISILVRNDKGRSSPYEVQLKQTVAELKQQVCQKERVQADQFWLSFEGRPMDDEHPLEEYGLMKGCTVFMNLRLRGG | null | null | defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; integrin-mediated signaling pathway [GO:0007229]; ISG15-protein conjugation [GO:0032020]; modification-dependent protein catabolic process [GO:0019941]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of ... | cytosol [GO:0005829]; extracellular region [GO:0005576] | integrin binding [GO:0005178]; polyubiquitin modification-dependent protein binding [GO:0031593]; protein tag activity [GO:0031386]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | null | PTM: S-nitrosylation decreases its dimerization, thereby increasing the availability as well as the solubility of monomeric ISG15 for its conjugation to cellular proteins. {ECO:0000250|UniProtKB:P05161}.; PTM: Induced as an inactive, precursor protein that is cleaved by specific proteases to expose the C-terminal digly... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05161}. Secreted {ECO:0000250|UniProtKB:P05161}. Note=Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins. {ECO:0000250|UniProtKB:P05161}. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze t... | Bos taurus (Bovine) |
O02750 | LEP_PANTR | VPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNMIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC | null | null | activation of protein kinase C activity [GO:1990051]; adult feeding behavior [GO:0008343]; bone growth [GO:0098868]; cellular response to leptin stimulus [GO:0044320]; energy reserve metabolic process [GO:0006112]; intestinal absorption [GO:0050892]; leptin-mediated signaling pathway [GO:0033210]; lipid metabolic proce... | extracellular space [GO:0005615] | hormone activity [GO:0005179]; peptide hormone receptor binding [GO:0051428] | PF02024; | 1.20.1250.10; | Leptin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P41159}. | null | null | null | null | null | FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-r... | Pan troglodytes (Chimpanzee) |
O02755 | CEBPB_BOVIN | MQRLVVWDPVCLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPADRPGPRPPTGELGSIGEHERAIDFSPYLEPLGAPQAPAPTTASDTFEAAPSAPAPVPASSGQHHDFLSDLFSDDYGGKNCKKAAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKATPAAAACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTGENERLQKKV... | null | null | cell differentiation [GO:0030154]; defense response to bacterium [GO:0042742]; DNA-templated transcription [GO:0006351]; hepatocyte proliferation [GO:0072574]; liver regeneration [GO:0097421]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription by RNA polymerase II [GO:0000122... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0... | PF07716; | 1.20.5.170; | BZIP family, C/EBP subfamily | PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-236. {ECO:0000250|UniProtKB:P17676}.; PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (By similarity). Sumoylation at Lys-174 is required for inhibiti... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17676}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000... | null | null | null | null | null | FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functiona... | Bos taurus (Bovine) |
O02766 | CP8B1_RABIT | MVLWGLLGALLMVMVGWLCLPGLLRQRRPQEPPLDKGSIPWLGHAMTFRKNMLEFLKHMRSKHGDVFTVQLGGQYFTFVMDPVSFGPILKDGQRKLDFVEYAKGLVLKVFGYQSIEGDHRMIHLASTKHLMGHGLEELNKAMLDSLSLVMLGPEGRSPDASRWHEDGLFHFCYGVMFKAGYLSLFGHTSDKRQDLLQAEEIFIKFRRFDLLFPRFVYSLLGPREWREVGRLQQLFHELLSVKHNPEKDGMSNWIGHMLQYLSEQGVAPAMQDKFNFMMLWASQGNTGPASFWALIYLLKHPEAMRAVKEEATRVLGEPRL... | 1.14.14.139 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:1400444}; | bile acid biosynthetic process [GO:0006699]; positive regulation of intestinal cholesterol absorption [GO:0045797] | endoplasmic reticulum membrane [GO:0005789] | 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase activity [GO:0033779]; 7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase activity [GO:0033778]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; sterol 12-alpha-hydroxylase activity [GO:0008397] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1400444}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:1400444}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=7alpha-hydroxycholest-4-en-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46752, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:C... | null | PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:O88962}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (PubMed:1400444, PubMed:8943286). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultim... | Oryctolagus cuniculus (Rabbit) |
O02768 | PGH2_RABIT | MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTHFKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRL... | 1.14.99.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q05769}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250|UniProtKB:Q05769}; | brown fat cell differentiation [GO:0050873]; cellular response to fluid shear stress [GO:0071498]; cellular response to hypoxia [GO:0071456]; cellular response to non-ionic osmotic stress [GO:0071471]; cyclooxygenase pathway [GO:0019371]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; negative regulati... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640] | enzyme binding [GO:0019899]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666];... | PF03098; | 1.10.640.10;2.10.25.10; | Prostaglandin G/H synthase family | PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}.; PTM: Acetylated at Ser-565 by SPHK1. During neuroinflammation, acetylation by SPHK1 promotes neuronal secretion of specialized preresolving med... | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Periphera... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=... | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P35354}. | null | null | FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endope... | Oryctolagus cuniculus (Rabbit) |
O02773 | MA1A1_PIG | MPVGGLLPLFSSPAGGGLGGGLGGGLGGGGGGGGRKGSGPSAFRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAADGRARPGEEGAPGDPAAALEDNLARIRENHERALMEAKETLQKLPEEIQRDILMEKEKVAQDQMSNRMGFRLPPVYLVPLIGAIDREPADAAVREKRAKIKEMMKHAWNNYKLYAWGKNELKPVSKGGHSSSLFGNIKGATIVDALDTLFIMKMKNEFEEAKAWVEEHLNFNVNAEVSVFEVNIRFIGGLISAYYLSGEEIFRKKAVELGVKLLP... | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; | carbohydrate metabolic process [GO:0005975]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9219526}; Single-pass type II membrane protein {ECO:0000269|PubMed:9219526}. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). | Sus scrofa (Pig) |
O02776 | PARG_BOVIN | MSAGPGCEPCTKRPRWDAAATSPPAASDARSFPGRQRRVLDSKDAPVQFRVPPSSSGCALGRAGQHRGSATSLVFKQKTITSWMDTKGIKTVESESLHSKENNNTREESMMSSVQKDNFYQHNMEKLENVSQLGFDKSPVEKGTQYLKQHQTAAMCKWQNEGPHSERLLESEPPAVTLVPEQFSNANVDQSSPKDDHSDTNSEESRDNQQFLTHVKLANAKQTMEDEQGREARSHQKCGKACHPAEACAGCQQEETDVVSESPLSDTGSEDVGTGLKNANRLNRQESSLGNSPPFEKESEPESPMDVDNSKNSCQDSEAD... | 3.2.1.143 | null | ATP generation from poly-ADP-D-ribose [GO:1990966]; carbohydrate metabolic process [GO:0005975]; DNA damage response [GO:0006974]; nucleotide-sugar metabolic process [GO:0009225]; regulation of DNA repair [GO:0006282] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | poly(ADP-ribose) glycohydrolase activity [GO:0004649] | PF05028;PF20811; | null | Poly(ADP-ribose) glycohydrolase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86W56}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q86W56}. | CATALYTIC ACTIVITY: Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143; Evidence={ECO:0000269|PubMed:15658938}; | null | null | null | null | FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose) (PubMed:15658938). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ... | Bos taurus (Bovine) |
O02810 | PI4KB_BOVIN | MGDTIVEPAPLKPTSEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPV... | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11526106}. Golgi apparatus membrane {ECO:0000... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000269|... | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP) (PubMed:11526106, PubMed:9218477). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in G... | Bos taurus (Bovine) |
O02812 | MK14_CANLF | MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGADLLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q16539}; | apoptotic process [GO:0006915]; cell motility [GO:0048870]; intracellular signal transduction [GO:0035556]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of myoblast differentiation [GO:0045663]; positive re... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells al... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16539}. Nucleus {ECO:0000250|UniProtKB:Q16539}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q16539}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to di... | Canis lupus familiaris (Dog) (Canis familiaris) |
O02824 | ADA1A_RABIT | MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVGPLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSC... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adult heart development [GO:0007512]; cell growth involved in cardiac muscle cell development [GO:0061049]; MAPK cascade [GO:0000165]; negative regulation of autophagy [GO:0010507]; negative regulation of heart rate involved in barorecepto... | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | alpha1-adrenergic receptor activity [GO:0004937]; protein heterodimerization activity [GO:0046982] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA1A sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerizatio... | null | null | null | null | null | FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocy... | Oryctolagus cuniculus (Rabbit) |
O02827 | MYLK_SHEEP | FRLVEKKTGKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMKQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDIKNRLNCTQCLQHPWLXXXTKNMEAKKLSKHRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLE... | 2.7.11.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | phosphorylation [GO:0016310] | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; stress fiber [GO:0001725] | actin binding [GO:0003779]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; myosin light chain kinase activity [GO:0004687] | PF07679;PF00069; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (By similarity). {ECO:0000250}.; PTM: Can probably be down-regulated by phosphorylation.... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15746}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15746}. Cleavage furrow {ECO:0000250|UniProtKB:Q15746}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q15746}. Note=Localized to stress fibers during interphase and to the cleavage furro... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g.... | Ovis aries (Sheep) |
O02828 | TAU_CAPHI | MAEPRQEFDVMEDHAQGDYTLQDHEGDMEPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKAKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPGTGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLD... | null | null | microtubule cytoskeleton organization [GO:0000226]; neuron projection development [GO:0031175] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; microtubule [GO:0005874]; plasma membrane [GO:0005886] | microtubule binding [GO:0008017] | PF00418; | null | null | PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (a few sites per protei... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10636}. Cell membrane {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10636}. Cell projection, axon {ECO:0000250|U... | null | null | null | null | null | FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity i... | Capra hircus (Goat) |
O02839 | MCP_PIG | MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASP... | null | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of complement activation, alternative pathway [GO:0045957]; negative regulation of complement activation, classical pathway [GO:0045959]; proteolysis [GO:0006508]; single fertilization [GO:0007338]; T cell me... | cell surface [GO:0009986]; extracellular space [GO:0005615]; inner acrosomal membrane [GO:0002079]; membrane [GO:0016020]; plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175] | PF00084; | 2.10.70.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:9029106}.; PTM: May be O-glycosylated. {ECO:0000269|PubMed:9029106}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Inner acrosomal membrane of spermatozoa. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cell... | Sus scrofa (Pig) |
O02840 | CADH5_PIG | MQVLVMLLAAAGTYLGLLTAPTAASNPGRQDTPSTLPLHRRQKRDWIWNQMHIDEEKNGSLPHYVGKIKSSVNHKNTKYQLKGESAGKVFRVDENTGDVYAFERLDREKIPEYQLVALVVDKNTEKNLESPSSFTIKVHDINDNWPVFTQLVFNASVPEMSVIGTSVIQLTAVDADDPTVADHASVIYRLKEGEEHFRIRGPGLIETASKNLDRETVPMYKIVVETQDAQGLRGDSGTATVFITLQDVNDNFPVFTQTRYTFSVPEDIRVGSPLGSLFVKDPDEPQNRKTKYSIVQGEYRDTFTIEPDPTRNEGIIKPMK... | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; homophilic cell adhesion via plasma membrane adhesi... | adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell-cell junction [GO:0005911] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028; | 2.60.40.60;4.10.900.10; | null | PTM: Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB (By similarity). {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q68SP4}. Cell membrane {ECO:0000250|UniProtKB:P33151}; Single-pass type I membrane protein {ECO:0000255}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to en... | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (By similarity). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). This cadherin may play a important role in endothelial cell... | Sus scrofa (Pig) |
O02853 | PTGDS_BOVIN | MATPNRLWMALLLLGVLGVLQTPAPAQAALQPNFEEDKFLGRWFTSGLASNSSWFLEKKKVLSMCKSVVAPAADGGLNLTSTFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTEGVRGPGQDFRMATLYSRSQNPRAEVKEHFTTFAKSLGFTEEGIVFLPKTDKCMEEHP | 5.3.99.2 | null | mast cell degranulation [GO:0043303]; negative regulation by host of viral process [GO:0044793]; negative regulation of viral genome replication [GO:0045071]; prostaglandin biosynthetic process [GO:0001516]; regulation of circadian sleep/wake cycle, sleep [GO:0045187] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791] | prostaglandin-D synthase activity [GO:0004667]; retinoid binding [GO:0005501]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic ret... | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:9510973}; | null | null | null | null | FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:9510973). Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in ol... | Bos taurus (Bovine) |
O03042 | RBL_ARATH | MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRL... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:29372894}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:29372894}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]; response to abscisic acid [GO:0009737]; response to cadmium ion [GO:0046686] | apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; cytosolic ribosome [GO:0022626]; plant-type cell wall [GO:0009505]; plastid [GO:0009536]; thylakoid [GO:0009579] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; mRNA binding [GO:0003729]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}. | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:12766230}. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:29372894}; CATALYTIC ... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (Prob... | Arabidopsis thaliana (Mouse-ear cress) |
O03986 | HS904_ARATH | MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIHIIPDKTNNTLTIIDSGIGMTKADLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVADKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEALGRGTKMILYLKEDQMEYIEERRLKDLVKKHSEFISYPISLWIEKTIEKEISDDEEEEEKKDEEGKVEEIDEEKEKEEKKKKKIKEVTHEWDLVNKQKPIWMRKPEEINKEEYAAFYKSLSNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPF... | null | null | cellular response to heat [GO:0034605]; protein stabilization [GO:0050821] | apoplast [GO:0048046]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plastid [GO:0009536]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; mRNA binding [GO:0003729]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner. {ECO:0000250|UniProtKB:P27323}. | Arabidopsis thaliana (Mouse-ear cress) |
O04017 | NAC98_ARATH | MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPY... | null | null | formation of plant organ boundary [GO:0090691]; leaf development [GO:0048366]; primary shoot apical meristem specification [GO:0010072]; regulation of timing of plant organ formation [GO:0090709]; secondary shoot formation [GO:0010223] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF02365; | 2.170.150.80; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:15500463}. | null | null | null | null | null | FUNCTION: Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner... | Arabidopsis thaliana (Mouse-ear cress) |
O04019 | PS6AB_ARATH | MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRAD... | null | null | embryo sac development [GO:0009553]; glucose mediated signaling pathway [GO:0010255]; pollen development [GO:0009555]; proteasomal protein catabolic process [GO:0010498]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proteasome-activating activity [GO:0036402] | PF00004;PF17862;PF16450; | 1.10.8.60;2.40.50.140;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. {ECO:0000269|PubMed:17081979}. | Arabidopsis thaliana (Mouse-ear cress) |
O04023 | SRC2_ARATH | MECRSLDLTIISAEDLKDVQLIGKQDLYAVVSINGDARTKQKTKVDKDCGTKPKWKHQMKLTVDDAAARDNRLTLVFEIVADRPIAGDKPVGEVSVPVKELLDQNKGDEEKTVTYAVRLPNGKAKGSLKFSFKFGEKYTYGSSSGPHAPVPSAMDHKTMDQPVTAYPPGHGAPSAYPAPPAGPSSGYPPQGHDDKHDGVYGYPQQAGYPAGTGGYPPPGAYPQQGGYPGYPPQQQGGYPGYPPQGPYGYPQQGYPPQGPYGYPQQQAHGKPQKPKKHGKAGAGMGLGLGLGAGLLGGLLVGEAVSDIADMGDMGDMGDMG... | null | null | cellular response to hypoxia [GO:0071456]; defense response [GO:0006952]; protein targeting to vacuole [GO:0006623] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; protein storage vacuole [GO:0000326]; protein storage vacuole membrane [GO:0032586] | null | PF00168; | 2.60.40.150; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16227454}; Single-pass type II membrane protein {ECO:0000255}. Protein storage vacuole membrane {ECO:0000269|PubMed:16227454}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:23872431}; Single-pass type II mem... | null | null | null | null | null | FUNCTION: May act as an activator of the calcium-dependent activation of RBOHF that mediates reactive oxygen species (ROS) production and may play a role in cold responses. {ECO:0000269|PubMed:23872431}. | Arabidopsis thaliana (Mouse-ear cress) |
O04046 | GGPP2_ARATH | MEPQILFLYLSLFILSLNFFFTNLKPRLVRLFQPSLESRVKTALLSRKEVAAFLDSPIVEDEEGEEREEEEEGGIVSNANFTFEFDPYMMSKAESVNKALEEAIPVGEPLKIHEAMRYAILAAGKRVRPILCLASCELVGGQENAAMPAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVYGEGVAILSGGALLSLAFEHMTTAEISSERMVWAVRELARSIGTRGLVAGQAMDISSEGLDLNEVGLEHLEFIHVHKTAVLLETAAVLGAIIGGGSDEEIESVRKFARCIGLLFQVVDDILDETKSSEELGKTAGK... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | carotenoid biosynthetic process [GO:0016117]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid biosynthetic process [GO:0008299] | endoplasmic reticulum [GO:0005783] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:10759500}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product pr... | Arabidopsis thaliana (Mouse-ear cress) |
O04073 | CTPA_TETOB | MHSRTNCLQTSVRAPQPHFRPFTAVKTCRQRCSTTAAAAKRDQAQEQQPWIQVGLGLAAAATAVAVGLGAAALPAQAVTSEQLLFLEAWRAVDRAYVDKSFNGQSWFKLRETYLKKEPMDRRAQTYDAIRKLLAVLDDPFTRFLEPSRLAALRRGTAGSVTGVGLEITYDGGSGKDVVVLTPAPGGPAEKAGARAGDVIVTVDGTAVKGLSLYDVSDLLQGEADSQVEVVLHAPGAPSNTRTLQLTRQKVTINPVTFTTCSNVAAAALPPGAAKQQLGYVRLATFNSNTTAAAQQAFTELSKQGVAGLVLDIRNNGGGLF... | 3.4.21.102 | null | proteolysis [GO:0006508]; signal transduction [GO:0007165] | chloroplast thylakoid lumen [GO:0009543] | serine-type endopeptidase activity [GO:0004252] | PF17820;PF03572; | 2.30.42.10;3.30.750.44; | Peptidase S41A family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000303|PubMed:9252339}. | CATALYTIC ACTIVITY: Reaction=The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-As... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.2. {ECO:0000269|PubMed:9252339}; | null | FUNCTION: Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. {ECO:0000269|PubMed:9252339}. | Tetradesmus obliquus (Green alga) (Acutodesmus obliquus) |
O04121 | CHMO_SPIOL | MMAASASATTMLLKYPTTVCGIPNPSSNNNNDPSNNIVSIPQNTTNPTLKSRTPNKITTNAVAAPSFPSLTTTTPSSIQSLVHEFDPQIPPEDAHTPPSSWYTEPAFYSHELERIFYKGWQVAGISDQIKEPNQYFTGSLGNVEYLVSRDGEGKVHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGMDGSLAKASKAKPEQNLDPKELGLVPLKVAVWGPFVLISLDRSLEEGGDVGTEWLGTSAEDVKAHAFDPSLQFIHRSEFPMESNWKIFSDNYLDSSYHVPYAHKYYATELNFDTYDTQMIENVTIQRVEGS... | 1.14.15.7 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305}; Note=Binds 1 Fe cation. {ECO:0000305}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | glycine betaine biosynthetic process from choline [GO:0019285] | chloroplast stroma [GO:0009570] | 2 iron, 2 sulfur cluster binding [GO:0051537]; choline monooxygenase activity [GO:0019133]; iron ion binding [GO:0005506] | PF00355;PF00848; | 2.102.10.10; | Choline monooxygenase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma. | CATALYTIC ACTIVITY: Reaction=choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17769, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15870, ChEBI... | null | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (monooxygenase route): step 1/1. | null | null | FUNCTION: Catalyzes the first step of the osmoprotectant glycine betaine synthesis. | Spinacia oleracea (Spinach) |
O04130 | SERA2_ARATH | MAFSSSCSSVKAVNSRWTSPSPSPSSRFAVLPAFLHRRYATSVKLTAISAALKTVEQTTLTEDNRFSTVGSDSDEYNPTLPKPRILVTEKLGEAGVNLLREFGDVDCSYDLSPEDLKKKVAESDALIVRSGTKVTREVFEAAKGRLKVVGRAGVGIDNVDLQAATEHGCLVVNAPTANTVAAAEHGIALLASMARNVAQADASIKAGKWERSKYVGVSLVGKTLAVMGFGKVGTEVARRAKGLGMTVISHDPYAPADRARALGVDLVSFDQAISTADFVSLHMPLTPATKKVFNDETFSKMKKGVRLINVARGGVIDEDA... | 1.1.1.95 | null | L-serine biosynthetic process [GO:0006564] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; nucleus [GO:0005634] | NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617] | PF00389;PF02826;PF01842;PF19304; | 3.30.70.260;3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.926 mM for 3-phospho-D-glycerate (at pH 7.2) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.899 mM for 3-phospho-D-glycerate (at pH 8.1) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=1.19 mM for 3-phospho-D-glycerate (at pH 9.0) {... | PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. | null | null | FUNCTION: Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}. | Arabidopsis thaliana (Mouse-ear cress) |
O04147 | CPD_ARATH | MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP | 3.1.4.37 | null | cyclic nucleotide metabolic process [GO:0009187]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113] | PF07823; | 3.90.1140.10; | 2H phosphoesterase superfamily, CPD1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9148938}. | CATALYTIC ACTIVITY: Reaction=ADP-alpha-D-ribose 1'',2''-cyclic phosphate + H2O = ADP-alpha-D-ribose 1''-phosphate + H(+); Xref=Rhea:RHEA:72083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58753, ChEBI:CHEBI:76596; Evidence={ECO:0000269|PubMed:9148938}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72084; E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.35 mM for Appr>p {ECO:0000269|PubMed:9148938}; KM=1.34 mM for A>p {ECO:0000269|PubMed:9148938}; KM=2.38 mM for C>p {ECO:0000269|PubMed:9148938}; KM=16.86 mM for G>p {ECO:0000269|PubMed:9148938}; KM=17.67 mM for U>p {ECO:0000269|PubMed:9148938}; Vmax=25 umol/min/m... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:9148938}; | null | FUNCTION: Hydrolyzes ADP-ribose 1'',2''-cyclic phosphate (Appr>1) that is produced during tRNA splicing into ADP-ribose 1''-phosphate (Appr-1''p) (PubMed:9148938). Acts also on nucleoside 2',3'-cyclic phosphates (PubMed:9148938). {ECO:0000269|PubMed:9148938}. | Arabidopsis thaliana (Mouse-ear cress) |
O04151 | CALR1_ARATH | MAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDAKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNPEFKDDPELYVFPKLKYVGV... | null | null | protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]; plasmodesma [GO:0009506]; secretory vesicle [GO:0099503] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; unfolded protein binding [GO:0051082] | PF00262; | 2.60.120.200;2.10.250.10; | Calreticulin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. | null | null | null | null | null | FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
O04153 | CALR3_ARATH | MGLPQNKLSFFCFFFLVSVLTLAPLAFSEIFLEEHFEGGWKSRWVLSDWKRNEGKAGTFKHTAGKWPGDPDNKGIQTYNDAKHYAISAKIPEFSNKNRTLVVQYSVKIEQDIECGGAYIKLLSGYVNQKQFGGDTPYSLMFGPDICGTQTKKLHVIVSYQGQNYPIKKDLQCETDKLNHFYTFILRPDASYSVLVDNKEREFGSMYTDWDILPPRKIKVKNAKKPEDWDDREYIDDPNDVKPEGFDSIPREIPDRKAKEPEDWDEEENGLWEPPKIPNSAYKGPWKAKRIKNPNYKGKWKNPWIDNPEFEDDPDLYVLKS... | null | null | anthocyanin-containing compound metabolic process [GO:0046283]; defense response to bacterium [GO:0042742]; plant-type hypersensitive response [GO:0009626]; protein folding [GO:0006457] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; unfolded protein binding [GO:0051082] | PF00262; | 2.60.120.200;2.10.250.10; | Calreticulin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:19717464}. | null | null | null | null | null | FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (E... | Arabidopsis thaliana (Mouse-ear cress) |
O04157 | RAG3B_ARATH | MSTRRRTLLKVIILGDSGVGKTSLMNQYVNNKFSQQYKATIGADFVTKELQIDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNHLKSFESLDNWHNEFLTRASPRDPMAFPFILLGNKVDIDGGNSRVVSEKKAREWCAEKGNIVYFETSAKEDYNVDDSFLCITKLALANERDQDIYFQPDTGSVPEQRGGCAC | null | null | positive regulation of autophagy [GO:0010508]; programmed cell death involved in cell development [GO:0010623]; protein transport [GO:0015031]; tracheary element differentiation [GO:1905177]; xylem development [GO:0010089] | nucleus [GO:0005634]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Intracellular vesicle trafficking and protein transport. Functions in autophagy. Involved in xylem and tracheary element differentiation. {ECO:0000269|PubMed:20659276}. | Arabidopsis thaliana (Mouse-ear cress) |
O04196 | ISOA1_ARATH | MDAIKCSSSFLHHTKLNTLFSNHTFPKISAPNFKPLFRPISISAKDRRSNEAENIAVVEKPLKSDRFFISDGLPSPFGPTVRDDGVNFSVYSTNSVSATICLISLSDLRQNKVTEEIQLDPSRNRTGHVWHVFLRGDFKDMLYGYRFDGKFSPEEGHYYDSSNILLDPYAKAIISRDEFGVLGPDDNCWPQMACMVPTREEEFDWEGDMHLKLPQKDLVIYEMHVRGFTRHESSKIEFPGTYQGVAEKLDHLKELGINCIELMPCHEFNELEYYSYNTILGDHRVNFWGYSTIGFFSPMIRYASASSNNFAGRAINEFKI... | 3.2.1.68 | null | amylopectin biosynthetic process [GO:0010021]; starch biosynthetic process [GO:0019252]; starch catabolic process [GO:0005983] | chloroplast [GO:0009507]; chloroplast isoamylase complex [GO:0010368] | isoamylase activity [GO:0019156] | PF00128;PF02922;PF21156; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: Involved in the trimming of pre-amylopectin chains. Accelerates the crystallization of nascent amylopectin molecules during starch synthesis. ISA1 and ISA2 work exclusively together as a multimeric holoenzyme. ISA1-ISA2 removes preferentially branches that are very close to other branches. Promotes negative g... | Arabidopsis thaliana (Mouse-ear cress) |
O04197 | COI1_ARATH | MEDPDIKRCKLSCVATVDDVIEQVMTYITDPKDRDSASLVCRRWFKIDSETREHVTMALCYTATPDRLSRRFPNLRSLKLKGKPRAAMFNLIPENWGGYVTPWVTEISNNLRQLKSVHFRRMIVSDLDLDRLAKARADDLETLKLDKCSGFTTDGLLSIVTHCRKIKTLLMEESSFSEKDGKWLHELAQHNTSLEVLNFYMTEFAKISPKDLETIARNCRSLVSVKVGDFEILELVGFFKAAANLEEFCGGSLNEDIGMPEKYMNLVFPRKLCRLGLSYMGPNEMPILFPFAAQIRKLDLLYALLETEDHCTLIQKCPNL... | null | null | anther dehiscence [GO:0009901]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; extracellular ATP signaling [GO:0106167]; jasmonic acid and ethylene-dependent systemic resistance [GO:0009861]; jasmonic acid mediated signaling pathway [GO:0009867]; nega... | SCF ubiquitin ligase complex [GO:0019005] | null | PF18511;PF18791; | 1.20.1280.50;3.80.10.10; | null | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Required for jasmonate-regulated plant fertility and defense processes, and for coronatine and/or other elicitors perceptions/responses. Seems to not be required for meiosis. Required for the regulation of some genes induced by wounding, but not for all. Component of SCF(COI1) E3 ubiquitin ligase complexes, w... | Arabidopsis thaliana (Mouse-ear cress) |
O04200 | PXN_ARATH | MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKG... | null | null | NAD transport [GO:0043132]; regulation of peroxisome size [GO:0044375] | glyoxysomal membrane [GO:0046861]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325] | antiporter activity [GO:0015297] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Glyoxysome membrane {ECO:0000269|PubMed:11522909, ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}; Multi-pass membrane protein {ECO:0000269|PubMed:11522909, ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=102 uM for the NAD(+)/NAD(+) exchange {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559}; KM=119 uM for the AMP/AMP exchange {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559}; Vmax=166 umol/min/g enzyme for the NAD(+)/NAD(+) exchange {ECO:0000269|P... | null | null | null | FUNCTION: Mediates the NAD(+) import into peroxisomes. Favors the NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a low unidirectional transport that might be essential under special conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-diphosphate (PAP), NAD(+), AMP, ADP and NADH, ... | Arabidopsis thaliana (Mouse-ear cress) |
O04202 | EIF3F_ARATH | MAATSEHTILQFVSPSSTASATTSVLTARIHPLVIFNVCDCFVRRPDSAERVIGTLLGSILPDGTVDIRNSYAVPHNESSDQVAVDIDYHHNMLASHLKVNSKETIVGWYSTGAGVNGGSSLIHDFYAREVPNPIHLTVDTGFTNGEGTIKAFVSSNLSLGDRQLVAHFQEIPVDLRMVDAERVGFDVLKATSVDKLPNDLEGMELTMERLLTLINDVYKYVDSVVGGQIAPDNNIGRFIADAVASLPKLPPQVFDNLVNDSLQDQLLLLYLSSITRTQLSLAEKLNTAAQML | null | null | embryo development ending in seed dormancy [GO:0009793]; formation of cytoplasmic translation initiation complex [GO:0001732]; pollen germination [GO:0009846]; response to sucrose [GO:0009744] | cytoplasm [GO:0005737]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | metallopeptidase activity [GO:0008237]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369] | PF01398;PF13012; | 3.40.140.10; | EIF-3 subunit F family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:20444226}. | null | null | null | null | null | FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and i... | Arabidopsis thaliana (Mouse-ear cress) |
O04209 | CLC2_ARATH | MSAFEDDSFVILNDDASESVPVSGSFDATDSFSAFDGSLQVEDSVDDVFAAPSSDYGAYSNGDGIFGSNGDHDGPILPPPSEMESDEGFALREWRRQNAIQLEEKEKREKELLKQIIEEADQYKEEFHKKIEVTCENNKAANREKEKLYLENQEKFYAESSKNYWKAIAELVPKEVPTIEKRRGKKEQQDPKKPTVSVIQGPKPGKPTDLTRMRQILVKLKHNPPSHLKLTSQPPSEEAAAPPKNVPETKPTEAVTAA | null | null | clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886] | cell plate [GO:0009504]; chloroplast envelope [GO:0009941]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; phragmoplast [GO:0009524] | clathrin heavy chain binding [GO:0032050]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198] | PF01086; | null | Clathrin light chain family | null | SUBCELLULAR LOCATION: Cell membrane. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, phragmoplast. Note=Cytoplasm... | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. | Arabidopsis thaliana (Mouse-ear cress) |
O04211 | ELF4_ARATH | MKRNGETKRRRNVAEEAEQGEDPAMWENLDRNFRQVQSVLDRNRSLIQQVNDNHQSRMADNMSKNVALIQELNGNISKVVNMYSDLNTSFSSGFHGGKNGHDGGGAAGTRA | null | null | entrainment of circadian clock [GO:0009649]; flower development [GO:0009908]; negative regulation of transcription by RNA polymerase II [GO:0000122]; photoperiodism [GO:0009648]; photoperiodism, flowering [GO:0048573]; positive regulation of circadian rhythm [GO:0042753]; red or far-red light signaling pathway [GO:0010... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | protein homodimerization activity [GO:0042803] | PF07011; | null | EARLY FLOWERING 4 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14605220, ECO:0000269|PubMed:22327739}. Note=Diffuse distribution. Targeted to nuclear bodies after interaction with ELF3 (PubMed:22327739). {ECO:0000269|PubMed:22327739}. | null | null | null | null | null | FUNCTION: Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles. Part of a corepressor complex consisting of ELF4, ELF3, and LUX involved in the transcriptional regulation of APRR9. Increas... | Arabidopsis thaliana (Mouse-ear cress) |
O04226 | P5CS1_ORYSJ | MASVDPSRSFVRDVKRVIIKVGTAVVSRQDGRLALGRVGALCEQVKELNSLGYEVILVTSGAVGVGRQRLRYRKLVNSSFADLQKPQMELDGKACAAVGQSGLMALYDMLFNQLDVSSSQLLVTDSDFENPKFREQLTETVESLLDLKVIPIFNENDAISTRKAPYEDSSGIFWDNDSLAGLLALELKADLLILLSDVDGLYSGPPSEPSSKIIHTYIKEKHQQEITFGDKSRVGRGGMTAKVKAAVLASNSGTPVVITSGFENRSILKVLHGEKIGTLFHKNANLWESSKDVSTREMAVAARDCSRHLQNLSSEERKKI... | 1.2.1.41; 2.7.2.11 | null | L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310]; proline biosynthetic process [GO:0006561] | mitochondrion [GO:0005739] | ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; glutamate-5-semialdehyde dehydrogenase activity [GO:0004350] | PF00696;PF00171; | 3.40.1160.10; | Glutamate 5-kinase family; Gamma-glutamyl phosphate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; CATALYTIC ACTIVITY: Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH; Xref=Rhea:... | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.; PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. | null | null | FUNCTION: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants. Involved in abiotic stress tolerance. {ECO:0000269|Ref.8}. | Oryza sativa subsp. japonica (Rice) |
O04291 | ATB14_ARATH | MMMVHSMSRDMMNRESPDKGLDSGKYVRYTPEQVEALERVYTECPKPSSLRRQQLIRECPILSNIEPKQIKVWFQNRRCREKQRKEAARLQTVNRKLNAMNKLLMEENDRLQKQVSNLVYENGHMKHQLHTASGTTTDNSCESVVVSGQQHQQQNPNPQHQQRDANNPAGLLSIAEEALAEFLSKATGTAVDWVQMIGMKPGPDSIGIVAISRNCSGIAARACGLVSLEPMKVAEILKDRPSWLRDCRSVDTLSVIPAGNGGTIELIYTQMYAPTTLAAARDFWTLRYSTCLEDGSYVVCERSLTSATGGPTGPPSSNFV... | null | null | adaxial/abaxial pattern specification [GO:0009955]; cell differentiation [GO:0030154]; determination of bilateral symmetry [GO:0009855]; integument development [GO:0080060]; meristem initiation [GO:0010014]; polarity specification of adaxial/abaxial axis [GO:0009944]; primary shoot apical meristem specification [GO:001... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; lipid binding [GO:0008289] | PF00046;PF08670;PF01852; | 3.30.530.20;1.10.10.60; | HD-ZIP homeobox family, Class III subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in the determination of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf fates. {ECO:0000269|PubMed:11395776, ECO:0000269|PubMed:15328016, ECO:0000269|PubMed:15598805}. | Arabidopsis thaliana (Mouse-ear cress) |
O04292 | ATBH9_ARATH | MMAHHSMDDRDSPDKGFDSGKYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECPILCNIEPRQIKVWFQNRRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYENGFMKHRIHTASGTTTDNSCESVVVSGQQRQQQNPTHQHPQRDVNNPANLLSIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCSGIAARACGLVSLEPMKVAEILKDRPSWFRDCRCVETLNVIPTGNGGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLTSATGGPNGPLSSSFVRAKM... | null | null | adaxial/abaxial axis specification [GO:0009943]; cell differentiation [GO:0030154]; determination of bilateral symmetry [GO:0009855]; embryonic pattern specification [GO:0009880]; integument development [GO:0080060]; meristem initiation [GO:0010014]; polarity specification of adaxial/abaxial axis [GO:0009944]; primary ... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; lipid binding [GO:0008289]; transcription cis-regulatory region binding [GO:0000976] | PF00046;PF08670;PF01852; | 3.30.530.20;1.10.10.60; | HD-ZIP homeobox family, Class III subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in the determination of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf fates. Binds to the DNA sequence 5'-GTAAT[GC]ATTAC-3'. {ECO:0000269|PubMed:11395776, ECO:0000269|PubMed:15598805, ECO:0000269|PubMed:17900520, ECO:0000269|PubMed:9747806}. | Arabidopsis thaliana (Mouse-ear cress) |
O04294 | IMPA3_ARATH | MSLRPSAKTEVRRNRYKVAVDAEEGRRRREDNLVEIRKNKREENLQKKRFTSSMAFGSATGQTEQDLSSANQLKDNLPAMVAGIWSEDSNSQLEATNLLRKLLSIEQNPPINEVVQSGVVPRVVKFLSRDDFPKLQFEAAWALTNIASGTSENTNVIIESGAVPIFIQLLSSASEDVREQAVWALGNVAGDSPKCRDLVLSYGAMTPLLSQFNENTKLSMLRNATWTLSNFCRGKPPPAFEQTQPALPVLERLVQSMDEEVLTDACWALSYLSDNSNDKIQAVIEAGVVPRLIQLLGHSSPSVLIPALRTIGNIVTGDDL... | null | null | defense response [GO:0006952]; NLS-bearing protein import into nucleus [GO:0006607] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15964279}. | null | null | null | null | null | FUNCTION: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as a cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). May be involved in ... | Arabidopsis thaliana (Mouse-ear cress) |
O04300 | RGP1_PEA | MASLPKPTPLLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGHEINALEQHIKNLLSPSTPFFFNTLYDPYREGTDFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPHERNTRFVDAVLTIPKGSLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGYGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEEIIPFFQAATLSKDCTSVQKCYIELSKQVKEKL... | 5.4.99.30 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8H8T0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8H8T0}; | cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; plant-type cell wall biogenesis [GO:0009832]; protein glycosylation [GO:0006486]; UDP-L-arabinose metabolic process [GO:0033356] | cytosol [GO:0005829]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; plasmodesma [GO:0009506] | UDP-arabinopyranose mutase activity [GO:0052691] | PF03214; | null | RGP family | PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose. {ECO:0000269|PubMed:1834664, ECO:0000269|PubMed:9207152}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9207152}. Cell junction, plasmodesma {ECO:0000269|PubMed:9207152}. Golgi apparatus {ECO:0000269|PubMed:9207152}. Note=Cell wall-associated, with highest concentrations on plasmodesmata. Also located in the Golgi apparatus. {ECO:0000269|PubMed:9207152}. | CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose; Xref=Rhea:RHEA:28350, ChEBI:CHEBI:61457, ChEBI:CHEBI:61463; EC=5.4.99.30; Evidence={ECO:0000250|UniProtKB:Q8H8T0}; | null | null | null | null | FUNCTION: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese (PubMed:9207152). {ECO:0000250|UniProtKB:Q8H8T0, ECO:0000269|Pu... | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
O04308 | MPPA2_ARATH | MYRTAASRAKALKGILNHNFRASRYASSSAVATSSSSSSWLSGGYSSSLPSMNIPLAGVSLPPPLSDHVEPSKLKTTTLPNGLTIATEMSPNPAASIGLYVDCGSIYETPQFRGATHLLERMAFKSTLNRSHFRLVREIEAIGGNTSASASREQMGYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKVKVEIGEFATNPMGFLLEAVHSAGYSGALANPLYAPESAITGLTGEVLENFVFENYTASRMVLAASGVDHEELLKVVEPLLSDLPNVPRPAEPKSQYVGGDFRQHTGGEATHFALAFEVPGWNNEKE... | null | null | proteolysis [GO:0006508] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrio... | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:22131051}. Mitochondrion matrix {ECO:0000269|PubMed:22131051}. Mitochondrion inner membrane {ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:22131051}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07257}; Matrix side {ECO:0000250|UniProtKB:P07... | null | null | null | null | null | FUNCTION: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. {ECO:0000250|UniProtKB:P11914}.; FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane c... | Arabidopsis thaliana (Mouse-ear cress) |
O04314 | JAL30_ARATH | MAQKVEAQGGKGANLWDDGSTHDAVTKIQLAAGIDGIQYVQFDYVKNGQPEQAPLRGTKGRVLPADPFVINHPDEHLVSVEGWYSPEGIIQGIKFISNKKTSDVIGSDEGTHFTLQVKDKKIIGFHGSAGGNLNSLGAYFAPLTTTTPLTPAKQLTAFGSDDGTVWDDGAYVGVKKVYVGQAQDGISAVKFVYDKSPEEVTGEEHGKSTLLGFEEFVLDYPSEYITAVDGTYDKIFGSDGSVITMLRFKTNKQTSPPFGLEAGTVFELKEEGHKIVGFHGRADVLLHKIGVHVRPLSN | null | null | protein folding [GO:0006457]; regulation of hydrolase activity [GO:0051336] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasmodesma [GO:0009506] | carbohydrate binding [GO:0030246]; copper ion binding [GO:0005507]; enzyme regulator activity [GO:0030234] | PF01419; | 2.100.10.30; | Jacalin lectin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15919674}. | null | null | null | null | null | FUNCTION: Inhibitor-type lectin that may regulate the correct polymerization of BGLU23/PYK10 upon tissue damage. Activates BGLU21, BGLU22 and BGLU23. {ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:18467340, ECO:0000269|PubMed:19965874}. | Arabidopsis thaliana (Mouse-ear cress) |
O04316 | JAL29_ARATH | MAQKVEAQGGNGGNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRSFEADPFVINHPEEHLVSVEGRYNPEGLILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAPLTNVTPLNAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGYREKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENGDGPGLRCSHDI... | 4.8.1.5 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8RY71}; | glucosinolate catabolic process [GO:0019762]; nitrile biosynthetic process [GO:0080028]; seed germination [GO:0009845] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasmodesma [GO:0009506] | carbohydrate binding [GO:0030246]; enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF01419;PF01344;PF13415;PF13418; | 2.100.10.30;2.120.10.80; | Jacalin lectin family | null | null | CATALYTIC ACTIVITY: Reaction=a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur; Xref=Rhea:RHEA:59956, ChEBI:CHEBI:16189, ChEBI:CHEBI:18379, ChEBI:CHEBI:26833, ChEBI:CHEBI:183089; EC=4.8.1.5; Evidence={ECO:0000269|PubMed:18987211}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidot... | null | null | null | null | FUNCTION: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (PubMed:27990154). Promotes simple nitriles, but not epithionitrile or thiocyanate formation (PubMed:18987211). Converts allylglucosinolate and benzylglucosinolate (glucotropaeolin) to their corresponding simple ... | Arabidopsis thaliana (Mouse-ear cress) |
O04318 | JAL27_ARATH | MAQKLVAQGGETGDVWDDGVYDNVTKVYVGQGQYGIAFVKFEYANGSEVVVGDEHGEKTELGVEEFEIDSDDYIVYVEGYREKVSDMTSEMITFLSFKTSKGKTSQPIVKKPGVKFVLHGGKIVGFHGRSTDVLHSLGAYVSLPSTPKLLGNWIKVEQNGEGPGLRCSHGIAQVGNKIYSFGGELIPNQPIDKHLYVFDLETRTWSIAPATGDVPHLSCLGVRMVSVGSTLYTFGGRDFSRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVGAMDRIKTLDSYNIVDKTWFHCSNPGDSFSIRG... | 4.8.1.5 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8RY71}; | glucosinolate catabolic process [GO:0019762]; nitrile biosynthetic process [GO:0080028]; seed germination [GO:0009845] | chloroplast [GO:0009507]; cytosol [GO:0005829]; nucleus [GO:0005634] | carbohydrate binding [GO:0030246]; enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF01419;PF01344; | 2.100.10.30;2.120.10.80; | Jacalin lectin family | null | null | CATALYTIC ACTIVITY: Reaction=a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur; Xref=Rhea:RHEA:59956, ChEBI:CHEBI:16189, ChEBI:CHEBI:18379, ChEBI:CHEBI:26833, ChEBI:CHEBI:183089; EC=4.8.1.5; Evidence={ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:19224919}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl... | null | null | null | null | FUNCTION: Specifier protein responsible for constitutive and herbivore-induced simple nitrile formation, especially in roots (PubMed:27990154). Promotes simple nitriles, but not epithionitrile or thiocyanate formation (PubMed:18987211). Converts allylglucosinolate and benzylglucosinolate (glucotropaeolin) to their corr... | Arabidopsis thaliana (Mouse-ear cress) |
O04331 | PHB3_ARATH | MGSQQAAVSFLSNLAKAAFGLGTAATVLNTSLFTVDGGERAVIFDRFRGVMDQTVGEGTHFLIPILQRPHIFDIRTKPHTFSSISGTKDLQMVNLTLRVLSRPEVSRLPYIFQTLGLEYDEKVLPSIGNEVLKAVVAQFNADQLLTERPHVSALVRESLITRAKDFNIVLDDVAITHLSYGVEFSRAVEQKQVAQQEAERSKFVVMKADQERRAAVIRAEGESEAAQLISDATAKAGMGLIELRRIEASREIASTLARSPNVAYLPGGQSMLFALNR | null | null | cell division [GO:0051301]; defense response to bacterium [GO:0042742]; lateral root development [GO:0048527]; mitochondrion organization [GO:0007005]; negative regulation of cell division [GO:0051782]; response to auxin [GO:0009733]; response to ethylene [GO:0009723]; response to nitric oxide [GO:0071731]; response to... | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886] | protein-containing complex binding [GO:0044877] | PF01145; | 3.30.479.30; | Prohibitin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}. Mitochondrion inner membrane {ECO:0000269|PubMed:12837548, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:21841088, ECO:0000269|PubMed:9132067}; Single-pass type II membrane protein {ECO:0000255... | null | null | null | null | null | FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins (By similarity). Necessary for mitochondrial and cell metabolism and biogenesis. Required to regulate the ethylene-mediated signaling; involved in growth maintenance in the presence of ethylene. F... | Arabidopsis thaliana (Mouse-ear cress) |
O04350 | TBCA_ARATH | MATIRNLKIKTSTCKRIVKELHSYEKEVEREAAKTADMKDKGADPYDLKQQENVLGESRMMIPDCHKRLESALADLKSTLAELEETDEKEGPEIEDAKKTVADVEKQFPTEDA | null | null | post-chaperonin tubulin folding pathway [GO:0007023]; tubulin complex assembly [GO:0007021] | cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; peroxisome [GO:0005777] | beta-tubulin binding [GO:0048487] | PF02970; | 1.20.58.90; | TBCA family | null | null | null | null | null | null | null | FUNCTION: Tubulin-folding protein involved in the control of the alpha-/beta-tubulin monomer balance. Functions as a reservoir of bound and non-toxic beta-tubulin. Required in the developing embryo. {ECO:0000269|PubMed:11959844, ECO:0000269|PubMed:12215519}. | Arabidopsis thaliana (Mouse-ear cress) |
O04373 | ILL4_ARATH | MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNAT... | 3.5.1.-; 3.5.1.127 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11923288}; Note=The Mn(2+) ion enhances activity. {ECO:0000269|PubMed:11923288}; | auxin metabolic process [GO:0009850]; response to wounding [GO:0009611] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; nucleus [GO:0005634] | IAA-Ala conjugate hydrolase activity [GO:0010179]; metal ion binding [GO:0046872] | PF07687;PF01546; | 3.30.70.360;3.40.630.10; | Peptidase M20 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. | CATALYTIC ACTIVITY: Reaction=a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino acid; Xref=Rhea:RHEA:52028, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:136183, ChEBI:CHEBI:136184; EC=3.5.1.127; Evidence={ECO:0000269|PubMed:24052260}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 uM for IAA-Ala {ECO:0000269|PubMed:11923288}; Vmax=20 nmol/min/mg enzyme with IAA-Ala as substrate {ECO:0000269|PubMed:11923288}; Note=kcat is 0.024 sec(-1) with IAA-Ala as substrate. {ECO:0000269|PubMed:11923288}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:11923288}; | null | FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly (PubMed:10072397, PubMed:11923288). Has a lower efficiency with IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile (PubMed:100723... | Arabidopsis thaliana (Mouse-ear cress) |
O04378 | SYP23_ARATH | MSFQDLEAGRGRSLASSRNINGGGSRQDTTQDVASGIFQINTSVSTFHRLVNTLGTPKDTPELREKLHKTRLYIGQLVKDTSAKLKEASETDHQRGVNQKKKIVDAKLAKDFQAVLKEFQKAQRLAAERETVYAPLVHKPSLPSSYTSSEIDVNGDKHPEQRALLVESKRQELVLLDNEIAFNEAVIEEREQGIQEIQQQIGEVHEIFKDLAVLVHDQGNMIDDIGTHIDNSYAATAQGKSHLVRHQRHKDQILL | null | null | intracellular protein transport [GO:0006886]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906] | endomembrane system [GO:0012505]; SNARE complex [GO:0031201] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF00804;PF14523; | 1.20.5.110;1.20.58.70; | Syntaxin family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. Membrane. Note=In cv. RLD, probably a type IV membrane protein. In cv. Columbia, probably associated with membranes by a post-translational modification or through protein-protein interactions. | null | null | null | null | null | FUNCTION: May function in the docking or fusion of transport vesicles with the prevacuolar membrane. | Arabidopsis thaliana (Mouse-ear cress) |
O04379 | AGO1_ARATH | MVRKRRTDAPSEGGEGSGSREAGPVSGGGRGSQRGGFQQGGGQHQGGRGYTPQPQQGGRGGRGYGQPPQQQQQYGGPQEYQGRGRGGPPHQGGRGGYGGGRGGGPSSGPPQRQSVPELHQATSPTYQAVSSQPTLSEVSPTQVPEPTVLAQQFEQLSVEQGAPSQAIQPIPSSSKAFKFPMRPGKGQSGKRCIVKANHFFAELPDKDLHHYDVTITPEVTSRGVNRAVMKQLVDNYRDSHLGSRLPAYDGRKSLYTAGPLPFNSKEFRINLLDEEVGAGGQRREREFKVVIKLVARADLHHLGMFLEGKQSDAPQEALQV... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | adaxial/abaxial pattern specification [GO:0009955]; adventitious root development [GO:0048830]; auxin metabolic process [GO:0009850]; cell differentiation [GO:0030154]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; leaf morphogenesis [GO:0009965]; leaf proximal/distal pattern formation [G... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA binding [GO:0003729]; RNA endonuclease activity [GO:0004521]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197] | PF08699;PF16488;PF16487;PF16486;PF12764;PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Ago subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28463111}. | null | null | null | null | null | FUNCTION: Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous m... | Arabidopsis thaliana (Mouse-ear cress) |
O04385 | IEMT_CLABR | MGSTGNAEIQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVCKFLTKNEDGVSLAPFLLTATDKVLLEPWFYLKDAILEGGIPFNKAYGMNEFDYHGTDHRFNKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGAVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIFIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVVIHTD... | 2.1.1.146 | null | aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259] | null | (iso)eugenol O-methyltransferase activity [GO:0050630]; protein dimerization activity [GO:0046983]; S-adenosyl-L-methionine:eugenol-O-methyltransferase activity [GO:0102719]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(E)-isoeugenol + S-adenosyl-L-methionine = (E)-isomethyleugenol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17081, ChEBI:CHEBI:6877, ChEBI:CHEBI:15378, ChEBI:CHEBI:50545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.146; | null | null | null | null | FUNCTION: Catalyzes the methylation of the para-4-hydroxyl of both eugenol and (iso)eugenol to methyleugenol and isomethyleugenol, respectively. The resulting products are part of a complex mixture of low-molecular-weight volatile compounds emitted by the flowers to attract pollinators. | Clarkia breweri (Fairy fans) (Eucharidium breweri) |
O04468 | STMP6_ARATH | MGMKSPNIAAFMLPLLLILFTLSSQLKVVESTGRKLAWGFSGTPIVYTPPSRSCGTSPAVFTSKWRRPRPCRLPPGSYIPASDQSP | null | null | response to bacterium [GO:0009617]; response to cold [GO:0009409]; response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | apoplast [GO:0048046]; plasma membrane [GO:0005886] | LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612] | null | null | Serine rich endogenous peptide (SCOOP) phytocytokine family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of STMP6 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP6 in the apoplasm. {ECO:0000269|PubMed:31001913}. | null | null | null | null | null | FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation... | Arabidopsis thaliana (Mouse-ear cress) |
O04479 | AS2_ARATH | MASSSTNSPCAACKFLRRKCQPECVFAPYFPPDQPQKFANVHKVFGASNVTKLLNELHPSQREDAVNSLAYEADMRLRDPVYGCVGVISLLQHQLRQLQIDLSCAKSELSKYQSLGILAATHQSLGINLLAGAADGTATAVRDHYHHHQFFPREQMFGGLDVPAGNNYDGGILAIGQITQFQQPRAAAGDDGRRTVDPS | null | null | adaxial/abaxial axis specification [GO:0009943]; petal development [GO:0048441]; polarity specification of adaxial/abaxial axis [GO:0009944]; proximal/distal pattern formation [GO:0009954]; specification of symmetry [GO:0009799] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | null | PF03195; | null | LOB domain-containing protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12040093, ECO:0000269|PubMed:23271976}. | null | null | null | null | null | FUNCTION: Negative regulator of cell proliferation in the adaxial side of leaves. Regulates the formation of a symmetric lamina and the establishment of venation. Positively regulates LATERAL ORGAN BOUNDARIES (LOB) within the shoot apex, and the class III HD-ZIP genes REV, PHB, and PHV. Interacts directly with ASYMMETR... | Arabidopsis thaliana (Mouse-ear cress) |
O04482 | UCH2_ARATH | MSWCTIESDPGVFTELIQQMQVKGVQVEELYSLDSDSLNNLRPVYGLIFLFKWQAGEKDERPTIQDQVSNLFFANQVINNACATQAILAILLNSPEVDIGPELSALKEFTKNFPSDLKGLAINNSDSIRAAHNSFARPEPFVPEEQKAATKDDDVYHFISYIPVDGVLYELDGLKEGPISLGPCPGDQTGIEWLQMVQPVIQERIERYSQSEIRFNLLAVIKNRKDIYTAELKELQRQREQLLQQANTCVDKSEAEAVNALIAEVGSGIEAASDKIVMEEEKFMKWRTENIRRKHNYIPFLFNFLKLLAEKKQLKPLIEK... | 3.4.19.12 | null | protein deubiquitination [GO:0016579]; shoot system morphogenesis [GO:0010016]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; Ino80 complex [GO:0031011]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF01088;PF18031; | 1.20.58.860;3.40.532.10; | Peptidase C12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}. Cytoplasm {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Ubiquitin-protein hydrolase involved in the release of ubiquitin attached via both peptide and isopeptide linkages. Able to cleave 'Lys-48'-linked polyubiquitin chains. Involved in the direct or indirect regulation of AUX/IAA proteins stability (PubMed:17559514). Acts as a linker between the TREX-2 complex an... | Arabidopsis thaliana (Mouse-ear cress) |
O04492 | DRB1_ARATH | MTSTDVSSGVSNCYVFKSRLQEYAQKYKLPTPVYEIVKEGPSHKSLFQSTVILDGVRYNSLPGFFNRKAAEQSAAEVALRELAKSSELSQCVSQPVHETGLCKNLLQEYAQKMNYAIPLYQCQKVETLGRVTQFTCTVEIGGIKYTGAATRTKKDAEISAGRTALLAIQSDTKNNLANYNTQLTVLPCEKKTIQAAIPLKETVKTLKARKAQFKKKAQKGKRTVAKNPEDIIIPPQPTDHCQNDQSEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGL... | null | null | leaf proximal/distal pattern formation [GO:0010589]; leaf vascular tissue pattern formation [GO:0010305]; miRNA processing [GO:0035196]; miRNA-mediated gene silencing by mRNA destabilization [GO:0035279]; pre-miRNA processing [GO:0031054]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response... | nuclear dicing body [GO:0010445]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; miRNA binding [GO:0035198]; ribonuclease III activity [GO:0004525] | PF00035; | 3.30.160.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14722360, ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:17442570}. Nucleus speckle {ECO:0000269|PubMed:26227967}. Note=Localizes to nuclear dicing body (also named D body), a nuclear body distributed throughout the nucleoplasm and involved in miRNA processing. | null | null | null | null | null | FUNCTION: Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus. Forms a complex with SERRATE (SE) and D... | Arabidopsis thaliana (Mouse-ear cress) |
O04499 | PMG1_ARATH | MATSSAWKLDDHPKLPKGKTIAVIVLDGWGESAPDQYNCIHNAPTPAMDSLKHGAPDTWTLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIFAQGAKLCDQALASGKIFEGEGFKYVSESFETNTLHLVGLLSDGGVHSRLDQLQLLIKGSAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLVALRENGVDAQIASGGGRMYVTLDRYENDWEVVKRGWDAQVLGEAPHKFKNAVEAVKTLRKEPGANDQYLPPFVIVDESGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYEDFDKFDRVRYPKIRYAGMLQY... | 5.4.2.12 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9X519}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q9X519}; | glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096]; pollen development [GO:0009555]; response to abscisic acid [GO:0009737]; response to blue light [GO:0009637]; response to carbon dioxide [GO:0010037]; response to cold [GO:0009409]; stomatal movement [GO:0010118] | chloroplast [GO:0009507]; cytosol [GO:0005829]; extracellular region [GO:0005576]; mitochondrial envelope [GO:0005740]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506] | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity [GO:0046537]; manganese ion binding [GO:0030145] | PF06415;PF01676; | 3.40.720.10;3.40.1450.10; | BPG-independent phosphoglycerate mutase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.12; Evidence={ECO:0000269|PubMed:21813794}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000250|UniProtKB:Q9X519}. | null | null | FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA) (PubMed:21813794). Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production) (PubMed:21813794). {ECO:0000269|PubM... | Arabidopsis thaliana (Mouse-ear cress) |
O04523 | TBL27_ARATH | MGLNEQQNVPSQRKIIVFIVLAFIPIALFRLCFNNPFSSIKDTSLQDSAANVVITSFSSSSQEEESQESFDHIQDEPLCDYTQGNWVRDEIGPLYNGSTCGTIKDGQNCFRHGRPDSGYLYWKWKPNECDIPRFDSNRFLDLMRDKHLAFIGDSMARNQLESLLCLLSTVSSPDLVYRNGEDNKFRRWRFESHNVTVSVYWSPFLVAGLEKSGNLDHNVLHIDRVDERWGNDLERFDTVVVSVGHWFLHPAVYYESGSVLGCHSCETSNCTEVGFYDVFRKAIRTTLRAVAGSGREVILTTFSPSHFEGRPWDSLGACNM... | 2.3.1.- | null | xyloglucan metabolic process [GO:0010411] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | O-acetyltransferase activity [GO:0016413] | PF13839;PF14416; | null | PC-esterase family, TBL subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.63 mM for xyloglucan oligomer {ECO:0000269|PubMed:30083810}; Vmax=65.4 pmol/min/mg enzyme with xyloglucan oligomer as substrate {ECO:0000269|PubMed:30083810}; | null | null | null | FUNCTION: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains (PubMed:30083810). Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers (PubMed:30083810). Involved in xyloglucan specifi... | Arabidopsis thaliana (Mouse-ear cress) |
O04529 | 2MMP_ARATH | MRFCVFGFLSLFLIVSPASAWFFPNSTAVPPSLRNTTRVFWDAFSNFTGCHHGQNVDGLYRIKKYFQRFGYIPETFSGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHIVIPRCGNPDVVNGTSLMHGGRRKTFEVNFSRTHLHAVKRYTLFPGEPRWPRNRRDLTYAFDPKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHAFSPPSGKFHLDADENWVVSGDLDSFLSVTAAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEGIQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | collagen catabolic process [GO:0030574]; defense response to fungus [GO:0050832]; developmental vegetative growth [GO:0080186]; extracellular matrix organization [GO:0030198]; negative regulation of leaf senescence [GO:1900056]; proteolysis [GO:0006508]; regulation of photoperiodism, flowering [GO:2000028]; response to... | apoplast [GO:0048046]; extracellular matrix [GO:0031012]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF00413;PF01471; | 3.40.390.10; | Peptidase M10A family, Matrix metalloproteinases (MMPs) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:24156403}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:24156403}; | FUNCTION: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Required for plant growth, morphogenesis, and development with particular relevance for flowering and senescence (Pub... | Arabidopsis thaliana (Mouse-ear cress) |
O04616 | CUT1A_ARATH | MAISVAASSSMAVMVPRVPAVSTRCSAVPYLPPRSFGRSSFTVPLKLVSGNGLQKVELLKTRASSEETSSIDTNELITDLKEKWDGLENKSTVLIYGGGAIVAVWLSSIVVGAINSVPLLPKVMELVGLGYTGWFVYRYLLFKSSRKELAEDIESLKKKIAGSE | null | null | granum assembly [GO:0090391]; membrane bending [GO:0097753] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829]; granal stacked thylakoid [GO:0009515]; plastoglobule [GO:0010287]; thylakoid [GO:0009579] | null | PF14159; | null | CURT family | null | SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. Note=Located almost exclusively at grana margins. {ECO:0000269|PubMed:23839788}. | null | null | null | null | null | FUNCTION: Determines thylakoid architecture by inducing membrane curvature. {ECO:0000269|PubMed:23839788}. | Arabidopsis thaliana (Mouse-ear cress) |
O04663 | IF4E4_ARATH | MATDDVNEPLPAAAELPATEAEKQPHKLERKWSFWFDNQSKKGAAWGASLRKAYTFDTVEDFWGLHETIFQTSKLTANAEIHLFKAGVEPKWEDPECANGGKWTWVVTANRKEALDKGWLETLMALIGEQFDEADEICGVVASVRPQSKQDKLSLWTRTKSNEAVLMGIGKKWKEILDVTDKITFNNHDDSRRSRFTV | null | null | negative regulation of defense response to virus [GO:0050687]; response to virus [GO:0009615] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]; plastid [GO:0009536] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-97-Cys-138 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Mediates susceptibility to Turnipmosaic potyvirus (TuMV) and Tobacco etch potyvirus (TEV). {E... | Arabidopsis thaliana (Mouse-ear cress) |
O04705 | GAO1D_WHEAT | MVQPVFDAAVLSGRADIPSQFIWPEGESPTPDAAEELHVPLIDIGGMLSGDPAAAAEVTRLVGEACERHGFFQVVNHGIDAELLADAHRCVDNFFTMPLPEKQRALRHPGESCGYASSFTGRFASKLPWKETLSFRSCPSDPALVVDYIVATLGEDHRRLGEVYARYCSEMSRLSLEIMEVLGESLGVGRAHYRRFFEGNDSIMRLNYYPPCQRPLETLGTGPHCDPTSLTILHQDNVGGLQVHTEGRWRSIRPRADAFVVNIGDTFMALSNGRYKSCLHRAVVNSRVPRKSLAFFLCPEMDKVVAPPGTLVDAANPRAY... | 1.14.11.- | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; | flower development [GO:0009908]; gibberellin biosynthetic process [GO:0009686]; response to light stimulus [GO:0009416]; unidimensional cell growth [GO:0009826] | null | gibberellin 20-oxidase activity [GO:0045544]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family, GA20OX subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + gibberellin A12 + H(+) + 3 O2 = 3 CO2 + gibberellin A9 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60772, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58627, ChEBI:CHEBI:73255; Evidence={ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 nM for GA12 {ECO:0000269|PubMed:16160850}; KM=59 nM for GA53 {ECO:0000269|PubMed:16160850}; KM=367 nM for GA15 {ECO:0000269|PubMed:16160850}; KM=3993 nM for GA44 {ECO:0000269|PubMed:16160850}; KM=820 nM for GA24 {ECO:0000269|PubMed:16160850}; KM=8640 nM for GA19... | null | null | null | FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA skeleton. {ECO:0000269|PubMed:16160850}. | Triticum aestivum (Wheat) |
O04714 | GCR1_ARATH | MSAVLTAGGGLTAGDRSIITAINTGASSLSFVGSAFIVLCYCLFKELRKFSFKLVFYLALSDMLCSFFLIVGDPSKGFICYAQGYTTHFFCVASFLWTTTIAFTLHRTVVKHKTDVEDLEAMFHLYVWGTSLVVTVIRSFGNNHSHLGPWCWTQTGLKGKAVHFLTFYAPLWGAILYNGFTYFQVIRMLRNARRMAVGMSDRVDQFDNRAELKVLNRWGYYPLILIGSWAFGTINRIHDFIEPGHKIFWLSVLDVGTAALMGLFNSIAYGFNSSVRRAIHERLELFLPERLYRWLPSNFRPKNHLILHQQQQQRSEMVSL... | null | null | abscisic acid-activated signaling pathway [GO:0009738]; activation of phospholipase C activity [GO:0007202]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; blue light signaling pathway [GO:0009785]; brassinosteroid mediated signaling pathway [GO:0009742]; cell surface receptor s... | Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930] | PF05462; | 1.20.1070.10; | G-protein coupled receptor 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15181210, ECO:0000269|Ref.7}; Multi-pass membrane protein {ECO:0000269|PubMed:15181210, ECO:0000269|Ref.7}. Note=Localized to the outer edge of the leaf epidermal cells in a punctuate pattern. | null | null | null | null | null | FUNCTION: Together with GPA1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP(3)) as a second messenger. Promotes PI-PLC activity and IP(3) accumulation. Involved in the blue light (BL) signaling. Tog... | Arabidopsis thaliana (Mouse-ear cress) |
O04719 | P2C77_ARATH | MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEV... | 3.1.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11882947, ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11882947}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000269|PubMed:11882947, ECO:0000269|Pu... | abscisic acid-activated signaling pathway [GO:0009738]; negative regulation of abscisic acid-activated signaling pathway [GO:0009788]; negative regulation of protein kinase activity [GO:0006469]; photoinhibition [GO:0010205]; regulation of stomatal opening [GO:1902456]; response to abscisic acid [GO:0009737]; response ... | nucleus [GO:0005634] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00481; | 3.60.40.10; | PP2C family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11882947}; CATALYTIC ACTIVITY: Reaction=H... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:11882947}; | null | FUNCTION: Repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation,... | Arabidopsis thaliana (Mouse-ear cress) |
O04795 | PERA_IPOBA | MASFMKQLSLVLSFIALALAGCAVYQNTQTAMKDQLKVTPTWLDNTLKSTNLLSLGLGKPSGGKLGDEACVFSAVKEVVVAAINAEARMGASLIRLFFHDCFVDGCDAGLLLNDTATFTGEQTAAGNNNSVRGFAVIEQAKQNVKTQMPDMSVSCADILSIAARDSFEKFSGSTYTVTLGRKDARTANFTGANTQLVGPNENLTSQLTKFAAKGFNGTEMVALLGSHTIGFARCPLLCISTFINPARVSTLNCNCSGTVNATGLVGLDPTPTTWDQRYFSDVVNDQGLLFSDNELLKGNTTNAAVRRYRDAMGAFLTDFA... | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Classical plant (class III) peroxidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | null | null | null | null | FUNCTION: 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.; FUNCTION: May... | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
O04796 | PERN_IPOBA | MASFVARLTLALSFIALALAGYSLVQNTLSSPTHTRLNLIPTWLDSTFDSADVLSYLGFGKSSGRLSDSNCVFSAVKEIVDAAITAETRMGASLIRLHFHDCFVDGCDGGILLNDTANFTGEQGAPANSNSVRGFSVIDQAKRNAQTKCADTPVSCADVLAIAARDAFRKFTNQTYNITLGRQDARTANLTGANTQLPAPFDNLSIQTAKFADKGFNQREMVVLAGAHTVGFSRCAVLCTSTNLNQNRSATLQCTCPASANDTGLVGLDPSPGTFDKKYFEELVKGQGLLFSDQELMQSNATVTAVRRYRDATGAFLTDF... | 1.11.1.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Classical plant (class III) peroxidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | null | null | null | null | FUNCTION: 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.; FUNCTION: May... | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
O04846 | ATCA1_ARATH | MKIMMMIKLCFFSMSLICIAPADAQTEGVVFGYKGKNGPNQWGHLNPHFTTCAVGKLQSPIDIQRRQIFYNHKLNSIHREYYFTNATLVNHVCNVAMFFGEGAGDVIIENKNYTLLQMHWHTPSEHHLHGVQYAAELHMVHQAKDGSFAVVASLFKIGTEEPFLSQMKEKLVKLKEERLKGNHTAQVEVGRIDTRHIERKTRKYYRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDTSFKNNSRPCQPLNGRRVEMFHDHERVDKKETGNKKKKPN | 4.2.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | one-carbon metabolic process [GO:0006730] | chloroplast stroma [GO:0009570]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886] | carbonate dehydratase activity [GO:0004089]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-class carbonic anhydrase family | PTM: N-glycosylation is required for activity and chloroplast targeting, probably by facilitating folding and endoplasmic reticulum (ER) export. {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}.; PTM: Disulfide bridge between Cys-52 and Cys-216 is required for correct folding. | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}. Endoplasmic reticulum {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}. Note=When glycosylated and folded, targeted to the chloroplast via a protein-targeting pathway that uses the secretory system vi... | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:21695217}; | null | null | null | null | FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
O04862 | FOLM_PEA | MSILKCLGVRGNQLCAARNYLKVLGFSSFHTAPNSSIEIQTQDEEVVIALGSNVGDRLHNFKEALKLMRKSGIHITRHASLYETAPAYVTDQPRFLNSAVRADTKLGPHELLAALKRIEKDMGRTDGIRYGPRPIDLDILFYGKFKVRSDILTVPHERIWERPFVMAPLMDLLGTAIDSDTVASWHSFSGHSGGLNALWEKLGGESLIGEEGMYRVMPVANGLLDWSRRTLVMGILNLTPDSFSDGGNFQSVKSAVSQARLMISEGADIIDIGAQSTRPMASRISAEEELGRLIPVLEAVMSIPEVEGKLISVDTFYSEV... | 2.5.1.15; 2.7.6.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0AC13}; | folic acid biosynthetic process [GO:0046656]; phosphorylation [GO:0016310]; tetrahydrofolate biosynthetic process [GO:0046654] | cytosol [GO:0005829]; mitochondrial envelope [GO:0005740]; mitochondrion [GO:0005739] | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity [GO:0003848]; ATP binding [GO:0005524]; dihydropteroate synthase activity [GO:0004156]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287] | PF01288;PF00809; | 3.30.70.560;3.20.20.20; | HPPK family; DHPS family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9118956}. | CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3; Evidence={ECO:0000269|PubMed:9118956}; CATALYTIC ACTIVITY: Rea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 uM for 6-hydroxymethyl-7,8-dihydropterin {ECO:0000269|PubMed:9118956}; KM=70 uM for ATP {ECO:0000269|PubMed:9118956}; KM=30 uM for 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate {ECO:0000269|PubMed:9118956}; KM=0.6 uM for p-aminobenzoic acid {ECO:0000269|PubMe... | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4. {ECO:0000305}.; PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-... | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:9118956}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:9118956}; | FUNCTION: Catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis. {ECO:0000269|PubMed:9118956}. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
O04905 | KCY3_ARATH | MGSVDAANGSGKKPTVIFVLGGPGSGKGTQCAYIVEHYGYTHLSAGDLLRAEIKSGSENGTMIQNMIKEGKIVPSEVTIKLLQKAIQENGNDKFLIDGFPRNEENRAAFEKVTEIEPKFVLFFDCPEEEMEKRLLGRNQGREDDNIETIRKRFKVFLESSLPVIHYYEAKGKVRKINAAKPIEAVFEEVKAIFSPEAEKVEA | 2.7.4.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; CDP biosynthetic process [GO:0046705]; phosphorylation [GO:0016310]; pyrimidine nucleotide biosynthetic process [GO:0006221]; pyrimidine ribonucleoside monophosphate metabolic process [GO:0009173]; UDP biosynthetic process [GO:0006225] | cytosol [GO:0005829]; nucleus [GO:0005634]; plastid [GO:0009536] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; CMP kinase activity [GO:0036430]; cytidylate kinase activity [GO:0004127]; dCMP kinase activity [GO:0036431]; nucleoside diphosphate kinase activity [GO:0004550]; UMP kinase activity [GO:0033862]; UMP/dUMP kinase activity [GO:0009041] | PF00406; | 3.40.50.300; | Adenylate kinase family, UMP-CMP kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. | CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:9576794}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29.3 uM for ATP (with UMP as cosubstrate) {ECO:0000269|PubMed:9576794}; KM=291.7 uM for ATP (with CMP as cosubstrate) {ECO:0000269|PubMed:9576794}; KM=152.9 uM for UMP {ECO:0000269|PubMed:9576794}; KM=266.4 uM for CMP {ECO:0000269|PubMed:9576794}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:9576794}; | null | FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Does not act on dCMP and dUMP. | Arabidopsis thaliana (Mouse-ear cress) |
O04921 | HEMH2_ARATH | MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLI... | 4.98.1.1 | null | heme biosynthetic process [GO:0006783]; porphyrin-containing compound biosynthetic process [GO:0006779]; tetrapyrrole biosynthetic process [GO:0033014] | chloroplast membrane [GO:0031969]; chloroplast thylakoid membrane [GO:0009535]; mitochondrion [GO:0005739]; plastid thylakoid membrane [GO:0055035] | ferrochelatase activity [GO:0004325] | PF00762; | 3.40.50.1400;1.10.3460.10; | Ferrochelatase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:9210462}; Peripheral membrane protein {ECO:0000305|PubMed:9210462}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:9210462}; Peripheral membrane protein {ECO:0000305|PubMed:9210462}. Note=(PubMed:11602264) shows experimental evidences ... | CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1; Evidence={ECO:0000305}; | null | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the last step of heme biosynthesis by inserting ferrous iron into protoporphyrin IX to produce protoheme. Produces heme for photosynthetic cytochromes, and for proteins involved in abiotic and biotic stress responses (PubMed:24329537). May play a role in the quality control of individual chloroplast... | Arabidopsis thaliana (Mouse-ear cress) |
O04951 | PP2A5_ARATH | MPPATGDIDRQIEQLMECKALSETEVKMLCEHAKTILVEEYNVQPVKCPVTVCGDIHGQFYDLIELFRIGGSSPDTNYLFMGDYVDRGYYSVETVSLLVALKVRYRDRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKHFTDLFDYLPLTALIESQVFCLHGGLSPSLDTLDNIRSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDIATQFNHTNGLSLISRAHQLVMEGFNWCQEKNVVTVFSAPNYCYRCGNMAAILEIGENMDQNFLQFDPAPRQVEPETTRKTPDYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | mitotic cell cycle [GO:0000278]; regulation of auxin polar transport [GO:2000012] | cytosol [GO:0005829]; nucleus [GO:0005634]; peroxisome [GO:0005777] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-2A subfamily | PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl methyltransferase 1 (LCMT1) and pectin methylesterase 1 (PME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity an... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25489022}. Peroxisome {ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA in the cytosol and peroxisomal import occurs by a piggybacking transport. {ECO:0000269|PubMed:25489022}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins (PubMed:25489022). Involved in the positive regulation of salt stress... | Arabidopsis thaliana (Mouse-ear cress) |
O04983 | ACCC_ARATH | MDASMITNSKSITSPPSLALGKSGGGGVIRSSLCNLMMPSKVNFPRQRTQTLKVSQKKLKRATSGGLGVTCSGGDKILVANRGEIAVRVIRTAHEMGIPCVAVYSTIDKDALHVKLADEAVCIGEAPSNQSYLVIPNVLSAAISRGCTMLHPGYGFLSENALFVEMCRDHGINFIGPNPDSIRVMGDKATARETMKNAGVPTVPGSDGLLQSTEEAVRVANEIGFPVMIKATAGGGGRGMRLAKEPGEFVKLLQQAKSEAAAAFGNDGCYLEKFVQNPRHIEFQVLADKFGNVVHFGERDCSIQRRNQKLLEEAPSPALT... | 6.3.4.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00969}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00969}; | fatty acid biosynthetic process [GO:0006633]; malonyl-CoA biosynthetic process [GO:2001295] | chloroplast [GO:0009507] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin carboxylase activity [GO:0004075]; metal ion binding [GO:0046872] | PF02785;PF00289;PF02786; | 3.40.50.20;3.30.1490.20;3.30.470.20; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for biotin {ECO:0000269|PubMed:9414551}; KM=88 mM for bicarbonate {ECO:0000269|PubMed:9414551}; Vmax=16 nmol/min/mg enzyme {ECO:0000269|PubMed:9414551}; | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3-8.9. {ECO:0000269|PubMed:9414551}; | null | FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000269|PubMed:9414551}. | Arabidopsis thaliana (Mouse-ear cress) |
O04985 | NSHB2_ORYSJ | MALVEGNNGVSGGAVSFSEEQEALVLKSWAIMKKDSANIGLRFFLKIFEVAPSASQMFSFLRNSDVPLEKNPKLKTHAMSVFVMTCEAAAQLRKAGKVTVRDTTLKRLGATHFKYGVGDAHFEVTRFALLETIKEAVPVDMWSPAMKSAWSEAYNQLVAAIKQEMKPAE | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P68168}; Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:P68168}; | cellular response to potassium ion starvation [GO:0051365]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to nitrite [GO:0080033] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low ... | Oryza sativa subsp. japonica (Rice) |
O04986 | NSHB1_ORYSJ | MALVEDNNAVAVSFSEEQEALVLKSWAILKKDSANIALRFFLKIFEVAPSASQMFSFLRNSDVPLEKNPKLKTHAMSVFVMTCEAAAQLRKAGKVTVRDTTLKRLGATHLKYGVGDAHFEVVKFALLDTIKEEVPADMWSPAMKSAWSEAYDHLVAAIKQEMKPAE | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175}; Note=Binds 1 heme group per subunit. {ECO:0000269|PubMed:10986467, ECO:0000269|PubMed:16893175}; | response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to nitrite [GO:0080033] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (PubMed:21495624). May not function as an oxygen storage or transport protein (PubMed:17540516, PubMed:9390447). Has an unusually high affinity for O(2) through an hexacoordinate heme iron be... | Oryza sativa subsp. japonica (Rice) |
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