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
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O02228 | SC5A7_CAEEL | MADLLGIVAIVFFYVLILVVGIWAGRKSKSSKELESEAGAATEEVMLAGRNIGTLVGIFTMTATWVGGAYINGTAEALYNGGLLGCQAPVGYAISLVMGGLLFAKKMREEGYITMLDPFQHKYGQRIGGLMYVPALLGETFWTAAILSALGATLSVILGIDMNASVTLSACIAVFYTFTGGYYAVAYTDVVQLFCIFVGLWVCVPAAMVHDGAKDISRNAGDWIGEIGGFKETSLWIDCMLLLVFGGIPWQVYFQRVLSSKTAHGAQTLSFVAGVGCILMAIPPALIGAIARNTDWRMTDYSPWNNGTKVESIPPDKRNMVVPLVFQYLTPRWVAFIGLGAVSAAVMSSADSSVLSAASMFAHNIWKLTIRPHASEKEVIIVMRIAIICVGIMATIMALTIQSIYGLWYLCADLVYVILFPQLLCVVYMPRSNTYGSLAGYAVGLVLRLIGGEPLVSLPAFFHYPMYTDGVQYFPFRTTAMLSSMATIYIVSIQSEKLFKSGRLSPEWDVMGCVVNIPIDHVPLPSDVSFAVSSETLNMKAPNGTPAPVHPNQQPSDENTLLHPYSDQSYYSTNSN | 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 | MSSISNNPDFSSIDPAVLMSLLMKSSGSLPTPPDTHSDGSESPDSTASDSSDKKRRRKPESKDIVRVAEEAEAAAATCSSIPSSSDTKENETEEDQNMTCDTTTNNAQKPTEQTATSADVVTSSVPSGLEGVPSFLFSQFMAPSFQKQLEIFTSGNMMSATHSDTSPSDVDSVLDGGVVTAEETSSSKSPMMTSSDTPKTPLTASSPPHSSGSESRVMSPITHTNISDELSISTTPTVAFTPNGSIPSPGTGYSWSIRREGKLACPTPGCDGSGHQTGLYTHHRSLSGCPRRPDKTVIQMLALRQDTVLRCTTAGCSGKGHVNGNRTSHRSLSGCPIAHQEKLARKGIKTTPQRTKTPIKGISISDECPLDLTLSGLPAGLSAQQLLAAAQAGLIPSSQMMDALFQQFSQTQPLATLEEESKKENEMEVDVETTSDDIPTLIKEEEEVKCESPVPSVIPEIQSTPSRPVAAPVAPGSAEKSSPTSQMLLQMPGFSEALLKMTAPQVPFPQYSPQAALFGNQSALLAQIMLTQLQMQQGF | 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 transdifferentiation [GO:1903620] | 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 generation of postembryonic neurons from epidermal cells (PubMed:31386623). {ECO:0000269|PubMed:31386623}. | Caenorhabditis elegans |
O02279 | NHR62_CAEEL | MFSTLSPSAIDDILRHAVHFGQGTTAIAPSPVTFISTTTQQSLGATYPGVFNPTTPTFNHYQHQALPVTMHTSTSSAHHTTTGHGRGRRKNSTINLVCVVCGDQAFGKHYGVNACNGCKGFFRRSVWHNRQYLCRFEGRCAIAKEHRNVCRACRLKQCFVAGMNPRAVQSERVEREQNGSPNQIEEDDYKDLSSPDTCSVEIQTDVDEQKPSSNNSAPLPSMELEMAKLSEQIVEMHRAVCSYVDPVTKRENFDMKMETETTKIAFMNAFYNPEMIGPRTPLDITGRRVATVKDVMDEWKRNFVLFSDWLRALPEYNQMSIEDQIVLAKNRYGTFHWWMCANWTVQAGCEGVCYSNGAYFPKQPEAQCIPDVKGSSGRMYDSLSIPIKELNLDETEIVLMLAVIIFSDEITELADLTPAGKEHVRMVGNRFVRMLHHHVNSKEYGEAMENGDDTQNSSESQAAVRIAKMMILLSATTNLVYLTSDNIQLMEVLHVVPSEYLCHEVQFIQNSYETP | 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 transcription of target genes (PubMed:23935515). {ECO:0000269|PubMed:23935515}. | Caenorhabditis elegans |
O02298 | GCY35_CAEEL | MFGWIHESFRQLVTRKYGKDIWEKIVHMSKFELGTESEIAHYYNDDETLRLVNSMANVIGIPIEEIWEAYGGFLIQFTMETGWDELLRAMAPDLEGFLDSLDSLHYFIDHVVYKTKLRGPSFRCDVQADGTLLLHYYSKRSGLYPIVKGVVREVARRIYDTEVVMKVQERKQEHLDAFVTEHVVFVITQIENANSTQPKSISSKADSQIDLSTGIYEISSSDFSLAFPYHICFDPDLFVEHFGNFIKKTFPNAMRQETRVTDLLELVHPEVPFSYESIKYYKNSLFVFRLKGLGDIVHNANDEAKTVLLKGSMVFIDEGKYILYMCSVNVTTVRELIERNLHLSDMQRHDGTRDVIMLNQSRMSQVELNRTLEETTKKLKKMAQELEIEKQKTDELLCELMPASVADSLRSGKAMDAKEFADCTLLFTDIVTFTNICAMCTPYDVVTLLNDLYLRFDRLVGLHDAYKVETIGDAYMIVGGVPERCENHAERVLNISIGMLMESKLVLSPITHKPIKIRLGVHCGPVVAGVVGIKMPRYCLFGDTVNVANKMESNGIQCKIHVSETGKLNGLKANPSYVFIDRGNTEIRGKGMMYTYFLERNDRKSVWELCSRPRSGEQTIDGYMELHDQSIYQEEGGQQENLTVENGNSAQNNHNNNNNTHHSGRKLMNGSSVDPGSHHIRSPTCTIS | 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 is implicated in oxygen sensation. Indeed, C.elegans exhibits a strong behavioral preference for 5-12% oxygen, avoiding higher and lower oxygen levels; a higher level of oxygen inducing a naturally polymorphic social feeding behavior. Involved in avoidance of hyperoxia and for oxygen-induced aggregation and bordering, probably by mediating oxygen-sensing in URX, AQR and PQR sensory neurons. {ECO:0000269|PubMed:15203005, ECO:0000269|PubMed:15220933}. | 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 the nucleus where it activates the transcription of genes promoting longevity and activation of mitochondrial beta oxidation (PubMed:25554789, PubMed:30713071). {ECO:0000269|PubMed:25554789, ECO:0000269|PubMed:30713071, ECO:0000269|PubMed:31292465}. | Caenorhabditis elegans |
O02326 | CFI1_CAEEL | MSVRIDEPQLFVSMSKEPTQETVNVGGHHDDSSSNCDERVDDQTEEQKSPPASPDLTANLNVFDLESRQKVVQRLLNSQLNLSNLRAPLNLPPIFQALQGPFSIQQQLLGLASGLTAISPGLDDYDEENTNQGEPEDLTLGGFRKETSVKSEEPSESGINASGPAWSYEEQFKQLYELSDDVKRKEWLDDWLNFMHRIGKPVTRIPIMAKQVLDLYELYRLVVQHGGLVEIINKKLWREITKGLNLPSSITSAAFTLRTQYQKYLYDYECEKEKLSNQSDLQQAIDGNRREAPGRRTAPSFPLPFQLPHAASAAATMLNNQLNGLGMRNDLLDDENTLSLQASGLFGTSYGAEQMAILEAHQRNLERAQRAVQQQVARQSLGLTACSNGNGGNIHNSGRESTSSNDSDIPAKRPKLENDVKTNGASSMRISTKHSDNSKTSMSVSMEINGITYQGVLFALDETVSES | 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 transcription by RNA polymerase II [GO:0006357] | 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 neurons (PubMed:28056346). Probably acts by binding to specific promoter elements (PubMed:28056346). Promotes differentiation of URA sensory neurons and prevents them from expressing male-specific CEM neuronal features (PubMed:11959845). Promotes differentiation of AVD and PVC interneurons and their glutamate receptor expression (PubMed:11959845). {ECO:0000269|PubMed:11959845, ECO:0000269|PubMed:28056346}. | Caenorhabditis elegans |
O02365 | IFA2_CAEEL | MTDPDSYRSSITSRPSFNRTVTSSSQNYGAPGSGNRVLKIVTETHSSSVSSGLSPYGQNAASTIRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQIMNGNRNDMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDKDAQIRKLREECQALMVELQMLLDTKQTLDGELKVYRQMLEGNSEGNGLRQLVEKVVRTSAINEEADTETMRVVKGEHSSRTSYQRSAKGNVAIKETSPEGKFVILENTHRAKEEPLGDWKLKRKIDGKREIVFTFPSDYILHPFQSVKIFARGQGIANPPEVLIFEGDETFGVGANVQTILYNNKGEERATHIQRQSQQTTSS | 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. Although expressed during embryogenesis, it is not required for embryonic development of muscle-cuticle linkages nor for the localization of other proteins to the hemidesmosomes in embryos. {ECO:0000269|PubMed:11427699, ECO:0000269|PubMed:14597206}. | 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 inhibiting these neurons. Acts in concert with Snmp and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Required for cVA response, probably by binding to VA. May act by serving as an adapter that bridges the presence of gaseous pheromone molecules, cVA, to activation of specific neuronal receptors expressed on T1 olfactory neurons, possibly via a specific conformational change induced by cVA that in turn activates T1 receptors. T1 neurons are excited by the pheromone VA, while T2 neurons are inhibited by alcohols. Also binds to phthalates. {ECO:0000269|PubMed:11238251, ECO:0000269|PubMed:14759510, ECO:0000269|PubMed:15664171, ECO:0000269|PubMed:16928861, ECO:0000269|PubMed:17943085, ECO:0000269|PubMed:9755202}. | Drosophila melanogaster (Fruit fly) |
O02373 | UGDH_DROME | MKVCCIGAGYVGGPTCAVMALKCPDIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADLIFISVNTPTKTCGNGKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRANQKPGIHYDILSNPEFLAEGTAINDLLNADRVLIGGEETPEGHQAVEKLSWIYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAYWQQVIDMNEYQKRRFSQKIIESLFNTVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIIDDLTHPSVTESPEKVKKAVQIHSDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAYIFDGRKILDHERLQQIGFHVQTIGKKYQRTGLLRSWGIVPQL | 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 process [GO:0015014]; mesoderm migration involved in gastrulation [GO:0007509]; segment polarity determination [GO:0007367]; UDP-glucuronate biosynthetic process [GO:0006065]; Wnt signaling pathway [GO:0016055] | 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 | MRVVDKMAGLMWAALTLVIGLGLLVPSNGEEYICDSMDIRNRVSNLRQLENCTVIEGYLQILLIDFAEEQDYSGLAFPNLVEITDYFLLYRVRGLTNLSELFPNLAVIRGTNLFFNYALVVFEMLDMQKIGLYSLQNITRGSVRIEKNPNLCYLDTIDWSFIAESGYSNNFIVDNREEEECVNFCPGRCRIKHPVLQDLCWAEEHCQKVCPESCLGNCRDGISGCCHENCIGGCDGPTERDCVACKYFVHNGECLIQCPPDTYQYKDRRCITEEECPNTTNSVWKLHHRKCIPECPSGYTTDINNPRLCTECEGQCPKSCKGGLVDSLAAAQRFRGCTIIEGELKISIRGGDNIIDELEENLGLIEEVGHYVAIVRSYALVTLDFLRSLKRIRGIQKENGYAFYVLDNRNLEKLFDWDRTDITIDEGKLFFHFNPKLCRHVILTMVDKVGLPEHAITDTDISTLTNGDQAQCSFSRLEIEEINTSKDMIILRWSEFRPPDPRDLLSYTVSYRETEDQGIDEYDGQDACGNTEWKEFDVSPTQTAHIITGLKPWTQYALLVKTYTKAGAREGSGAKSDIVYARTDADKPTHPQDVVVYSNSSNTLIITWKPPNRPNGNVTHYIVKYKRQQEDVAEMEQREYCKGGLKPHRPTQGLEDIVNNEEEPNNSTIGDGTCCECPKSEDEIRIEEEEAAFQQEFENFLHNNVYHKRENETRAGRRRRELPVTARPFYSNQTVNVTLPSTNRTVPPTPTPNPNPQLETTVWNEHMVVLTGLRHFSEYIIEVIACNADAAVGCSGSAVELARTQADDSADNIPGNITVVEIKEDMAKLYWPKPDSPNSMVVHYNIEYKKLGSDFNYEQQEPKCVENFKFLQSQGYTISNLVAGNYSVRFRATSFAGNGSWSNYVTFYVEEEDTSPDPQDPQQQVPVSLMIGMGVGFSLLLILAVIFGIWYCTKKRFGDKQMPNGVLYASVNPEYMSSDDVYVPDEWEVPREKITLIRELGQGSFGMVYEGEAKDVVKDEPMVSVAVKTVNESASIRERIEFLNEASVMKTFNCHHVVKLMGVVSKGQPTLVVMELMALGDLKNYLRRHRPEEDVGLSDSPASNEAKNSPFAENDNDLPPTFKDIIQMAGVIADGMSYLAAKKFVHRDLACRNCMVAQDRTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKVGVFTSQSDVWSYGVVLWEMATLASQPYQGKSNEEVLKFVIDGGMLEKPEGCPNKLYDLMKLCWQYRQSMRPTFLEIVEILSPELQAHFNEVSFYHSLDNHGREPLEMDDVALDSGADTETEMYPSGSEFSSTPSPPSETPYSHMNGSHPQNGSMNLRIPKSTLC | 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:PRU10028}; | 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 | MKASYLETLDRIKDEHAEMSKHVNQQRSDIEKVALEKENMNRSYMTYAEVSNTLRSDLRKAEEINKRLQEFIMQSLAPQLSQDNQANCLAALEAFKTASPRENGNGAPALPPGFPPGAAGMLGMMPNMPFGMSPAMSQLFNQFASPHVNGGDGAGGSSGGASEAKKAKLEDPDDGELEIDVTNDDHPSTASNGGAANKNGRDSTNSVASSGASTPSIASNSRARQQQQPLAGLQGLEQMNFLAGFNPNLLRQASAAGGFNFLNDPHAQARLAAAIGQIGSRPAYSFKIVDGGVPTPTSFPPDAQKGPGIPTGLKKKMELNHGEVVCAATISRDNSRVYTGGKGCVKIWDVKESDISGATVVNRPPIASLDCLKENYIRSCKLFEDGNTLLIGGEASTVALWDLTTETKTLDLETDSQACYALAMSPDEKLLFACLADGNILIYDIHNKVKVGTLPGHQDGASCLDLSKDGTKLWSGGLDNSVRCWDLAQRKEVAKHDFASQVFSLGCCPNDEWVAVGMENNYVEVLSTTGKEKYQLTQHESCVLSLKFAHSGKFFISTGKDNALNAWRTPYGASLFQLKENSSVLSCDISFDDSLIVTGSGEKKATLYAVEY | 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 (PubMed:10557206, PubMed:17289921). May function with transcription factor mls-1 to promote uterine muscle specification and formation (PubMed:21852953). {ECO:0000269|PubMed:21852953, ECO:0000269|PubMed:9165118}. | 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:0006906] | 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 {ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}. Synapse, synaptosome. Note=Observed in discrete synaptic vesicle puncta along the ventral cord. Functional unc-104, a kinesin-like protein, is required for localization. The two pools of synaptobrevin are recycled by clatherin- and dynamin- dependent endocytosis. AP180-like adapter protein, unc-11, is thought to act as a molecular chaperone. {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:10476681, ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:16844789}. | 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 | MEDLSDVFDIYAICACCKVAPTSEGTKNEPFSPRTFRGLGNKGTLPWKCNSVDMKYFSSVTTYVDESKYEKLKWKRERYLRMEASQGGGDNTSGGDNTHGGDNADKLQNVVVMGRSSWESIPKQYKPLPNRINVVLSKTLTKEDVKEKVFIIDSIDDLLLLLKKLKYYKCFIIGGAQVYRECLSRNLIKQIYFTRINGAYPCDVFFPEFDESQFRVTSVSEVYNSKGTTLDFLVYSKVGGGVDGGASNGSTATALRRTAMRSTAMRRNVAPRTAAPPMGPHSRANGERAPPRARARRTTPRQRKTTSCTSALTTKWGRKTRSTCKILKFTTASRLMQHPEYQYLGIIYDIIMNGNKQGDRTGVGVMSNFGYMMKFNLSEYFPLLTTKKLFLRGIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFHREVNDLGPIYGFQWRHFGAEYTNMHDNYEDKGVDQLKNVIHLIKNEPTSRRIILCAWNVKDLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTHMIAQVCNLQPAQFIHILGNAHVYNNHVDSLKVQLNRIPYPFPTLKLNPEVKNIEDFTISDFTIENYVHHDKITMEMAA | 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-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000269|PubMed:16135570}; | 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 | MNDKEKEICPRLIDFLVVVGKRNRTRGASQSSPDATTDTTVTYPEILRRYPTDDHKDFILPTDVTVFCQPEGCTTTSARLRKNARNDPQFFVFMLTEKDSAKVRYGICLNFYQSFDRRSTPKDEIKKVPDDAHHKKRDSHVSLTSLCFISHHPFVSIFHQVLLLLKRIIDSSNHRAAQRTGLKDVVWAILTGHYNEPIVPEVMKEIKEIETWILMLLSSPVPVPGKTKVQIEVMPMDLSQVFEFALPDHTRFTLIDFPLHIPFEILGIDMALRVLTAAMLEFKIVIQSRNYNAVSMCILSIVALLYPLEYMFPVIPLLPAYMPSAEQLLLAPTPFLIGVPSSFFHHRKIRELPSDVILVDLDTNCLQVPDDLYIPDLPEPDATHLKERLKNAINKMTTMTVDNETSVTDADFGIDIDSVDVACRVAMVQFFNSANVFGNFSEHTRTLRLYPRPVVSLQTDSFLRSRPQCTQLITDLCRTQAVEYFAECCLCPKNETFVRVQAGIESAEQVGDKPKWFSESLMPVHFMVYPNNSTLDSAIRVYNAEIDNDDYEDDSATSTENSNSIDDLVFDENQVTDAGGEVTKPLAEVNYIYKEPMTLELPQSESVVSIDSSLSSGRSSPDSSLSTSAVDSEADFARLADNLALKSNSQGAFSFDHGSDSEYESTPVSQRRKTIHNPGSDASDTPTSRGSIKSGLRMKGLTTLTDSGEKVLGPSLMNAINGYAEKSQSVFSQVINKTAPKAQALKERTMKPLANRIEQSQHIVRSKTQPNPTSQQTANQQSKNQQTVKEFCDQALVGQSVGMFSAPKLKRLMEDESLRELVCSKLNLGLEVKLSEDEYVKEVQLTKGQFKAYVKILKACLEGIEVSFNTPGCCGFASVFHVLEIAHTHYWAMGGGEVITPSSSAPSTMTTPSEHSNDILKESRPKLPASTIDLRTPTKPLGQNVTPTSTNNHEIAQSTRSPALPPPVPPREAPPIPKRNPPPLGAPPKVPEGARAPPPLPPRPKVKTTAVDETPQNLVPNNQPAQPSSPSFLADADEQTKPLLKPAPPTTLPVGKQEPCKVLPTPNEPVRHYIYQELILAVQHQIWQNLQFWENAFVDLVAQEREIVGMDQEPSEMIDRYSALNDSEKKRLELEEDRLLSTLLHNMTAYMIMCGTGQKALQQKVRRLLGKAHIGLVCSKEINKLLDELPSTQGNFIPLKPLGSRLVQKQSFTVCPGQSSDGQMMFMEVCDDAVVLRSITGAATERWWYERLVNITYSPKTKILCLWRRHDDKVHMHKFHTKKCRELYQCMKAAMERAAARGKVNVEGRALGGEFPVHDTETNQGGLLQVRCDGVAVIFAHNQIFIGLSNIKKCNTFGGNVFLLEEFDRKKGEIIQRRYFSQMADQICYAVLCVFSLAAAGHKKEEHSK | 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 anterior/posterior axon guidance [GO:1905488]; positive regulation of defecation [GO:2000294]; positive regulation of intestinal lipid absorption [GO:1904731]; regulation of apoptotic process [GO:0042981]; regulation of Rab protein signal transduction [GO:0032483]; ventral cord development [GO:0007419] | 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 regulator of the cab-1 synaptic transmission pathway (PubMed:10970871). Probably by converting rab-3 to its GTP-bound active form, plays a role in the recruitment of endophilin unc-57 to synaptic vesicles (PubMed:21029864). Probably by activating rab-3 and thus regulating the trafficking of dense-core vesicles, plays a role in AVG neuron-mediated formation of the right axon tract of the ventral nerve cord (PubMed:27116976). Regulates anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP) (PubMed:18852466). Probably by regulating DMP, required for fatty acid uptake by intestinal cells (PubMed:25849533). {ECO:0000250|UniProtKB:Q8WXG6, ECO:0000269|PubMed:10970871, ECO:0000269|PubMed:18852466, ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:25849533, ECO:0000269|PubMed:27116976, ECO:0000269|PubMed:9136770}. | Caenorhabditis elegans |
O02649 | CH60A_DROME | MFRLPVSLARSSISRQLAMRGYAKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIELKDKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKEGFEKISKGANPVEIRRGVMLAVETVKDNLKTMSRPVSTPEEIAQVATISANGDQAIGNLISEAMKKVGRDGVITVKDGKTLTDELEVIEGMKFDRGYISPYFINSSKGAKVEFQDALLLLSEKKISSVQSIIPALELANAQRKPLVIIAEDIDGEALSTLVVNRLKIGLQVAAVKAPGFGDNRKSTLTDMAIASGGIVFGDDADLVKLEDVKVSDLGQVGEVVITKDDTLLLKGKGKKDDVLRRANQIKDQIEDTTSEYEKEKLQERLARLASGVALLRVGGSSEVEVNEKKDRVHDALNATRAAVEEGIVPGGGTALLRCIEKLEGVETTNEDQKLGVEIVRRALRMPCMTIAKNAGVDGAMVVAKVENQAGDYGYDALKGEYGNLIEKGIIDPTKVVRTAITDASGVASLLTTAEAVVTEIPKEDGAPAMPGMGGMGGMGGMGGMGGMM | 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 regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of type II interferon production [GO:0032729]; protein folding [GO:0006457]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026] | 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 | MSATSATNFAVQTHPVKAPDEEYFFEGAEKLLELWFCSSTQNETRSLRIIPREEIDAMLDIARCKILHSKHNESIDSYVLSESSLFISDNRVILKTCGTTRLLAALPVIMQLAGAYAGLDQVQSVYYSRKNFLRPDLQPSLHKNFDAEVEYLDSFFVDGHAYCLGSLKQDRWYLYTFHREVEFPAHKQPDHTLEILMSDLDEEVLHKFTKDYAVDGNDCFMRAGIDKIIPAGADVHDELFDPCGYSMNAYMNDTDQYATIHVTPEKAFSFASFETNQDLVCLYSQTRKVLQCFRPNKILMTVFANDISEKGKDAQQQLWDRELPGYRRTNVQFVRLETETLVYAHFVRKASTGQDSSSSDEDDGERSD | 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 in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. {ECO:0000250|UniProtKB:P17707}. | 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=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|RuleBase:RU004273}; | 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 pseudopodium (PubMed:22042574). {ECO:0000269|PubMed:16943775, ECO:0000269|PubMed:22042574}. | Caenorhabditis elegans |
O02662 | ADRB3_CANLF | MAPWPHGNGSVASWPAAPTPTPDAANTSGLPGAPWAVALAGALLALEVLATVGGNLLVIVAIARTPRLQTMTNVFVTSLATADLVVGLLVVPPGATLALTGRWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSKWWRVGADAEAQRCHSNPHCCAFASNIPYALLSSSVSFYLPLLVMLFVYARVFLVATRQLRLLRRELGRFPPAESPPAASRSRSPGPARRCASPAAVPSDRLRPARLLPLREHRALRTLGLIVGTFTLCWLPFFVANVMRALGGPSLVPSPALLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCRREEHRAAASPPGDPSAAPAALTSPAESSRCQALDGASWGIS | 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 cyclic nucleotide second messenger [GO:0007187]; norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0002025]; positive regulation of MAPK cascade [GO:0043410] | 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 | MTCPKFSVALLHWEFIYVITAFDLAYPITPWKFKLSCMPPNTTYDFLLPAGISKNTSTLNGHDEAVVETELNSSGTYLSNLSSKTTFHCCFWSEEDKNCSVHADNIAGKAFVSAVNSLVFQQTGANWNIQCWMKEDLKLFICYMESLFKNPFKNYDLKVHLLYVLLEVLEGSPLLPQKGSFQSVQCNCSARECCECHVPVSAAKLNYTLLMYLKITSGGAVFHSPLMSVQPINVVKPDPPLGLHMEITDTGNLKISWSSPTLVPFQLQYQVKYSENSTTNMREADEIVSDTSLLVDSVLPGSSYEVQVRGKRLDGPGIWSDWSTPFTFTTQDVIYFPPKILTSVGSNISFHCIYKNENKIVSSKKIVWWMNLAEKIPQSQYDVVGDHVSKVTFPNMNATKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTNAIQSLVGSTLQLRYHRSSLYCSDVPSVHPISEPKDCQLQRDGFYECIFQPIFLLSGYTMWIRINHPLGSLDSPPTCVIPDSVVKPLPPSSVKAEITAKIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKIYEVYDTKLKSTSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSTPAYTVVTDVKVPIRGPEFWRIINEDATKKERNITLLWKPLMKNDSLCSVRSYVVKHHTSRHGTWSEDVGNHTKLTFLWTEQAHSVTVLAVNSIGASSANFNLTFSWPMSKVNIVQSLSAYPLNSSCVGLSWLLSPSDYNLMYFILEWKILNEDHEIKWLRIPSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDGEKHRNDAGLYVIVPIIISSSILLLGTLLMSHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTESVTFGPLLLEPETISEDISVDTSWKNKDEMVPPTTVSLLLTTPDLEKSSICISDQRSSAHFSEAESMEITREDENRRQPSIKYATLLSSPKSGETEQEQELVSSLVSRCFSSSNSLPKESFSNSSWEIETQAFFILSDQHPNMTSPHLSFSEGLDELMKFEGNFPKEHNDERSVYYLGVTSIKKRESDVFLTDESRVRCPFPAHCLFADIKILQESCSHLVENNFNLGTSGQKTFVSYMPQFQTCSTQTQKIMENKMYDLTV | 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 remodeling [GO:0046850]; regulation of feeding behavior [GO:0060259]; response to leptin [GO:0044321]; sexual reproduction [GO:0019953]; T cell differentiation [GO:0030217] | 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/activation. Phosphorylation of Tyr-1079 has a more accessory role. {ECO:0000250|UniProtKB:P48356}. | 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 and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (By similarity). Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T-cells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity). {ECO:0000250|UniProtKB:P48356, ECO:0000250|UniProtKB:P48357}. | 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 catabolic process [GO:0006550]; mitochondrial tRNA 3'-end processing [GO:1990180]; mitochondrial tRNA 5'-end processing [GO:0097745]; mitochondrial tRNA methylation [GO:0070901]; protein homotetramerization [GO:0051289]; steroid catabolic process [GO:0006706] | 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:0106281]; cholate 7-alpha-dehydrogenase activity [GO:0008709]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106282]; testosterone dehydrogenase (NAD+) activity [GO:0047035]; testosterone dehydrogenase [NAD(P)] activity [GO:0030283]; tRNA binding [GO:0000049]; ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106283] | 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:22433; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3-oxobutanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:13281, ChEBI:CHEBI:15378, ChEBI:CHEBI:57312, ChEBI:CHEBI:57335, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.178; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13282; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.159; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31197; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378, ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31161; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78594; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cortisone + NAD(+) = 17alpha-hydroxypregn-4-en-3,11,20-trione-21-al + H(+) + NADH; Xref=Rhea:RHEA:42016, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78596; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=11-dehydrocorticosterone + NAD(+) = H(+) + NADH + pregn-4-ene-3,11,20,21-tetraone; Xref=Rhea:RHEA:42020, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600, ChEBI:CHEBI:78601; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-ene-3,20,21-trione + H(+) + NADH; Xref=Rhea:RHEA:42012, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78595; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=NAD(+) + ursodeoxycholate = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42028, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=3beta,7beta-dihydroxy-5beta-cholan-24-oate + NAD(+) = 3beta-hydroxy-7-oxo-5beta-cholan-24-oate + H(+) + NADH; Xref=Rhea:RHEA:42024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78602, ChEBI:CHEBI:78603; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025; Evidence={ECO:0000250|UniProtKB:Q99714}; | 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:Q99714}. | 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 reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA. Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway. Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel. Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Essential for structural and functional integrity of mitochondria. {ECO:0000250|UniProtKB:Q99714}.; FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. {ECO:0000250|UniProtKB:Q99714}. | Bos taurus (Bovine) |
O02695 | PTPR2_MACNE | MALPLLLLLLLLLPPRVLPAAPSSVPHGRQLPGRLGCLLEEGLCGASEACVNDGVFGRCQKVPAMDFYRYEVSPVALQRLRVALQKLSGTGFTWQDDYTQYVMDQELADLPKTYLRHPEASGPARPSKHSIGSERRYSQEGGAALAKAFRRHLPFLEALSQAPASDALARTRMAQDRPRAEGDDRFSKSILTYVAHTSVLTYPPGPQAQLPEDLLPRTLSQLQPDELSPKVDSSVERHHLMAALSAYAAQRPPAPPGKGSLEPQYLLRAPSRMPRPLLSPAVPQKWPSPLGDPEDPPSTGEGARIHTLLKDLQRQPAEARGLSDLELDSMAELMAGLMQGMDHRGALGGPGKAALGESGEQADGPKAALRGESFPDDGVQDDDDRLYQEVHRLSATLGGLLQDHGSRLSPGALPFAKPLKMERKKSERPEASLSSEEETAGVENVKSQTYSKDLLGQQPHSEPGAGAFGELQNQMPGPSEEEQSLPAGAQEALGDGLQLEVKPSEEEARGYIVTDRDPLRPEEGRQLVEDVARLLQMPSSTFADVEVLGPAVTFKVGANVQNVTTADVEKATVDNKDKLEETSGLKILQTGVGSKSKLKFLPPQAEQEDSTKFIALTLVSLACILGVLLASGLIYCLRHSSQHRLKEKLSGLGRDPGADATAAYQELCRQRMATRPPDRPEGPHTSRISSVSSQFSDGPMPSPSARSSASSWSEEPVQSNMDISTGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQKEENVPKNRSLAVLTYDHSRVLLKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLTENGVRQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWYDRGVPSSSRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALPQ | 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|UniProtKB:P80560}. Note=Predominantly found on dense-core secretory granules. Sorting to secretory granules in part is dependent of the N-terminal propeptide domain of the precursor and its interaction with CPE. Transiently found at the cell membrane, when secretory vesicles fuse with the cell membrane to release their cargo. Is then endocytosed and recycled to secretory vesicles involving clathrin-dependent AP2-mediated endocytosis. Recycled via STX6- but not TTTGN1/TGN38-containing compartments. {ECO:0000250|UniProtKB:P80560, ECO:0000250|UniProtKB:Q63475}. | 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 response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH). Required to maintain normal levels of renin expression and renin release. May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization. Has phosphatidylinositol phosphatase activity; the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate. Regulates PI(4,5)P2 level in the plasma membrane and localization of cofilin at the plasma membrane and thus is indirectly involved in regulation of actin dynamics related to cell migration and metastasis; upon hydrolyzation of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments. {ECO:0000250|UniProtKB:P80560, ECO:0000250|UniProtKB:Q63475, ECO:0000250|UniProtKB:Q92932}. | Macaca nemestrina (Pig-tailed macaque) |
O02696 | PI3R5_PIG | MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLAPLALLFYSTVLCTPHFPPDSDLLLKAARTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLSTRSHRSSTVTVLLLNPVEVQAEFLDVADKLSTPGPSPHSAYITLLLHAFQATFGAHCDLSGLHRRLQSKTLAELEAIFTETAEAQELASGIGDAAEARQWLRTKLQAVGEKAGFPGVLDTAKPGKLRTIPIPVARCYTYSWNQDSFDILQEILLKEQELLQPEILDDEEDEDEEDEEEDLDADGHCAERDSVLSTGSAASHASTLSLASSQASGPTLSRQLLTSFVSGLSDGVDSGYMEDIEESAYERPRRPGGHERRGHRRPGQKFNRIYKLFKSTSQMVLRRDSRSLEGSPDSGPPLRRAGSLCSPLDSPTLPPSRAQGSRSLPQPKLSPQLPGWLLAPASRHQRRRPFLSGDEDPKASTLRVVVFGSDRISGKVVRAYSNLRRLENNRPLLTRFFKLQFFYVPVKRSRGTGTPTSPAPRSQTPPLPTDAPRHPGPAELGAAPWEESTNDISHYLGMLDPWYERNVLGLMHLPPEVLCQSLKAEPRPLEGSPAQLPILADMLLYYCRFAARPVLLQVYQTELTFITGEKTTEIFIHSLELGHSAATRAIKASGPGSKRLGIDGDREAVPLTLQIIYSKGAISGRSRWSNMEKLCTSVNLSKACRQQEELDSSTEALTLNLTEVVKRQTPKSKKGFNQISTSQIKVDKVQIIGSNSCPFAVCLDQDERKILQSVIRCEVSPCYKPEKSSLCPPPQRPSYPPAPATPDLCSLLCLPIMTFSGALP | 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 localized in the nucleus in absence of PIK3CG/p120 (PubMed:12507995, PubMed:15611065). Colocalizes with PIK3CG/p120 in the cytoplasm (PubMed:12507995, PubMed:15611065). Translocated to the plasma membrane in a beta-gamma G protein-dependent manner (PubMed:12507995, PubMed:15611065). {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}. | 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 | MELENYEQPVVLREDNRRRRRRMKPRSTAASLSSMELIPIEFVLPTSQRNTKTPETALLHVAGHGNVEQMKAQVWLRALETSVSADFYHRLGPDHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKVLHRSPGQIHVVQRHAPSEETLAFQRQLNALIGYDVTDVSNVHDDELEFTRRRLVTPRMAEVAGRDPKLYAMHPWVTSKPLPEYLLKKITNNCVFIVIHRSTTSQTIKVSADDTPGTILQSFFTKMAKKKSLMDIPESQNERDFVLRVCGRDEYLVGETPIKNFQWVRQCLKNGEEIHLVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRTADLTVFVEANIQYGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSGKTSAEMPSPESKGKAQLLYYVNLLLIDHRFLLRHGEYVLHMWQLSGKGEDQGSFNADKLTSRTNPDKENSMSISILLDNYCHPIALPKHRPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKDPKAYPKLFSSVKWGQQEIVAKTYQLLAKREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIDMLQKVTIDIKSLSAEKYDVSSQVISQLKQKLENLQNLNLPQSFRVPYDPGLKAGALVIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLSHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMISETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKSEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA | 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]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | 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=2.7.1.153; Evidence={ECO:0000250|UniProtKB:P48736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; Evidence={ECO:0000250|UniProtKB:P48736}; 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-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000250|UniProtKB:P48736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000250|UniProtKB:P48736}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000250|UniProtKB:P48736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000250|UniProtKB:P48736}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P48736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P48736}; | 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 involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Required for B-lymphocyte development and signaling. Together with other PI3Ks are involved in the oxidative burst produced by neutrophils in response to chemotactic agents. Together with PIK3CD regulate neutrophil extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contribute to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis (By similarity). {ECO:0000250|UniProtKB:P48736}. | 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 [GO:0001783]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial fusion [GO:0008053]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of protein binding [GO:0032091]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; regulation of apoptotic process [GO:0042981]; regulation of mitochondrial membrane potential [GO:0051881]; release of cytochrome c from mitochondria [GO:0001836]; release of matrix enzymes from mitochondria [GO:0032976]; response to toxic substance [GO:0009636] | 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 [GO:0005739]; nucleus [GO:0005634]; pore complex [GO:0046930] | 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 conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane (By similarity). {ECO:0000250|UniProtKB:Q07812}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000250}. | 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, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. {ECO:0000250|UniProtKB:Q07812}. | Bos taurus (Bovine) |
O02705 | HS90A_PIG | MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDSSAAVTEEMPPLEGDDDTSRMEEVD | 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 process [GO:0045429]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; response to antibiotic [GO:0046677]; response to cold [GO:0009409]; response to heat [GO:0009408] | 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 the membrane and secretory pathways. {ECO:0000250|UniProtKB:P07901}. | 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 cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response. {ECO:0000250|UniProtKB:P07900}. | Sus scrofa (Pig) |
O02713 | S22A2_PIG | MLTVDDILEHTGEFNFFQKQTFFLLALLSAAFTPIYVGIVFLGFIPDHRCRSPGVAELSQRCGWSLAEELNYTVPGPGPAGQAFPRQCRRYEVDWNQSTLGCVDPLAGLAANSSHLPLGPCRYGWVYDTPGSSIVTEFDLVCANSWLLDLFQSAVNVGFFIGSVGIGYIADRFGRKLCLLLTILINAVSGVLMAISPTYTWMLVFRLIQGLVSKAGWMIGYILITEFVGLSYRRTVGIFYQVAFTFGLLVLAGVAYALPHWRWLQFTVTLPNFCFLFYYWCVPESPRWLISQNKNAKAMSIIKHIAKKNGKSLPASLQSLRPDEEVGEKLKPSFLDLVRTPQIRKHTLILMYNWFTSAVLYQGLVMHMGLAGSNLYLDFFYSALVEFPAALLILLTIDRLGRRHPWAASNVVAGAACLASVFIPEDPHWLRITVLCLGRMGITMAYEMVCLVNAELYPTFIRNLGVLVCSSMCDIGGIITPFLVYRLTDIWHELPLVVFAVVGLIAGGLVLLLPETKGKTLPETIEEAETMRRPRKNKEKIIYLQVKKLDIPPN | 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:0015847]; serotonin transport [GO:0006837]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934] | 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]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; thiamine transmembrane transporter activity [GO:0015234]; xenobiotic transmembrane transporter activity [GO:0042910] | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: 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}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=creatinine(in) = creatinine(out); Xref=Rhea:RHEA:74539, ChEBI:CHEBI:16737; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:O15244}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72132; Evidence={ECO:0000250|UniProtKB:O15244}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72133; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:O70577}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=N-methyl-(R)-salsolinol(in) = N-methyl-(R)-salsolinol(out); Xref=Rhea:RHEA:74795, ChEBI:CHEBI:194083; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15244}; | 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.e. membrane potential and concentration gradient (By similarity). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow. Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters. Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system. Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium. Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN). Mediates the uptake and efflux of quaternary ammonium compound choline. Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine. Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:O15244, ECO:0000250|UniProtKB:Q9R0W2}. | 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 regulation of intrinsic apoptotic signaling pathway [GO:2001243]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane potential [GO:0051881]; release of cytochrome c from mitochondria [GO:0001836] | 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 phosphorylated by other protein kinases such as ERKs and stress-activated kinases. Phosphorylated by MAPK8/JNK1 at Thr-62, Ser-63 and Ser-77, which stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250|UniProtKB:P10415, ECO:0000250|UniProtKB:P10417}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity (By similarity). {ECO:0000250|UniProtKB:P10415}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P10415}. | 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:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}. | 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 release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}. | 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 process [GO:0006629]; negative regulation of appetite [GO:0032099]; negative regulation of appetite by leptin-mediated signaling pathway [GO:0038108]; negative regulation of autophagy [GO:0010507]; negative regulation of glucose import [GO:0046325]; phagocytosis [GO:0006909]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of TOR signaling [GO:0032008]; positive regulation of tumor necrosis factor production [GO:0032760]; prostaglandin secretion [GO:0032310]; regulation of angiogenesis [GO:0045765]; regulation of bone remodeling [GO:0046850]; regulation of brown fat cell differentiation [GO:0090335]; regulation of cell cycle [GO:0051726]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of endothelial cell proliferation [GO:0001936]; regulation of natural killer cell activation [GO:0032814]; regulation of natural killer cell mediated cytotoxicity [GO:0042269]; regulation of natural killer cell proliferation [GO:0032817]; regulation of nitric-oxide synthase activity [GO:0050999]; response to insulin [GO:0032868]; sexual reproduction [GO:0019953]; T cell differentiation [GO:0030217] | 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-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (By similarity). {ECO:0000250|UniProtKB:P41159, ECO:0000250|UniProtKB:P41160, ECO:0000250|UniProtKB:P50596}. | Canis lupus familiaris (Dog) (Canis familiaris) |
O02740 | GUC2F_BOVIN | MFLAPWPFSHLMLWFVTLGRQRGQHGLASFKLLWCLWLLVLMSLPLQVWAPPYKIGVVGPWTCDPLFSKALPEIAAQLATERINKDPALDLGHSLEYVIFNEDCQASRALSSFISHHQMASGFIGPANPGYCEAASLLGNSWDKGIFSWACVNYELDSKNSHPTFSRTLPSPIRVLLTVMKYFQWAHAGVISSDEDIWVHTAYRVASALRSRGLPVGVVLTTGQDSQSIQKALQQIRQADRIRIIIMCMHSTLIGGETQTHLLEWAHDLQMTDGTYVFVPYDTLLYSLPYKHTPYKVLRNNPKLREAYDAVLTITVESQEKTFYQAFEEAAARGEIPEKLESDQVSPLFGTIYNSIYFIAQAMNNAMKENGWASAASLVQHSRNVQFYGFNQLIRTDANGNGISEYVILDTNWKEWELHSTYTVDMETELLRFGETPIHFPGGRPPRADAQCWFADGRICQGGINPTFALMVCLALLIALLSINGFAYFIRHRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSHASVSFQITSEVQSGRSPRLSFSSGSLTPATCENSNIAIYEGDWVWLKKFPSGNFGDIKSVESSASDIFEMMKDLRHENINPLVGFFYDSGVFAIVTEFCSRRSLEDILMNQDVKLDWMFKSSLLLDLIKGMKYLHHREFAHGRLKSRNCVVDGRFVLKVTDYGFNDILETLRLSQEEPSAEELLWTAPELLRAPRGSRLRSFAGDVYSFAIIMQEVMVRGTPFCMMDLPAKEIIERIKKPPPVYRPVVPPEHAPPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIQERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGMRHAAEIANMSLDILSSVGTFKMRHMPEVPVRIRIGLHSGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSHSTVTILRTLGEGYEVELRGRTELKGKGTEETFWLVGKKGFTKPLPVPPPVGKDGQVGHGLQSVEIAAFQRRKQKSSW | 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 photoreceptor outer segment membrane (By similarity). {ECO:0000250|UniProtKB:Q5SDA5, ECO:0000269|PubMed:9175772, ECO:0000269|PubMed:9571173}. | 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 type I interferon-mediated signaling pathway [GO:0060339]; negative regulation of viral genome replication [GO:0045071]; positive regulation of bone mineralization [GO:0030501]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of protein oligomerization [GO:0032461]; positive regulation of type II interferon production [GO:0032729]; protein localization to mitochondrion [GO:0070585]; regulation of type II interferon production [GO:0032649]; response to type I interferon [GO:0034340]; ubiquitin-dependent protein catabolic process [GO:0006511] | 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 diglycine (LRLRGG) motif. This motif is essential not only for its conjugation to substrates but also for its recognition by the relevant processing proteases. {ECO:0000250|UniProtKB:P05161}. | 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 the conjugation of ISG15 to a lysine residue in the target protein. Exhibits antiviral activity towards both DNA and RNA viruses. The secreted form of ISG15 can: induce natural killer cell proliferation, augment lymphokine-activated-killer (LAK) activity, induce dendritic cell maturation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity (By similarity). The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10; the interaction is mediated by ITGAL (By similarity). In response to IFN-tau secreted by the conceptus, may ligate to and regulate proteins involved in the release of prostaglandin F2-alpha (PGF), and thus prevent lysis of the corpus luteum and maintain the pregnancy (PubMed:9546718). {ECO:0000250|UniProtKB:P05161, ECO:0000250|UniProtKB:Q64339, ECO:0000269|PubMed:9546718}. | 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 process [GO:0006629]; negative regulation of appetite [GO:0032099]; negative regulation of appetite by leptin-mediated signaling pathway [GO:0038108]; negative regulation of autophagy [GO:0010507]; negative regulation of glucose import [GO:0046325]; phagocytosis [GO:0006909]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of TOR signaling [GO:0032008]; positive regulation of tumor necrosis factor production [GO:0032760]; prostaglandin secretion [GO:0032310]; regulation of angiogenesis [GO:0045765]; regulation of bone remodeling [GO:0046850]; regulation of brown fat cell differentiation [GO:0090335]; regulation of cell cycle [GO:0051726]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of endothelial cell proliferation [GO:0001936]; regulation of natural killer cell activation [GO:0032814]; regulation of natural killer cell mediated cytotoxicity [GO:0042269]; regulation of natural killer cell proliferation [GO:0032817]; regulation of nitric-oxide synthase activity [GO:0050999]; response to insulin [GO:0032868]; sexual reproduction [GO:0019953]; T cell differentiation [GO:0030217] | 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-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (By similarity). {ECO:0000250|UniProtKB:P41159, ECO:0000250|UniProtKB:P41160, ECO:0000250|UniProtKB:P50596}. | Pan troglodytes (Chimpanzee) |
O02755 | CEBPB_BOVIN | MQRLVVWDPVCLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPADRPGPRPPTGELGSIGEHERAIDFSPYLEPLGAPQAPAPTTASDTFEAAPSAPAPVPASSGQHHDFLSDLFSDDYGGKNCKKAAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKATPAAAACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTGENERLQKKVEQLSREVSTLRNLFKTLPEPLLASSGHC | 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]; ovarian follicle development [GO:0001541]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of interleukin-4 production [GO:0032753]; regulation of cell differentiation [GO:0045595]; regulation of DNA-templated transcription [GO:0006355]; regulation of odontoblast differentiation [GO:1901329]; regulation of osteoclast differentiation [GO:0045670]; regulation of transcription by RNA polymerase II [GO:0006357]; response to endoplasmic reticulum stress [GO:0034976] | 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:0000978] | 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 inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P28033}.; PTM: Phosphorylated at Thr-236 by MAPK and CDK2, serves to prime phosphorylation at Thr-227 and Ser-232 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-236 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-269 enhances transactivation activity. Phosphorylation at Ser-328 in response to calcium increases transactivation activity. Phosphorylated at Thr-236 by RPS6KA1. {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.; PTM: O-glycosylated, glycosylation at Ser-228 and Ser-229 prevents phosphorylation on Thr-236, Ser-232 and Thr-227 and DNA binding activity which delays the adipocyte differentiation program. {ECO:0000250|UniProtKB:P28033}.; PTM: Acetylated. Acetylation at Lys-43 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 129-133, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity. {ECO:0000250|UniProtKB:P28033}. | 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:0000250|UniProtKB:P28033}. | 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 functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing. During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation. Essential for female reproduction because of a critical role in ovarian follicle development. Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033}. | Bos taurus (Bovine) |
O02766 | CP8B1_RABIT | MVLWGLLGALLMVMVGWLCLPGLLRQRRPQEPPLDKGSIPWLGHAMTFRKNMLEFLKHMRSKHGDVFTVQLGGQYFTFVMDPVSFGPILKDGQRKLDFVEYAKGLVLKVFGYQSIEGDHRMIHLASTKHLMGHGLEELNKAMLDSLSLVMLGPEGRSPDASRWHEDGLFHFCYGVMFKAGYLSLFGHTSDKRQDLLQAEEIFIKFRRFDLLFPRFVYSLLGPREWREVGRLQQLFHELLSVKHNPEKDGMSNWIGHMLQYLSEQGVAPAMQDKFNFMMLWASQGNTGPASFWALIYLLKHPEAMRAVKEEATRVLGEPRLEAKQSFTVQLSALQHIPVLDSVMEETLRLGAAPTLYRVVQKDILLKMASGQECLLRQGDIVTLFPYLSVHMDPDIHPEPTTFKYDRFLNPNGSRKVDFYKAGQKIHHYTMPWGSGVSICPGRFFALSEMKLFVLLMVQYFDLELVDPNTPVPPIDPRRWGFGTMQPTHDVRIRYRLKPLE | 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:CHEBI:15379, ChEBI:CHEBI:17899, ChEBI:CHEBI:28477, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000269|PubMed:1400444, ECO:0000269|PubMed:8943286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46753; Evidence={ECO:0000305|PubMed:1400444, ECO:0000305|PubMed:8943286}; CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha-diol + O2 + reduced [NADPH--hemoprotein reductase] = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:15261, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16496, ChEBI:CHEBI:28047, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000269|PubMed:1400444, ECO:0000269|PubMed:8943286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15262; Evidence={ECO:0000305|PubMed:1400444, ECO:0000305|PubMed:8943286}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholate + O2 + reduced [NADPH--hemoprotein reductase] = cholate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65700, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29747, ChEBI:CHEBI:36234, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.139; Evidence={ECO:0000269|PubMed:1400444, ECO:0000269|PubMed:8943286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65701; Evidence={ECO:0000305|PubMed:1400444, ECO:0000305|PubMed:8943286}; | 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, ultimately regulating the intestinal absorption of dietary lipids (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (PubMed:1400444, PubMed:8943286). {ECO:0000250|UniProtKB:O88962, ECO:0000269|PubMed:1400444, ECO:0000269|PubMed:8943286}. | Oryctolagus cuniculus (Rabbit) |
O02768 | PGH2_RABIT | MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTHFKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQQYNYQQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPPAVQKVAKASIDQSRQMKYQSLNEYRKRFLLKPYESFEELTGEKEMAAELEALYGDIDAVELYPALLVERPRPDAIFGESMVEMGAPFSLKGLMGNPICSPNYWKPSTFGGEVGFKIVNTASIQSLICNNVKGCPFTSFNVPDPQLTKTVTINASASHSRLEDINPTVLLKGRSTEL | 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 regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902219]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of fever generation [GO:0031622]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin secretion [GO:0032310]; regulation of blood pressure [GO:0008217]; regulation of cell population proliferation [GO:0042127]; regulation of neuroinflammatory response [GO:0150077]; response to nematode [GO:0009624]; response to oxidative stress [GO:0006979] | 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]; protein homodimerization activity [GO:0042803] | 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 mediators (SPMs), especially 15-R-lipoxin A4, which results in an increase of phagocytic microglia. {ECO:0000250|UniProtKB:Q05769}. | 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}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}. | 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=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:133133; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, ChEBI:CHEBI:138100; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132083; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90818; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132087; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R-hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, ChEBI:CHEBI:90824; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13-hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90815; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90812; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90814; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90813; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90810; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2-glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, ChEBI:CHEBI:85166; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy-(5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P79208}; | 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 endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner,being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:P79208, ECO:0000250|UniProtKB:Q05769}. | Oryctolagus cuniculus (Rabbit) |
O02773 | MA1A1_PIG | MPVGGLLPLFSSPAGGGLGGGLGGGLGGGGGGGGRKGSGPSAFRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAADGRARPGEEGAPGDPAAALEDNLARIRENHERALMEAKETLQKLPEEIQRDILMEKEKVAQDQMSNRMGFRLPPVYLVPLIGAIDREPADAAVREKRAKIKEMMKHAWNNYKLYAWGKNELKPVSKGGHSSSLFGNIKGATIVDALDTLFIMKMKNEFEEAKAWVEEHLNFNVNAEVSVFEVNIRFIGGLISAYYLSGEEIFRKKAVELGVKLLPAFYTPSGIPWALLNIKSGIGRNWPWASGGSSILAEFGTLHLEFIHLSYLSGNPFFAEKVMNIRKVLNNLEKPQGLYPNYLNPNSGQWGQYHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAIKAIETHLIRKSRNGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADDAPDGLTQHYLQLGAEIARTCHESYSRTFVKLGPEAFRFDGGVEAIATRQNEKYYILRPEVVETYLYMWRLTHDPKYRKWAWEAVEALEKHCRVNGGYSGLRDVYVSAQTYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNTEAHPLPVLSRNIKKVEDNEK | 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 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[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 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; | 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 | MSAGPGCEPCTKRPRWDAAATSPPAASDARSFPGRQRRVLDSKDAPVQFRVPPSSSGCALGRAGQHRGSATSLVFKQKTITSWMDTKGIKTVESESLHSKENNNTREESMMSSVQKDNFYQHNMEKLENVSQLGFDKSPVEKGTQYLKQHQTAAMCKWQNEGPHSERLLESEPPAVTLVPEQFSNANVDQSSPKDDHSDTNSEESRDNQQFLTHVKLANAKQTMEDEQGREARSHQKCGKACHPAEACAGCQQEETDVVSESPLSDTGSEDVGTGLKNANRLNRQESSLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDSSSAQTANKPSRFQPREADTELRKRSSAKGGEIRLHFQFEGGESRAGMNDVNAKRPGSTSSLNVECRNSKQHGRKDSKITDHFMRVPKAEDKRKEQCEMKHQRTERKIPKYIPPHLSPDKKWLGTPIEEMRRMPRCGIRLPPLRPSANHTVTIRVDLLRIGEVPKPFPTHFKDLWDNKHVKMPCSEQNLYPVEDENGERAAGSRWELIQTALLNRLTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKLLTRLHVTYEGTIEGNGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDRSERDDWQRRTTEIVAIDALHFRRYLDQFVPEKIRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAVAERDVVYFTFGDSELMRDIYSMHTFLTERKLTVGEVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCTQTTNQPGQRTGA | 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 ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). {ECO:0000250|UniProtKB:Q86W56, ECO:0000269|PubMed:15658938}. | Bos taurus (Bovine) |
O02810 | PI4KB_BOVIN | MGDTIVEPAPLKPTSEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLGCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | 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:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}. | 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|PubMed:11526106, ECO:0000269|PubMed:9218477}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000305|PubMed:9218477}; | 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 Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8, ECO:0000269|PubMed:11526106, ECO:0000269|PubMed:9218477}. | Bos taurus (Bovine) |
O02812 | MK14_CANLF | MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGADLLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVVSFVPPPLDQEEMES | 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 regulation of myoblast fusion [GO:1901741]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of phosphorylation [GO:0042327]; regulation of transcription by RNA polymerase II [GO:0006357]; smooth muscle contraction [GO:0006939] | 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 also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16 (By similarity). PPM1D also mediates dephosphorylation and inactivation of MAPK14 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16539}.; PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By similarity). {ECO:0000250|UniProtKB:Q16539}.; PTM: Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity). {ECO:0000250|UniProtKB:Q16539}. | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q16539}; | 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 direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression (By similarity). Phosphorylates S100A9 at 'Thr-113' (By similarity). {ECO:0000250|UniProtKB:Q16539}. | Canis lupus familiaris (Dog) (Canis familiaris) |
O02824 | ADA1A_RABIT | MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVGPLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFFSSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV | 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 baroreceptor response to increased systemic arterial blood pressure [GO:0001985]; neuron-glial cell signaling [GO:0150099]; norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure [GO:0001994]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; pilomotor reflex [GO:0097195]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of heart rate by epinephrine-norepinephrine [GO:0001996]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of the force of heart contraction by epinephrine-norepinephrine [GO:0001997]; positive regulation of vasoconstriction [GO:0045907]; regulation of cardiac muscle contraction [GO:0055117] | 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 heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}. | 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 myocytes (By similarity). {ECO:0000250}. | Oryctolagus cuniculus (Rabbit) |
O02827 | MYLK_SHEEP | FRLVEKKTGKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMKQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDIKNRLNCTQCLQHPWLXXXTKNMEAKKLSKHRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYQEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGGEEEEEE | 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. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC promotes CTTN binding (By similarity). {ECO:0000250}. | 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 furrow during mitosis. {ECO:0000250|UniProtKB:Q15746}. | 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: Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900, Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.18; | 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. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells (By similarity). {ECO:0000250}. | Ovis aries (Sheep) |
O02828 | TAU_CAPHI | MAEPRQEFDVMEDHAQGDYTLQDHEGDMEPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKAKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPGTGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL | 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 protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3, MARK4), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylation at Ser-224 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10636}. | 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|UniProtKB:P10636}. Cell projection, dendrite {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. {ECO:0000250|UniProtKB:P10636}. | 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 is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. | Capra hircus (Goat) |
O02839 | MCP_PIG | MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASPPKDAESLDGGIIAAIVVGVLAAIAVIAGGVYFFHHKYNKKRSK | 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 mediated immunity [GO:0002456] | 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-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. {ECO:0000269|PubMed:9029106, ECO:0000269|PubMed:9199970}. | Sus scrofa (Pig) |
O02840 | CADH5_PIG | MQVLVMLLAAAGTYLGLLTAPTAASNPGRQDTPSTLPLHRRQKRDWIWNQMHIDEEKNGSLPHYVGKIKSSVNHKNTKYQLKGESAGKVFRVDENTGDVYAFERLDREKIPEYQLVALVVDKNTEKNLESPSSFTIKVHDINDNWPVFTQLVFNASVPEMSVIGTSVIQLTAVDADDPTVADHASVIYRLKEGEEHFRIRGPGLIETASKNLDRETVPMYKIVVETQDAQGLRGDSGTATVFITLQDVNDNFPVFTQTRYTFSVPEDIRVGSPLGSLFVKDPDEPQNRKTKYSIVQGEYRDTFTIEPDPTRNEGIIKPMKPLDYERIQQYSFTIEATDPTIDLRYLSGTSTKNIARVIINVTDVDEPPNFKQPFYHFQLRENEKKPWIGSVLAVDPDAAQRSIGYSIRRTSDKGQFFGINKHGNIYNVKELDREVYPWYNLTVEAKELDSRGTPTGKESIVQVHIEVLDENDNAPEFAKPYEAKVCEDAPQGKLVVQISAIDKDVTPRDVKFKFSLSTEDSNFTLTDNHDNTANITVKHGYFDRERAKVHHLPILISDNGRPSLTGTSTLHVTVCKCNERGEFTLCEEMGAQVGVSIQALVAIFLCILTIAVISLLVYLRRRLRKQARAHGKSVPEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRHGGAKPPRPALDARPSLYAQVQKPPRHAPGAHAPGEMAAMIEVKKDEADHDGGGPPYDTLHIFGYEGAESIAESLSSLGTDSSDSDIDYDFLNDWGPRFKMLAELYGSDPREELLY | 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 adhesion molecules [GO:0007156]; regulation of complement-dependent cytotoxicity [GO:1903659]; regulation of establishment of cell polarity [GO:2000114]; vasculature development [GO:0001944] | 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 endothelial cell-cell junctions. {ECO:0000250|UniProtKB:P33151}. | 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 biology through control of the cohesion and organization of the intercellular junctions (By similarity). It associates with alpha-catenin forming a link to the cytoskeleton (By similarity). Acts in concert with KRIT1 and PALS1 to establish and maintain correct endothelial cell polarity and vascular lumen (By similarity). These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B (By similarity). Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (By similarity). {ECO:0000250|UniProtKB:P33151, ECO:0000250|UniProtKB:P55284, ECO:0000250|UniProtKB:Q8AYD0}. | 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 reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}. | 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 oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222, ECO:0000269|PubMed:9510973}. | Bos taurus (Bovine) |
O03042 | RBL_ARATH | MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGDRESTLGFVDLLRDDYVEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAVEGNEIIREACKWSPELAAACEVWKEITFNFPTIDKLDGQE | 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 ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:29372894}; | 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 (Probable). Binds to abscisic acid (ABA) (PubMed:26197050). {ECO:0000269|PubMed:26197050, ECO:0000305|PubMed:29372894}. | Arabidopsis thaliana (Mouse-ear cress) |
O03986 | HS904_ARATH | MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIHIIPDKTNNTLTIIDSGIGMTKADLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVADKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEALGRGTKMILYLKEDQMEYIEERRLKDLVKKHSEFISYPISLWIEKTIEKEISDDEEEEEKKDEEGKVEEIDEEKEKEEKKKKKIKEVTHEWDLVNKQKPIWMRKPEEINKEEYAAFYKSLSNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTKKKPNNIKLYVRRVFIMDNCEDIIPDYLGFVKGIVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQNEIFYITGESKKAVENSPFLEKLKKKGYEVLYMVDAIDEYAIGQLKEFEGKKLVSATKEGLKLEETDDEKKKKEELKEKFEGLCKVIKDVLGDKVEKVIVSDRVVDSPCCLVTGEYGWTANMERIMKAQALKDSNTGGYMSSKKTMEINPENSIMDELRKRAEADKNDKSVKDLVLLLFETALLTSGFSLDEPNTFGSRIHRMLKLGLSIEEDDAVEADAEMPPLEDDADAEGSKMEEVD | 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 | MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPYFGSSSASTMTSAVNLPSFQGGGGVSGMNYWLPATAEENESKVGVLHAGLDCIWNY | 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. Controls leaf margin development and required for leaf serration. Involved in axillary meristem initiation and separation of the meristem from the main stem. Regulates the phyllotaxy throughout the plant development. Seems to act as an inhibitor of cell division. {ECO:0000269|PubMed:10079219, ECO:0000269|PubMed:10750709, ECO:0000269|PubMed:12163400, ECO:0000269|PubMed:12492830, ECO:0000269|PubMed:12610213, ECO:0000269|PubMed:15202996, ECO:0000269|PubMed:15294871, ECO:0000269|PubMed:15500463, ECO:0000269|PubMed:15723790, ECO:0000269|PubMed:16798887, ECO:0000269|PubMed:17098808, ECO:0000269|PubMed:17122068, ECO:0000269|PubMed:17251269, ECO:0000269|PubMed:17287247, ECO:0000269|PubMed:9212461}. | Arabidopsis thaliana (Mouse-ear cress) |
O04019 | PS6AB_ARATH | MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRADILDPALMRSGRLDRKIEFPHPTEEARGRILQIHSRKMNVNADVNFEELARSTDDFNGAQLKAVCVEAGMLALRRDATEVNHEDFNEGIIQVQAKKKASLNYYA | 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 | MECRSLDLTIISAEDLKDVQLIGKQDLYAVVSINGDARTKQKTKVDKDCGTKPKWKHQMKLTVDDAAARDNRLTLVFEIVADRPIAGDKPVGEVSVPVKELLDQNKGDEEKTVTYAVRLPNGKAKGSLKFSFKFGEKYTYGSSSGPHAPVPSAMDHKTMDQPVTAYPPGHGAPSAYPAPPAGPSSGYPPQGHDDKHDGVYGYPQQAGYPAGTGGYPPPGAYPQQGGYPGYPPQQQGGYPGYPPQGPYGYPQQGYPPQGPYGYPQQQAHGKPQKPKKHGKAGAGMGLGLGLGAGLLGGLLVGEAVSDIADMGDMGDMGDMGGFDF | 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 membrane protein {ECO:0000255}. Note=Binds to C-terminal sequence of alpha-TIP and moves from the ER to vacuoles. Movement is accompanied by membrane internalization, and SRC2 is present in crystalloid-like structures within protein storage vacuoles (PSVs) in mature seeds. {ECO:0000269|PubMed:16227454}. | 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 | MEPQILFLYLSLFILSLNFFFTNLKPRLVRLFQPSLESRVKTALLSRKEVAAFLDSPIVEDEEGEEREEEEEGGIVSNANFTFEFDPYMMSKAESVNKALEEAIPVGEPLKIHEAMRYAILAAGKRVRPILCLASCELVGGQENAAMPAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVYGEGVAILSGGALLSLAFEHMTTAEISSERMVWAVRELARSIGTRGLVAGQAMDISSEGLDLNEVGLEHLEFIHVHKTAVLLETAAVLGAIIGGGSDEEIESVRKFARCIGLLFQVVDDILDETKSSEELGKTAGKDQLAGKLTYPKLIGLEKSKEFVKRLTKDARQHLQGFSSEKVAPLVALTTFIANRNK | 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,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:9150607}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000305|PubMed:9150607}; | 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.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. | 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 profile is not changed. {ECO:0000269|PubMed:19482937}. | Arabidopsis thaliana (Mouse-ear cress) |
O04073 | CTPA_TETOB | MHSRTNCLQTSVRAPQPHFRPFTAVKTCRQRCSTTAAAAKRDQAQEQQPWIQVGLGLAAAATAVAVGLGAAALPAQAVTSEQLLFLEAWRAVDRAYVDKSFNGQSWFKLRETYLKKEPMDRRAQTYDAIRKLLAVLDDPFTRFLEPSRLAALRRGTAGSVTGVGLEITYDGGSGKDVVVLTPAPGGPAEKAGARAGDVIVTVDGTAVKGLSLYDVSDLLQGEADSQVEVVLHAPGAPSNTRTLQLTRQKVTINPVTFTTCSNVAAAALPPGAAKQQLGYVRLATFNSNTTAAAQQAFTELSKQGVAGLVLDIRNNGGGLFPAGVNVARMLVDRGDLVLIADSQGIRDIYSADGNSIDSATPLVVLVNRGTASASEVLAGALKDSKRGLIAGERTFGKGLIQTVVDLSDGSGVAVTVARYQTPAGVDINKIGVSPDVQLDPEVLPTDLEGVCRVLGSDAAPRLFG | 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-Asn-Tyr-Ala-Leu-Ala-Ala.; EC=3.4.21.102; Evidence={ECO:0000303|PubMed:9252339}; | 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 | MMAASASATTMLLKYPTTVCGIPNPSSNNNNDPSNNIVSIPQNTTNPTLKSRTPNKITTNAVAAPSFPSLTTTTPSSIQSLVHEFDPQIPPEDAHTPPSSWYTEPAFYSHELERIFYKGWQVAGISDQIKEPNQYFTGSLGNVEYLVSRDGEGKVHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGMDGSLAKASKAKPEQNLDPKELGLVPLKVAVWGPFVLISLDRSLEEGGDVGTEWLGTSAEDVKAHAFDPSLQFIHRSEFPMESNWKIFSDNYLDSSYHVPYAHKYYATELNFDTYDTQMIENVTIQRVEGSSNKPDGFDRVGIQAFYAFAYPNFAVERYGPWMTTMHIHPLGPRKCKLVVDYYIENSMLDDKDYIEKGIAINDNVQREDVVLCESVQRGLETPAYRSGRYVMPIEKGIHHFHCWLQQTLK | 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:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.7; | 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 | MAFSSSCSSVKAVNSRWTSPSPSPSSRFAVLPAFLHRRYATSVKLTAISAALKTVEQTTLTEDNRFSTVGSDSDEYNPTLPKPRILVTEKLGEAGVNLLREFGDVDCSYDLSPEDLKKKVAESDALIVRSGTKVTREVFEAAKGRLKVVGRAGVGIDNVDLQAATEHGCLVVNAPTANTVAAAEHGIALLASMARNVAQADASIKAGKWERSKYVGVSLVGKTLAVMGFGKVGTEVARRAKGLGMTVISHDPYAPADRARALGVDLVSFDQAISTADFVSLHMPLTPATKKVFNDETFSKMKKGVRLINVARGGVIDEDALVRALDAGIVAQAALDVFCEEPPSKDSRLIQHENVTVTPHLGASTKEAQEGVAIEIAEAVAGALKGELSATAVNAPMVAPEVLSELTPYIVLAEKLGRLAVQLASGGKGVQSIRVVYRSARDRDDLDTRLLRAMITKGIIEPISDSYVNLVNADFIAKQKGLRISEERMVVDSSPEYPVDSIQVQILNVESNFAGAVSDAGDISIEGKVKYGVPHLTCVGSFGVDVSLEGNLILCRQVDQPGMIGQVGNILGEQNVNVNFMSVGRTVLRKQAIMAIGVDEEPDNKTLERIGGVSAIEEFVFLKL | 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) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.271 mM for NAD(+) (at pH 7.2) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.189 mM for NAD(+) (at pH 8.1) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.01 mM for NAD(+) (at pH 9.0) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.35 mM for 3-phosphonooxypyruvate (at pH 7.1) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; KM=0.12 mM for NADH (at pH 7.1) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; Vmax=133 umol/min/mg enzyme (at pH 8.1) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; Vmax=108 umol/min/mg enzyme (at pH 7.2) {ECO:0000269|PubMed:24368794, ECO:0000269|PubMed:9867856}; | 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; Evidence={ECO:0000269|PubMed:9148938}; CATALYTIC ACTIVITY: Reaction=2',3'-cyclophospho-AMP + H2O = adenosine 2'-phosphate + H(+); Xref=Rhea:RHEA:37191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:60879, ChEBI:CHEBI:77740; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:9148938}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37192; Evidence={ECO:0000269|PubMed:9148938}; CATALYTIC ACTIVITY: Reaction=2',3'-cyclophospho-GMP + H2O = guanosine 2'-phosphate + H(+); Xref=Rhea:RHEA:37211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:60837, ChEBI:CHEBI:74604; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:9148938}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37212; Evidence={ECO:0000269|PubMed:9148938}; CATALYTIC ACTIVITY: Reaction=2',3'-cyclophospho-UMP + H2O = H(+) + uridine 2'-phosphate; Xref=Rhea:RHEA:37239, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:60873, ChEBI:CHEBI:77802; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:9148938}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37240; Evidence={ECO:0000269|PubMed:9148938}; CATALYTIC ACTIVITY: Reaction=2',3'-cyclophospho-CMP + H2O = cytidine 2'-phosphate + H(+); Xref=Rhea:RHEA:41956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:60877, ChEBI:CHEBI:77766; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:9148938}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41957; Evidence={ECO:0000269|PubMed:9148938}; | 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/mg enzyme toward A>p {ECO:0000269|PubMed:9148938}; Vmax=37 umol/min/mg enzyme toward G>p {ECO:0000269|PubMed:9148938}; Vmax=79 umol/min/mg enzyme toward C>p {ECO:0000269|PubMed:9148938}; Vmax=47 umol/min/mg enzyme toward U>p {ECO:0000269|PubMed:9148938}; Vmax=16 umol/min/mg enzyme towardr Appr>p {ECO:0000269|PubMed:9148938}; | 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 | MAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDAKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNPEFKDDPELYVFPKLKYVGVELWQVKSGSLFDNVLVSDDPEYAKKLAEETWGKHKDAEKAAFDEAEKKREEEESKDAPAESDAEEEAEDDDNEGDDSDNESKSEETKEAEETKEAEETDAAHDEL | 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 | MGLPQNKLSFFCFFFLVSVLTLAPLAFSEIFLEEHFEGGWKSRWVLSDWKRNEGKAGTFKHTAGKWPGDPDNKGIQTYNDAKHYAISAKIPEFSNKNRTLVVQYSVKIEQDIECGGAYIKLLSGYVNQKQFGGDTPYSLMFGPDICGTQTKKLHVIVSYQGQNYPIKKDLQCETDKLNHFYTFILRPDASYSVLVDNKEREFGSMYTDWDILPPRKIKVKNAKKPEDWDDREYIDDPNDVKPEGFDSIPREIPDRKAKEPEDWDEEENGLWEPPKIPNSAYKGPWKAKRIKNPNYKGKWKNPWIDNPEFEDDPDLYVLKSIKYAGIEVWQVKAGSIFDNILICDDPAYARSIVDDYFAQHRESEKELFAEAEKERKAREDEEARIAREEGERRRKERDHRYGDRRRRYKRPNPRDYMDDYHDEL | 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 (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. {ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087}. | 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 | MDAIKCSSSFLHHTKLNTLFSNHTFPKISAPNFKPLFRPISISAKDRRSNEAENIAVVEKPLKSDRFFISDGLPSPFGPTVRDDGVNFSVYSTNSVSATICLISLSDLRQNKVTEEIQLDPSRNRTGHVWHVFLRGDFKDMLYGYRFDGKFSPEEGHYYDSSNILLDPYAKAIISRDEFGVLGPDDNCWPQMACMVPTREEEFDWEGDMHLKLPQKDLVIYEMHVRGFTRHESSKIEFPGTYQGVAEKLDHLKELGINCIELMPCHEFNELEYYSYNTILGDHRVNFWGYSTIGFFSPMIRYASASSNNFAGRAINEFKILVKEAHKRGIEVIMDVVLNHTAEGNEKGPIFSFRGVDNSVYYMLAPKGEFYNYSGCGNTFNCNHPVVRQFILDCLRYWVTEMHVDGFRFDLGSIMSRSSSLWDAANVYGADVEGDLLTTGTPISCPPVIDMISNDPILRGVKLIAEAWDAGGLYQVGMFPHWGIWSEWNGKFRDVVRQFIKGTDGFSGAFAECLCGSPNLYQGGRKPWHSINFICAHDGFTLADLVTYNNKNNLANGEENNDGENHNYSWNCGEEGDFASISVKRLRKRQMRNFFVSLMVSQGVPMIYMGDEYGHTKGGNNNTYCHDNYMNYFRWDKKEEAHSDFFRFCRILIKFRDECESLGLNDFPTAKRLQWHGLAPEIPNWSETSRFVAFSLVDSVKKEIYVAFNTSHLATLVSLPNRPGYRWEPFVDTSKPSPYDCITPDLPERETAMKQYRHFLDANVYPMLSYSSIILLLSPIKDP | 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 gravitropic responses in shoots by facilitating starch granules (statoliths) formation in hypocotyls (PubMed:34367195). {ECO:0000269|PubMed:15743447, ECO:0000269|PubMed:18815382, ECO:0000269|PubMed:19074683, ECO:0000269|PubMed:34367195}. | Arabidopsis thaliana (Mouse-ear cress) |
O04197 | COI1_ARATH | MEDPDIKRCKLSCVATVDDVIEQVMTYITDPKDRDSASLVCRRWFKIDSETREHVTMALCYTATPDRLSRRFPNLRSLKLKGKPRAAMFNLIPENWGGYVTPWVTEISNNLRQLKSVHFRRMIVSDLDLDRLAKARADDLETLKLDKCSGFTTDGLLSIVTHCRKIKTLLMEESSFSEKDGKWLHELAQHNTSLEVLNFYMTEFAKISPKDLETIARNCRSLVSVKVGDFEILELVGFFKAAANLEEFCGGSLNEDIGMPEKYMNLVFPRKLCRLGLSYMGPNEMPILFPFAAQIRKLDLLYALLETEDHCTLIQKCPNLEVLETRNVIGDRGLEVLAQYCKQLKRLRIERGADEQGMEDEEGLVSQRGLIALAQGCQELEYMAVYVSDITNESLESIGTYLKNLCDFRLVLLDREERITDLPLDNGVRSLLIGCKKLRRFAFYLRQGGLTDLGLSYIGQYSPNVRWMLLGYVGESDEGLMEFSRGCPNLQKLEMRGCCFSERAIAAAVTKLPSLRYLWVQGYRASMTGQDLMQMARPYWNIELIPSRRVPEVNQQGEIREMEHPAHILAYYSLAGQRTDCPTTVRVLKEPI | 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]; negative regulation of defense response [GO:0031348]; protein ubiquitination [GO:0016567]; regulation of flower development [GO:0009909]; response to far red light [GO:0010218]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611]; root development [GO:0048364]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; shade avoidance [GO:0009641]; stamen development [GO:0048443]; stomatal movement [GO:0010118] | 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, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including the ribulose bisphosphate carboxylase small chain 1B RBCS-1B and the histone deacetylase HDA6). These SCF complexes play crucial roles in regulating response to jasmonate, and their interactions with the COP9 signalosome (CSN) appear to be important for their activity. Interacts with TIFY10A and inositol pentakisphosphate to form a high-affinity jasmonates coreceptor. Involved in the regulation of plant gene expression during plant-pathogen interactions with Pseudomonas syringae and Alternaria brassicicola. {ECO:0000269|PubMed:10810145, ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12172836, ECO:0000269|PubMed:12244256, ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12724535, ECO:0000269|PubMed:12805591, ECO:0000269|PubMed:14756769, ECO:0000269|PubMed:9582125}. | Arabidopsis thaliana (Mouse-ear cress) |
O04200 | PXN_ARATH | MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKGAKLLLSNATSS | 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|PubMed:21895810, ECO:0000269|PubMed:22555559}; Vmax=416 umol/min/g enzyme for the AMP/AMP exchange {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22555559}; | 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, but has no activity with ATP, GTP, GDP, NADPH, NADP(+) or FAD. Required for peroxisomes proliferation. {ECO:0000269|PubMed:21895810, ECO:0000269|PubMed:22034551, ECO:0000269|PubMed:22555559}. | 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 initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Involved in cell growth and differentiation, especially during embryogenesis and male gametophyte germination (PubMed:20444226). Regulates sensitivity to sugars (e.g. sucrose) (PubMed:20444226). {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:20444226}. | 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=Cytoplasmic face of coated pits and vesicles (By similarity). Localized in the forming cell plate and the cortical division zone (CDZ) during cytokinesis. {ECO:0000250}. | 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:0010017]; red, far-red light phototransduction [GO:0009585]; regulation of circadian rhythm [GO:0042752]; regulation of flower development [GO:0009909]; response to red light [GO:0010114]; rhythmic process [GO:0048511] | 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. Increases ELF3 nuclear distribution and localization in nuclear bodies. Required for responsiveness to continuous red, by regulating phytochrome B (phyB) signaling (including during seedling de-etiolation) and gene expression. Mediates both entrainment to an environmental cycle and circadian rhythm sustainability under constant conditions. Controls flowering time. Necessary for light-induced expression of both CCA1 and LHY. {ECO:0000269|PubMed:12214234, ECO:0000269|PubMed:14605220, ECO:0000269|PubMed:15659097, ECO:0000269|PubMed:15908595, ECO:0000269|PubMed:16212608, ECO:0000269|PubMed:17384164, ECO:0000269|PubMed:20357892, ECO:0000269|PubMed:21255161, ECO:0000269|PubMed:22327739}. | Arabidopsis thaliana (Mouse-ear cress) |
O04226 | P5CS1_ORYSJ | MASVDPSRSFVRDVKRVIIKVGTAVVSRQDGRLALGRVGALCEQVKELNSLGYEVILVTSGAVGVGRQRLRYRKLVNSSFADLQKPQMELDGKACAAVGQSGLMALYDMLFNQLDVSSSQLLVTDSDFENPKFREQLTETVESLLDLKVIPIFNENDAISTRKAPYEDSSGIFWDNDSLAGLLALELKADLLILLSDVDGLYSGPPSEPSSKIIHTYIKEKHQQEITFGDKSRVGRGGMTAKVKAAVLASNSGTPVVITSGFENRSILKVLHGEKIGTLFHKNANLWESSKDVSTREMAVAARDCSRHLQNLSSEERKKILLDVADALEANEDLIRSENEADVAAAQVAGYEKPLVARLTIKPGKIASLAKSIRTLANMEDPINQILKKTEVADDLVLEKTSCPLGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAIRSNTILHKVITDAIPRNVGEKLIGLVTTRDEIADLLKLDDVIDLVIPRGSNKLVSQIKASTKIPVLGHADGICHVYIDKSADMDMAKHIVMDAKIDYPAACNAMETLLVHKDLMKSPGLDDILVALKTEGVNIYGGPIAHKALGFPKAVSFHHEYSSMACTVEFVDDVQSAIDHIHRYGSAHTDCIVTTDDKVAETFLRRVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGRGQVVNGDKDVVYTHKSLPLQ | 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:RHEA:19541, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; | 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 | MMMVHSMSRDMMNRESPDKGLDSGKYVRYTPEQVEALERVYTECPKPSSLRRQQLIRECPILSNIEPKQIKVWFQNRRCREKQRKEAARLQTVNRKLNAMNKLLMEENDRLQKQVSNLVYENGHMKHQLHTASGTTTDNSCESVVVSGQQHQQQNPNPQHQQRDANNPAGLLSIAEEALAEFLSKATGTAVDWVQMIGMKPGPDSIGIVAISRNCSGIAARACGLVSLEPMKVAEILKDRPSWLRDCRSVDTLSVIPAGNGGTIELIYTQMYAPTTLAAARDFWTLRYSTCLEDGSYVVCERSLTSATGGPTGPPSSNFVRAEMKPSGFLIRPCDGGGSILHIVDHVDLDAWSVPEVMRPLYESSKILAQKMTVAALRHVRQIAQETSGEVQYGGGRQPAVLRTFSQRLCRGFNDAVNGFVDDGWSPMGSDGAEDVTVMINLSPGKFGGSQYGNSFLPSFGSGVLCAKASMLLQNVPPAVLVRFLREHRSEWADYGVDAYAAASLRASPFAVPCARAGGFPSNQVILPLAQTVEHEESLEVVRLEGHAYSPEDMGLARDMYLLQLCSGVDENVVGGCAQLVFAPIDESFADDAPLLPSGFRIIPLEQKSTPNGASANRTLDLASALEGSTRQAGEADPNGCNFRSVLTIAFQFTFDNHSRDSVASMARQYVRSIVGSIQRVALAIAPRPGSNISPISVPTSPEALTLVRWISRSYSLHTGADLFGSDSQTSGDTLLHQLWNHSDAILCCSLKTNASPVFTFANQTGLDMLETTLVALQDIMLDKTLDEPGRKALCSEFPKIMQQGYAHLPAGVCASSMGRMVSYEQATVWKVLEDDESNHCLAFMFVNWSFV | 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:0010072] | 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 | MMAHHSMDDRDSPDKGFDSGKYVRYTPEQVEALERVYAECPKPSSLRRQQLIRECPILCNIEPRQIKVWFQNRRCREKQRKESARLQTVNRKLSAMNKLLMEENDRLQKQVSNLVYENGFMKHRIHTASGTTTDNSCESVVVSGQQRQQQNPTHQHPQRDVNNPANLLSIAEETLAEFLCKATGTAVDWVQMIGMKPGPDSIGIVAVSRNCSGIAARACGLVSLEPMKVAEILKDRPSWFRDCRCVETLNVIPTGNGGTIELVNTQIYAPTTLAAARDFWTLRYSTSLEDGSYVVCERSLTSATGGPNGPLSSSFVRAKMLSSGFLIRPCDGGGSIIHIVDHVDLDVSSVPEVLRPLYESSKILAQKMTVAALRHVRQIAQETSGEVQYSGGRQPAVLRTFSQRLCRGFNDAVNGFVDDGWSPMSSDGGEDITIMINSSSAKFAGSQYGSSFLPSFGSGVLCAKASMLLQNVPPLVLIRFLREHRAEWADYGVDAYSAASLRATPYAVPCVRTGGFPSNQVILPLAQTLEHEEFLEVVRLGGHAYSPEDMGLSRDMYLLQLCSGVDENVVGGCAQLVFAPIDESFADDAPLLPSGFRVIPLDQKTNPNDHQSASRTRDLASSLDGSTKTDSETNSRLVLTIAFQFTFDNHSRDNVATMARQYVRNVVGSIQRVALAITPRPGSMQLPTSPEALTLVRWITRSYSIHTGADLFGADSQSCGGDTLLKQLWDHSDAILCCSLKTNASPVFTFANQAGLDMLETTLVALQDIMLDKTLDDSGRRALCSEFAKIMQQGYANLPAGICVSSMGRPVSYEQATVWKVVDDNESNHCLAFTLVSWSFV | 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 shoot apical meristem specification [GO:0010072] | 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 | MSLRPSAKTEVRRNRYKVAVDAEEGRRRREDNLVEIRKNKREENLQKKRFTSSMAFGSATGQTEQDLSSANQLKDNLPAMVAGIWSEDSNSQLEATNLLRKLLSIEQNPPINEVVQSGVVPRVVKFLSRDDFPKLQFEAAWALTNIASGTSENTNVIIESGAVPIFIQLLSSASEDVREQAVWALGNVAGDSPKCRDLVLSYGAMTPLLSQFNENTKLSMLRNATWTLSNFCRGKPPPAFEQTQPALPVLERLVQSMDEEVLTDACWALSYLSDNSNDKIQAVIEAGVVPRLIQLLGHSSPSVLIPALRTIGNIVTGDDLQTQMVLDQQALPCLLNLLKNNYKKSIKKEACWTISNITAGNADQIQAVIDAGIIQSLVWVLQSAEFEVKKEAAWGISNATSGGTHDQIKFMVSQGCIKPLCDLLTCPDLKVVTVCLEALENILVVGEAEKNLGHTGEDNLYAQMIDEAEGLEKIENLQSHDNNDIYDKAVKILETFWTEDNEEEGNDENHAPQSGFQFGSTNVPPGQFNFI | 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 the regulation of pathogen-induced salicylic acid accumulation (PubMed:15964279). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:15964279, ECO:0000269|PubMed:18836040}. | Arabidopsis thaliana (Mouse-ear cress) |
O04300 | RGP1_PEA | MASLPKPTPLLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGHEINALEQHIKNLLSPSTPFFFNTLYDPYREGTDFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPHERNTRFVDAVLTIPKGSLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGYGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEEIIPFFQAATLSKDCTSVQKCYIELSKQVKEKLGTIDPYFIKLADAMVTWVEAWDEINNNKSEETTSTKASEVAATK | 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|PubMed:9207152}. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
O04308 | MPPA2_ARATH | MYRTAASRAKALKGILNHNFRASRYASSSAVATSSSSSSWLSGGYSSSLPSMNIPLAGVSLPPPLSDHVEPSKLKTTTLPNGLTIATEMSPNPAASIGLYVDCGSIYETPQFRGATHLLERMAFKSTLNRSHFRLVREIEAIGGNTSASASREQMGYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKVKVEIGEFATNPMGFLLEAVHSAGYSGALANPLYAPESAITGLTGEVLENFVFENYTASRMVLAASGVDHEELLKVVEPLLSDLPNVPRPAEPKSQYVGGDFRQHTGGEATHFALAFEVPGWNNEKEAIIATVLQMLMGGGGSFSAGGPGKGMHSWLYLRLLNQHQQFQSCTAFTSVFNNTGLFGIYGCTSPEFASQGIELVASEMNAVADGKVNQKHLDRAKAATKSAILMNLESRMIAAEDIGRQILTYGERKPVDQFLKTVDQLTLKDIADFTSKVITKPLTMATFGDVLNVPSYDSVSKRFR | 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]; mitochondrion [GO:0005739]; plant-type vacuole [GO:0000325] | 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:P07257}. | 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 complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000250|UniProtKB:P07257}. | 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 | MAQKVEAQGGNGGNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRSFEADPFVINHPEEHLVSVEGRYNPEGLILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAPLTNVTPLNAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGYREKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENGDGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARGGAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQLTDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA | 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)methanimidothioate = phenylacetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:69308, ChEBI:CHEBI:16189, ChEBI:CHEBI:25979, ChEBI:CHEBI:26833, ChEBI:CHEBI:183061; Evidence={ECO:0000269|PubMed:18987211}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = but-3-enenitrile + sulfate + sulfur; Xref=Rhea:RHEA:69276, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833, ChEBI:CHEBI:183062, ChEBI:CHEBI:183063; Evidence={ECO:0000269|PubMed:18987211}; | 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 nitriles in the presence of myrosinase (PubMed:18987211). {ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:27990154}. | Arabidopsis thaliana (Mouse-ear cress) |
O04318 | JAL27_ARATH | MAQKLVAQGGETGDVWDDGVYDNVTKVYVGQGQYGIAFVKFEYANGSEVVVGDEHGEKTELGVEEFEIDSDDYIVYVEGYREKVSDMTSEMITFLSFKTSKGKTSQPIVKKPGVKFVLHGGKIVGFHGRSTDVLHSLGAYVSLPSTPKLLGNWIKVEQNGEGPGLRCSHGIAQVGNKIYSFGGELIPNQPIDKHLYVFDLETRTWSIAPATGDVPHLSCLGVRMVSVGSTLYTFGGRDFSRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVGAMDRIKTLDSYNIVDKTWFHCSNPGDSFSIRGGAGLEVVQGKVWIVYGFNGCEVDDVHFYDPAEDKWTQVETFGVKPNERSVFASAAIGKHIVIFGGEIAMDPRAHVGPGQLIDGTFALDTETLQWERLDKFEGTPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSV | 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-N-(sulfonatooxy)methanimidothioate = phenylacetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:69308, ChEBI:CHEBI:16189, ChEBI:CHEBI:25979, ChEBI:CHEBI:26833, ChEBI:CHEBI:183061; Evidence={ECO:0000269|PubMed:19224919}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = but-3-enenitrile + sulfate + sulfur; Xref=Rhea:RHEA:69276, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833, ChEBI:CHEBI:183062, ChEBI:CHEBI:183063; Evidence={ECO:0000269|PubMed:19224919}; | 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 corresponding simple nitriles in the presence of myrosinase (PubMed:18987211). {ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:27990154}. | 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 salt stress [GO:0009651]; salicylic acid biosynthetic process [GO:0009697] | 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}. Nucleus {ECO:0000269|PubMed:17525078}. Cytoplasm {ECO:0000269|PubMed:17525078}. | 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. Functions in nitric oxide (NO)-mediated responses and in hydrogen peroxide-induced NO accumulation. {ECO:0000250, ECO:0000269|PubMed:17525078, ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:20068191}. | 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 | MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNATVDFIEEEKPFFPPTVNDKALHQFFKNVSGDMLGIENYVEMQPLMGSEDFSFYQQAIPGHFSFVGMQNKARSPMASPHSPYFEVNEELLPYGASLHASMATRYLLELKASTLNKSNKKDEL | 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:10072397, PubMed:11923288). Important for IAA-Leu hydrolysis in roots (PubMed:15155875). Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid (PubMed:24052260). {ECO:0000269|PubMed:10072397, ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:15155875, ECO:0000269|PubMed:24052260}. | 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 | MVRKRRTDAPSEGGEGSGSREAGPVSGGGRGSQRGGFQQGGGQHQGGRGYTPQPQQGGRGGRGYGQPPQQQQQYGGPQEYQGRGRGGPPHQGGRGGYGGGRGGGPSSGPPQRQSVPELHQATSPTYQAVSSQPTLSEVSPTQVPEPTVLAQQFEQLSVEQGAPSQAIQPIPSSSKAFKFPMRPGKGQSGKRCIVKANHFFAELPDKDLHHYDVTITPEVTSRGVNRAVMKQLVDNYRDSHLGSRLPAYDGRKSLYTAGPLPFNSKEFRINLLDEEVGAGGQRREREFKVVIKLVARADLHHLGMFLEGKQSDAPQEALQVLDIVLRELPTSRYIPVGRSFYSPDIGKKQSLGDGLESWRGFYQSIRPTQMGLSLNIDMSSTAFIEANPVIQFVCDLLNRDISSRPLSDADRVKIKKALRGVKVEVTHRGNMRRKYRISGLTAVATRELTFPVDERNTQKSVVEYFHETYGFRIQHTQLPCLQVGNSNRPNYLPMEVCKIVEGQRYSKRLNERQITALLKVTCQRPIDREKDILQTVQLNDYAKDNYAQEFGIKISTSLASVEARILPPPWLKYHESGREGTCLPQVGQWNMMNKKMINGGTVNNWICINFSRQVQDNLARTFCQELAQMCYVSGMAFNPEPVLPPVSARPEQVEKVLKTRYHDATSKLSQGKEIDLLIVILPDNNGSLYGDLKRICETELGIVSQCCLTKHVFKMSKQYMANVALKINVKVGGRNTVLVDALSRRIPLVSDRPTIIFGADVTHPHPGEDSSPSIAAVVASQDWPEITKYAGLVCAQAHRQELIQDLFKEWKDPQKGVVTGGMIKELLIAFRRSTGHKPLRIIFYRDGVSEGQFYQVLLYELDAIRKACASLEAGYQPPVTFVVVQKRHHTRLFAQNHNDRHSVDRSGNILPGTVVDSKICHPTEFDFYLCSHAGIQGTSRPAHYHVLWDENNFTADGLQSLTNNLCYTYARCTRSVSIVPPAYYAHLAAFRARFYMEPETSDSGSMASGSMARGGGMAGRSTRGPNVNAAVRPLPALKENVKRVMFYC | 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 [GO:0010589]; leaf vascular tissue pattern formation [GO:0010305]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; post-transcriptional gene silencing [GO:0016441]; regulation of translation [GO:0006417]; response to auxin [GO:0009733]; response to far red light [GO:0010218]; RNAi-mediated antiviral immune response [GO:0009616] | 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 mRNAs to repress gene expression. Requires DRB1 for directional loading of the small RNA duplex (guide stand and passenger strand) onto RISC for passenger strand degradation. Unlike animal RISC that associates in high molecular weight complex, Arabidopsis RISC is probably composed only of the AGO1 protein and associated RNA without any other proteins. Associates mainly with miRNAs of 21 nucleotide in length and preferentially recruits small RNAs with a 5' terminal uridine. Associates with 22 nucleotide miRNAs to trigger RDR6-dependent secondary siRNAs biogenesis. This pathway amplifies silencing by using the target RNA as substrate to generate secondary siRNAs. Binds to miR168 which targets its own mRNA for repression, establishing a homeostatic regulatory loop. Involved in antiviral RNA silencing by contributing to viral RNA clearance. Is capable of targeting viral RNAs with more compact structures than AGO7 which favors less structured RNA targets. May not associate with 24 nucleotide siRNAs involved in chromatin silencing. Essential for multiple processes in development. Essential for proper development of leaves and floral organs, and formation of axillary meristems. Like AGO10, required for stem cell function and organ polarity. {ECO:0000269|PubMed:15882589, ECO:0000269|PubMed:16081530, ECO:0000269|PubMed:17158744, ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18342362, ECO:0000269|PubMed:18344228, ECO:0000269|PubMed:18799732, ECO:0000269|PubMed:19763164, ECO:0000269|PubMed:19861421, ECO:0000269|PubMed:20562854, ECO:0000269|PubMed:9427751}. | Arabidopsis thaliana (Mouse-ear cress) |
O04385 | IEMT_CLABR | MGSTGNAEIQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVCKFLTKNEDGVSLAPFLLTATDKVLLEPWFYLKDAILEGGIPFNKAYGMNEFDYHGTDHRFNKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGAVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIFIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVVIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFLKTA | 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 (By similarity). Prevents general growth and development (PubMed:31001913). {ECO:0000250|UniProtKB:B3H7I1, ECO:0000269|PubMed:31001913}. | 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 ASYMMETRIC LEAVES 1 (AS1) to repress the knox homeobox genes KNAT1, KNAT2, and KNAT6 and the abaxial determinants ARF3, KAN2 and YAB5. May act in parallel with the RDR6-SGS3-AGO7 pathway, an endogenous RNA silencing pathway, to regulate the leaf morphogenesis (PubMed:11311158, PubMed:12787254, PubMed:12874130, PubMed:14508003, PubMed:16006579, PubMed:16699177, PubMed:17395603, PubMed:17559509). Required for the binding of AS1 to the KNOX genes (PubMed:23271976). Involved in leaf polarity establishment by functioning cooperatively with RH10 or RID2 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures (PubMed:27334696). {ECO:0000269|PubMed:11311158, ECO:0000269|PubMed:12787254, ECO:0000269|PubMed:12874130, ECO:0000269|PubMed:14508003, ECO:0000269|PubMed:16006579, ECO:0000269|PubMed:16699177, ECO:0000269|PubMed:17395603, ECO:0000269|PubMed:17559509, ECO:0000269|PubMed:23271976, ECO:0000269|PubMed:27334696}. | Arabidopsis thaliana (Mouse-ear cress) |
O04482 | UCH2_ARATH | MSWCTIESDPGVFTELIQQMQVKGVQVEELYSLDSDSLNNLRPVYGLIFLFKWQAGEKDERPTIQDQVSNLFFANQVINNACATQAILAILLNSPEVDIGPELSALKEFTKNFPSDLKGLAINNSDSIRAAHNSFARPEPFVPEEQKAATKDDDVYHFISYIPVDGVLYELDGLKEGPISLGPCPGDQTGIEWLQMVQPVIQERIERYSQSEIRFNLLAVIKNRKDIYTAELKELQRQREQLLQQANTCVDKSEAEAVNALIAEVGSGIEAASDKIVMEEEKFMKWRTENIRRKHNYIPFLFNFLKLLAEKKQLKPLIEKAKKQKTESST | 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 and 26S proteasome (PubMed:22951400). {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}. | Arabidopsis thaliana (Mouse-ear cress) |
O04492 | DRB1_ARATH | MTSTDVSSGVSNCYVFKSRLQEYAQKYKLPTPVYEIVKEGPSHKSLFQSTVILDGVRYNSLPGFFNRKAAEQSAAEVALRELAKSSELSQCVSQPVHETGLCKNLLQEYAQKMNYAIPLYQCQKVETLGRVTQFTCTVEIGGIKYTGAATRTKKDAEISAGRTALLAIQSDTKNNLANYNTQLTVLPCEKKTIQAAIPLKETVKTLKARKAQFKKKAQKGKRTVAKNPEDIIIPPQPTDHCQNDQSEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLEPSSCMNGLKEAAFGSVETEKIETTPNLEPPSCMNGLKEAAFGSVETEKIETTPNLESSSCMSGLKEAAFGSVETEASHA | 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 to cytokinin [GO:0009735]; ta-siRNA processing [GO:0010267] | 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 DCL1 to promote accurate processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate processing of precursor miRNAs (pre-miRNA). Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved with argonaute 1 (AGO1) in the guide strand selection from miRNA duplexes, presumably by directional loading of the miRNA duplex (guide stand and passenger strand) onto the RNA-induced silencing complex (RISC) for passenger strand degradation. Does not participate in sense transgene-induced post-transcriptional gene silencing (S-PTGS). Involved in several plant development aspects and response to hormones through its role in miRNAs processing. {ECO:0000269|PubMed:11148283, ECO:0000269|PubMed:14722360, ECO:0000269|PubMed:14972688, ECO:0000269|PubMed:15821876, ECO:0000269|PubMed:16428603, ECO:0000269|PubMed:16889646, ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:18632569, ECO:0000269|PubMed:19304749, ECO:0000269|PubMed:19861421, ECO:0000269|PubMed:20462493, ECO:0000269|PubMed:20735118}. | Arabidopsis thaliana (Mouse-ear cress) |
O04499 | PMG1_ARATH | MATSSAWKLDDHPKLPKGKTIAVIVLDGWGESAPDQYNCIHNAPTPAMDSLKHGAPDTWTLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIFAQGAKLCDQALASGKIFEGEGFKYVSESFETNTLHLVGLLSDGGVHSRLDQLQLLIKGSAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLVALRENGVDAQIASGGGRMYVTLDRYENDWEVVKRGWDAQVLGEAPHKFKNAVEAVKTLRKEPGANDQYLPPFVIVDESGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYEDFDKFDRVRYPKIRYAGMLQYDGELKLPSRYLVSPPEIDRTSGEYLTHNGVSTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIGEKARDAILSGKFDQVRVNIPNGDMVGHTGDIEATVVACEAADLAVKMIFDAIEQVKGIYVVTADHGNAEDMVKRDKSGKPALDKEGKLQILTSHTLKPVPIAIGGPGLAQGVRFRKDLETPGLANVAATVMNLHGFVAPSDYEPTLIEVVE | 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|PubMed:21813794}. | Arabidopsis thaliana (Mouse-ear cress) |
O04523 | TBL27_ARATH | MGLNEQQNVPSQRKIIVFIVLAFIPIALFRLCFNNPFSSIKDTSLQDSAANVVITSFSSSSQEEESQESFDHIQDEPLCDYTQGNWVRDEIGPLYNGSTCGTIKDGQNCFRHGRPDSGYLYWKWKPNECDIPRFDSNRFLDLMRDKHLAFIGDSMARNQLESLLCLLSTVSSPDLVYRNGEDNKFRRWRFESHNVTVSVYWSPFLVAGLEKSGNLDHNVLHIDRVDERWGNDLERFDTVVVSVGHWFLHPAVYYESGSVLGCHSCETSNCTEVGFYDVFRKAIRTTLRAVAGSGREVILTTFSPSHFEGRPWDSLGACNMTKPYEGKVLEGLDLDMRKIEIEEYTAAAAEVRLEVLDVTAMSVLRPDGHPGPYMYADPFKNGVPERIPNDCLHWCLPGPVDTWNEIMIEMLRRWKV | 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 specific O-acetylation in roots and rosette leaves (PubMed:22086088). {ECO:0000269|PubMed:22086088, ECO:0000269|PubMed:30083810}. | Arabidopsis thaliana (Mouse-ear cress) |
O04529 | 2MMP_ARATH | MRFCVFGFLSLFLIVSPASAWFFPNSTAVPPSLRNTTRVFWDAFSNFTGCHHGQNVDGLYRIKKYFQRFGYIPETFSGNFTDDFDDILKAAVELYQTNFNLNVTGELDALTIQHIVIPRCGNPDVVNGTSLMHGGRRKTFEVNFSRTHLHAVKRYTLFPGEPRWPRNRRDLTYAFDPKNPLTEEVKSVFSRAFGRWSDVTALNFTLSESFSTSDITIGFYTGDHGDGEPFDGVLGTLAHAFSPPSGKFHLDADENWVVSGDLDSFLSVTAAVDLESVAVHEIGHLLGLGHSSVEESIMYPTITTGKRKVDLTNDDVEGIQYLYGANPNFNGTTSPPSTTKHQRDTGGFSAAWRIDGSSRSTIVSLLLSTVGLVLWFLP | 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 cadmium ion [GO:0046686]; response to jasmonic acid [GO:0009753]; response to salt stress [GO:0009651] | 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 (PubMed:11726650). Active on McaPLGLDpaAR-NH(2) (QF24) and myelin basic protein (MBP) and, to some extent, on beta-casein (PubMed:24156403). {ECO:0000250|UniProtKB:O23507, ECO:0000269|PubMed:11726650, ECO:0000269|PubMed:24156403}. | 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). {ECO:0000269|PubMed:12123581, ECO:0000269|PubMed:9234949}. | Arabidopsis thaliana (Mouse-ear cress) |
O04705 | GAO1D_WHEAT | MVQPVFDAAVLSGRADIPSQFIWPEGESPTPDAAEELHVPLIDIGGMLSGDPAAAAEVTRLVGEACERHGFFQVVNHGIDAELLADAHRCVDNFFTMPLPEKQRALRHPGESCGYASSFTGRFASKLPWKETLSFRSCPSDPALVVDYIVATLGEDHRRLGEVYARYCSEMSRLSLEIMEVLGESLGVGRAHYRRFFEGNDSIMRLNYYPPCQRPLETLGTGPHCDPTSLTILHQDNVGGLQVHTEGRWRSIRPRADAFVVNIGDTFMALSNGRYKSCLHRAVVNSRVPRKSLAFFLCPEMDKVVAPPGTLVDAANPRAYPDFTWRSLLDFTQKHYRADMKTLEVFSSWIVQQQQPQPART | 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:0000269|PubMed:16160850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773; Evidence={ECO:0000269|PubMed:16160850}; CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + gibberellin A53 + H(+) + 3 O2 = 3 CO2 + gibberellin A20 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58526, ChEBI:CHEBI:143954; Evidence={ECO:0000269|PubMed:16160850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797; Evidence={ECO:0000269|PubMed:16160850}; | 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 {ECO:0000269|PubMed:16160850}; | 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 | MSAVLTAGGGLTAGDRSIITAINTGASSLSFVGSAFIVLCYCLFKELRKFSFKLVFYLALSDMLCSFFLIVGDPSKGFICYAQGYTTHFFCVASFLWTTTIAFTLHRTVVKHKTDVEDLEAMFHLYVWGTSLVVTVIRSFGNNHSHLGPWCWTQTGLKGKAVHFLTFYAPLWGAILYNGFTYFQVIRMLRNARRMAVGMSDRVDQFDNRAELKVLNRWGYYPLILIGSWAFGTINRIHDFIEPGHKIFWLSVLDVGTAALMGLFNSIAYGFNSSVRRAIHERLELFLPERLYRWLPSNFRPKNHLILHQQQQQRSEMVSLKTEDQQ | 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 signaling pathway [GO:0007166]; cytokinin-activated signaling pathway [GO:0009736]; flower development [GO:0009908]; gibberellic acid mediated signaling pathway [GO:0009740]; L-phenylalanine biosynthetic process [GO:0009094]; lipid metabolic process [GO:0006629]; maintenance of seed dormancy [GO:0010231]; mitotic cell cycle [GO:0000278]; negative regulation of abscisic acid-activated signaling pathway [GO:0009788]; positive regulation of gibberellic acid mediated signaling pathway [GO:0009939]; regulation of inositol trisphosphate biosynthetic process [GO:0032960]; response to cytokinin [GO:0009735]; response to low fluence blue light stimulus by blue low-fluence system [GO:0010244]; tyrosine biosynthetic process [GO:0006571] | 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. Together with GPA1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Probably involved in cytokinin signal transduction. Plays a positive role in gibberellin- (GA) and brassinosteroid- (BR) regulated seed germination, probably independently of a heterotrimeric G-protein. Mediates seed dormancy abolition, and promotes seed germination and flowering. {ECO:0000269|PubMed:11930019, ECO:0000269|PubMed:12972659, ECO:0000269|PubMed:15155892, ECO:0000269|PubMed:15181210, ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:17322342, ECO:0000269|PubMed:9512416}. | Arabidopsis thaliana (Mouse-ear cress) |
O04719 | P2C77_ARATH | MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGIRKFKSKSLN | 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|PubMed:20729862, ECO:0000269|PubMed:22116026}; | 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 to heat [GO:0009408]; response to osmotic stress [GO:0006970]; response to water deprivation [GO:0009414] | 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=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11882947}; | 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, modulates the inward calcium-channel permeability as well as H(2)O(2) and oxidative burst in response to ABA and dehydration. Represses GHR1 and, to some extent, SRK2E/OST1, kinases involved in the regulation of SLAC1-dependent stomatal closure (PubMed:22730405). Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response. {ECO:0000269|PubMed:10488243, ECO:0000269|PubMed:10872217, ECO:0000269|PubMed:10950871, ECO:0000269|PubMed:11208021, ECO:0000269|PubMed:11701885, ECO:0000269|PubMed:11707572, ECO:0000269|PubMed:12119381, ECO:0000269|PubMed:12194854, ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12447533, ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:14596925, ECO:0000269|PubMed:15599761, ECO:0000269|PubMed:15923322, ECO:0000269|PubMed:16339784, ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:18278579, ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:8787023, ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297, ECO:0000269|PubMed:9165752, ECO:0000269|PubMed:9276963}. | Arabidopsis thaliana (Mouse-ear cress) |
O04795 | PERA_IPOBA | MASFMKQLSLVLSFIALALAGCAVYQNTQTAMKDQLKVTPTWLDNTLKSTNLLSLGLGKPSGGKLGDEACVFSAVKEVVVAAINAEARMGASLIRLFFHDCFVDGCDAGLLLNDTATFTGEQTAAGNNNSVRGFAVIEQAKQNVKTQMPDMSVSCADILSIAARDSFEKFSGSTYTVTLGRKDARTANFTGANTQLVGPNENLTSQLTKFAAKGFNGTEMVALLGSHTIGFARCPLLCISTFINPARVSTLNCNCSGTVNATGLVGLDPTPTTWDQRYFSDVVNDQGLLFSDNELLKGNTTNAAVRRYRDAMGAFLTDFAAAMVKMSNLPPSPGVALEIRDVCSRVNANSVDPCEESRLLASPD | 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 contribute to protection against cold-induced oxidative stress. | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
O04796 | PERN_IPOBA | MASFVARLTLALSFIALALAGYSLVQNTLSSPTHTRLNLIPTWLDSTFDSADVLSYLGFGKSSGRLSDSNCVFSAVKEIVDAAITAETRMGASLIRLHFHDCFVDGCDGGILLNDTANFTGEQGAPANSNSVRGFSVIDQAKRNAQTKCADTPVSCADVLAIAARDAFRKFTNQTYNITLGRQDARTANLTGANTQLPAPFDNLSIQTAKFADKGFNQREMVVLAGAHTVGFSRCAVLCTSTNLNQNRSATLQCTCPASANDTGLVGLDPSPGTFDKKYFEELVKGQGLLFSDQELMQSNATVTAVRRYRDATGAFLTDFAAAMVKMSNLPPSAGVQLEIRNVCSRVN | 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 contribute to protection against cold-induced oxidative stress. | 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 via the endoplasmic reticulum (ER) and Golgi apparatus. {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}. | 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 | MSILKCLGVRGNQLCAARNYLKVLGFSSFHTAPNSSIEIQTQDEEVVIALGSNVGDRLHNFKEALKLMRKSGIHITRHASLYETAPAYVTDQPRFLNSAVRADTKLGPHELLAALKRIEKDMGRTDGIRYGPRPIDLDILFYGKFKVRSDILTVPHERIWERPFVMAPLMDLLGTAIDSDTVASWHSFSGHSGGLNALWEKLGGESLIGEEGMYRVMPVANGLLDWSRRTLVMGILNLTPDSFSDGGNFQSVKSAVSQARLMISEGADIIDIGAQSTRPMASRISAEEELGRLIPVLEAVMSIPEVEGKLISVDTFYSEVALEAVRKGAHIINDVSAGKLDASMFKVMAELDVPYVAMHMRGDPSTMQDSENLKYDNVCKDISSELYSRVREAEISGIPAWRIIMDPGIGFSKKTEDNLAALTGIPDIREEISKRSLAISHAPILIGPSRKRFLGEICSRPSAVDRDPATIASVTAGVLCGANIVRVHNVKDNLDAVKLCDAILKQKSSPIKFKQ | 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: Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949, ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019, ChEBI:CHEBI:72950; EC=2.5.1.15; Evidence={ECO:0000269|PubMed:9118956}; | 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|PubMed:9118956}; | 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-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. {ECO:0000305}. | 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:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:9576794}; CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:9576794}; | 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 | MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELDKRKITNAYTLAYQSRVGPVEWLKPYTEEAITELGKKGVENLLAVPISFVSEHIETLEEIDVEYKELALKSGIKNWGRVPALGTEPMFISDLADAVVESLPYVGAMAVSNLEARQSLVPLGSVEELLATYDSQRRELPAPVTMWEWGWTKSAETWNGRAAMLAVLALLVLEVTTGKGFLHQWGILPSL | 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 that FC2 is not present in Arabidopsis mitochondria in vivo. {ECO:0000305|PubMed:11602264}. | 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 chloroplasts during photo-oxidative stress through regulation of heme biosynthesis (PubMed:26494759). {ECO:0000269|PubMed:24329537, ECO:0000269|PubMed:26494759}. | 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 and cellular localization. {ECO:0000305|PubMed:28741704}.; PTM: Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation. {ECO:0000250|UniProtKB:P67774}.; PTM: Ubiquitinated. CHIP-mediated ubiquitination enhances phosphatase activity after an abiotic stress such as low temperature or darkness (By similarity). {ECO:0000250}. | 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-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: 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 responses. May function by increasing chloride channel activities on vacuolar membranes (PubMed:27676158). {ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:27676158}. | Arabidopsis thaliana (Mouse-ear cress) |
O04983 | ACCC_ARATH | MDASMITNSKSITSPPSLALGKSGGGGVIRSSLCNLMMPSKVNFPRQRTQTLKVSQKKLKRATSGGLGVTCSGGDKILVANRGEIAVRVIRTAHEMGIPCVAVYSTIDKDALHVKLADEAVCIGEAPSNQSYLVIPNVLSAAISRGCTMLHPGYGFLSENALFVEMCRDHGINFIGPNPDSIRVMGDKATARETMKNAGVPTVPGSDGLLQSTEEAVRVANEIGFPVMIKATAGGGGRGMRLAKEPGEFVKLLQQAKSEAAAAFGNDGCYLEKFVQNPRHIEFQVLADKFGNVVHFGERDCSIQRRNQKLLEEAPSPALTAELRKAMGDAAVAAAASIGYIGVGTVEFLLDERGSFYFMEMNTRIQVEHPVTEMIYSVDLIEEQIRVAMGEKLRYKQEDIVLRGHSIECRINAEDPFKGFRPGPGRITSYLPSGGPFVRMDSHVYSDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALNDTIITGVPTTINYHKLILDVEDFKNGKVDTAFIVKHEEELAEPQEIVAVKDLTNATV | 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:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000269|PubMed:9414551}; | 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:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986}; | 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 dissociation constant (By similarity). Promotes tolerance to low potassium K(+) conditions (By similarity). {ECO:0000250|UniProtKB:A2XE45, ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831}. | 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:0000269|PubMed:21495624}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000269|PubMed:21495624}; | 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 because of a very low dissociation constant (PubMed:9390447). {ECO:0000269|PubMed:21495624, ECO:0000269|PubMed:9390447, ECO:0000303|PubMed:17540516}. | Oryza sativa subsp. japonica (Rice) |
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