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stringlengths 6
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stringlengths 5
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stringlengths 3
2.44k
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E1BMF7
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UBP13_BOVIN
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Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13)
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MQRRGALFGMPGGSGSRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKMFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDTGYPLAVKLGTITPDGADVYSFQEEEAVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKPRVSEWEVIQETGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAESNRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSVDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMTQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIVVHMEEPDFAEPLTMPGYGGAASAGASVFGATGLDNQPPEETVAIITSMGFHRNQAIQALRATNSNLERALDWIFSHPEFEEDSDFVIEMENNANANIVSEAKPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS
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Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression or DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Alternatively, forms with NEDD4 a deubiquitination complex, which subsequently stabilizes VPS34 to promote autophagy. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Regulates the cell cycle progression by stabilizing cell cycle proteins such as SKP2 and AURKB. In addition, plays an important role in maintaining genomic stability and in DNA replication checkpoint activation via regulation of RAP80 and TOPBP1. Deubiquitinates the multifunctional protein HMGB1 and subsequently drives its nucleocytoplasmic localization and its secretion. Positively regulates type I and type II interferon signalings by deubiquitinating STAT1 but negatively regulates antiviral response by deubiquitinating STING1.
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E1BMP7
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DNA2_BOVIN
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DNA replication ATP-dependent helicase/nuclease DNA2 (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)]
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MERVDELELLMEKSFWQEAEPSAELFQKKKVEASFSKIVLSRGMDNRYLVLAVDIVQSEEGNHEKHLIITASQSLEYKELCILRNDWCSVPVEPGDIIHLEGDCISNTWIIDEDFGYLILYPDMLISGTSIASSIRCMRRAVLSETFRSSDPATRQMLIGTVLHEVFQKAVSDSFAPEKLQELASQTIQEIRHLKEMYRLKLNQDEIKQEVEEYLPSFSKWAGDFMHKHTSTDFPQMQLSLPSDGSNSNSTCNIEVTNSLDIEESIWSPRFGLKGKIDVTVGVKIHRGCKTKYKIMPLELKTGKESNSIEHRSQLVLYTLLSQERRADPEAGLLLYLKTGQMYPVPAKHLDKRELLRLRNQMAFSLFHRINKSTGEKTELAPLPQIIEEQQTCKYCSQMGNCALYSRAVEQQMEDSSVPTSMWPKIKEETQHLKPIHLEYFSLWCLMLTLESQSKDNKRNYQHIWLMPASEMEESGSCIGSLIRIEHVKTVCDGQYLHNFQRKNGAIPITNLMAGDRIILSGEERTLFALSRGYVKEINSTTVTCSLDRNLSGLPESTLFRLDQEEKNCDIDTPLGNLSKLMENTRASQKLRDLIIDFREPQFISYLSSVLPHEAKDTVACILKGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQKVHPDIQKFTEEEICRSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKTFDFCIVDEASQISQPVCLGPLFFSRRFVLVGDHQQLPPLVLNREARALGMSESLFKRLEQNKNAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLPNFKDVKLELEFYADYSENPWLIAAFEPNNPVCFLNTHKVPAPEQVEKGGVSNIMEAKLVVFLTSVFIKAGCKPSDIGIIAPYRQQLKVISDLLAQSSVGMVEVNTVDRYQGRDKSIVVVSFVRSNEDGTLGELLKDWRRLNVAITRAKHKLILLGCVPSLSRYPPLRKLLNHLNSEKLIIDLPSGEHESLFHLLGDFQRK
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Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function (By similarity).
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E1BPK6
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MYO6_BOVIN
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Unconventional myosin-VI (Unconventional myosin-6)
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MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLMGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLAVHRNIRDDEGFIVRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHDFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAQLVKRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKAEMNKQVKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIARSEAELIIDEAQADPAALRSLDFHPVTSKINGTRRTMTPEQMAKEMSEILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1 CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity).
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E1BPQ1
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FOXO1_BOVIN
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Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)
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MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDGAAGLPSASAAAVNADFMSNLSLLEESGDFQQAPGSVAAAAPLSQHPPVPPAAAAAAAGGQLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPTPNYQKYTYGQSSMSPLPQMPMQTLQDNKSSYGGMSQYCAPGLLKELLTSDSPPHNDIMTPVDPGVAQANSRVLGQSVLMGPNSVMPAYGGQASHNKMMTPSSHTHPGHAQSTSAVNGRALPHAVNTMPHTSGMNRLAPVKTALQVPLAHPMQMSALGGYSSVSSCNGYGRMGVLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG
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Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).
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E1BPW0
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ENTP5_BOVIN
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Ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase 5) (EC 3.6.1.6) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5)
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MALYQGAAFFMLVASCVCSTVFHREQQTWFEGVFLSSMCPVNVSAGTLYGIMFDAGSTGTRIHVYTFVQKVPDNTGQLPVLEGEIFDSVKPGLSAFVDQPKQGAETVQELLEVAKDSIPPSHWKRTPVVLKATAGLRLLPEEKAEALLFEVKEIFKKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHNQETVGTLDLGGASTQITFLPQFEKTLEQTPRDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETAGIDGYTFRSACLPRWLEAEWIFGGVKYQYGGNQEAGEVGFEPCYAEVLRVVQGKLHQPDEVQRGSFYAFSYYYDRAVDTDMIDYEKGGVLKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFASSTVLQLTKKVNNIETGWALGATFHLLQSLGISH
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Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity).
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E1BPX4
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MCM8_BOVIN
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DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8)
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MNGKYRGRGFGQGRFQSWKSGRGGRGFSGKWREREHRPDLNKATGKHPEQTPQSLLLQSTLDHFIPYKGWKLYFSEVYSDSIPFIEKIEAFESFFTERIELYDKDEIERKGSILVDFKELINDDEIIKLIPNIANELRDTPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLSRNGETVVNVPHIHARVYNYEPLTQLKNVRANYYGKYIALRGTVVRVSNTKPLCTKMAFLCAACGEIQSLSLPDGKYNLPTKCPVPACRGKSFTALRSSPLTVTMDWQSIKIQELMSDDQREAGRIPRTIECELVHDLVDSCVPGDTVTITGVVKVSNAEEANSVSNNKGQKTKASEDGCKHGALMEFSLKDLYAIQEIQSEENLFKLIVNSLCPVIFGHELVKAGLALALFGGSQKYADDKNRIPIRGDPHVLVVGDPGLGKSQMLQAVCSVAPRGVYVCGNTTTTSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGMVCSLPARTSIIAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEDHDHLLSEHVIAIRAGKQRAVSSATVARMNSQDSNTSILEVVSDKPLSERLKVVPGETIDPIPHQLLRKYIGYSRQYVYPRLSTEAAQILQNFYLELRKQSQRLSSSPITTRQLESLIRLTEARARLELREEATKEDAEDIVEIMKYSMLGTYSDEFGNLDFERSQHGSGMSNRSAAKRFISALNKIAERTYNNLFQFHQLQQIAKELNIQVADFENFIGSLNDQGYLLKKGPKVYQLQTM
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Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC). Probably by regulating HR, plays a key role during gametogenesis. Stabilizes MCM9 protein.
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E1BSI0
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PARP3_CHICK
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Protein mono-ADP-ribosyltransferase PARP3 (cPARP3) (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3)
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MAPKRRAPPASQPADGGKKAKGGQEEEEDAWSSALNALKTAPREKPPATIDGQCPLSAGPDAKVYEDYDCTLNQTNISANNNKFYIIQLIEHGGTYSTWNRWGRVGEVGQSKLLPFTSLEAAKKDFEKKFWEKTKNRWAARDNFVAQPGKYTLIEVQPGAGQEVALRVDGAGDEKVSKRRVLPCALDETTQKLVALIFSSDMFRHAMQAMNIDVKKMPLGKLSKQQIARGFEALEELEAALGEQPRSMSRLEELSSRFYTIVPHNFGRARPPPIDSPELLRAKKDMLLVLADIEVAQSLQAQKVEEEEVVAHPLDRDYALLCCQLTLLEDTSQEYEMILNYVAQTGGQVYVLNVWRVAREGEDKLFQAHDHLEHRRLLWHGTNVAVVAAILKNGLRIMPHSGGRVGKGIYFASENSKSACYVGCTSKRVGLMFLTEVALGKPYCITRDEPTLQQPPNGYDSVQACGRTEPDPAQDVEVTLDGKKVLVCQGKPIPMPAYKDSSFFQSEYLIYQESQCRIRYLVQLHF
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Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage. Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as histone H2B, XRCC5 and XRCC6 (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA. Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (By similarity). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (By similarity). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (By similarity).
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E1BSW7
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CENPS_CHICK
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Centromere protein S (CENP-S)
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MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA
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DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (By similarity).
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E1BTG2
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LMOD2_CHICK
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Leiomodin-2 (Cardiac leiomodin) (C-LMOD)
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MSTFGYRRELSKYEDIDEDELLASLTEEELKELERELEDIEPDRNLPVGQRQKSLTEKTPTGTFSREALMAYWERETRKLLEKERLGACEKDSEQEEDNSEDIQEECFTESNSEVSEEAYTEEDDEEEEEEEEEEEDEDDSDDEDEEKQNSAASERPVNCEDGRSSSHVRHKKCSNAKNSENLFNGHDGKDTENLSFKSSAIHPCGNPTVIEDALEKVRSNDPETTEVNLNNIENITSQMLIQFSQALRDNTVVKSFSLANTHADDNVAIAIAGMLKVNQHITSLNIESNFITGKGVLAIMRALQHNKVLTELRFHNQRHIMGSQVEMDIVKLLKENTTLVKLGYHFDLAGPRMSMTSILTRNMDKQRQKRMQEQRQQEYGCDGAINPKTKVLQKGTPRSSPYTSPKSSPWSSPKLPRKSAPAKSQPPAPAPPPPPPPPPPPPPPPPPVIPDKKAPTRNIAEVIKQQESSRKALQNGQKKKKGKKGKKHENSILKEIKDSLKSVSDRKSEEGSRPSTRPSTPQRSLHDNLMEAIRASSIKQLRRVEVPEALR
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Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length. Required for normal sarcomere organization in the heart, and for normal heart function (By similarity).
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E1BY77
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UBP13_CHICK
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Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13)
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MQRAALFGGGDAQMAAGDLGELLVPYMPTIRVPKSGDRVYKTECAFSYDSPDSEGGLYVCMNTFLGFGREHIERHYRKTGQCVYLHLKRHVIEKVPGASGGALPKRRNAKLFLDLEANGDLSSDDFEYEDEAKLVIFPDHYEISLPNIEELPALVTIASDALLSAKSPYRKQDPDSWEEELQASKHAKSLVQLDNGVRIPPSGWKCSKCDLRENLWLNLTDGSVLCGKWFFDGSGGNGHAMEHYKETGYPLAVKLGTITPDGADVYSFDEEEPVLDPHIAKHLAHFGIDMLQMQVAENGLRDNDIKPRVSEWEVIQEAGVKLKPMYGPGYTGMKNLGNSCYLNAVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMAKLGHGLLSGQYSKPPMKSELIEQVMKEEHKPQQNGISPQMFKAFISKDHTEFSSNRQQDAQEFFLHLINLVERNPVGSENPSDVFRFLVEERTQCCQSRKVRYTERVDYIMQLPVAMEAATNKDELIAYELKRREAEAARRAPPELVRAKIPFSACLQAFSEPTNVEDFWSSALQAKSAGVKTSRFASFPQYLVVQIKKFTFGLDWIPKKLDVSIDMPDFLDISHLRAMGLQPGEEELPDIAPPIIIPEDPKDRMMNNFVESLDIDESSVMQLAEMGFPLEACRKAVYYTGNLGAEVAFNWIIAHMEEPDFAEPLVVPVFGGAASSGVAGLGAVGLDNQPPEEMVSIIISMGFQRSLAIQALKATNNNLERALEWIFSHPELEEEDGEPALNVMDLENHTNANILAEARSEGPRIKDGPGRYELFGFISHMGTSTMSGHYVCHLKKEGRWVIYNDLRVCASERPPKDLGYIYFYHRIPS
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Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD).
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E1C1L6
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ENTP5_CHICK
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Ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase 5) (EC 3.6.1.6) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5)
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MTSSRLPVLLALVFSSLSPVLSHSNREMWFQDLFPPNTCPINAKTKTFYGIMFDAGSTGTRIHIYTFVQKSPEILPELEGEIFESVKPGLSAYADQPEKGAESVKRLLDMAIDAVPPHLWKKTPVVLKATAGLRLLSEEKAQALLSEVKEVFEESPFLVPEDSVSIMDGSYEGILAWITVNFLTGQLSGQNQHTVGTLDLGGASTQITFLPRFEETLKESPTDFLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALNTEVADRQMFRSSCLPKQLEAEWHFGGVKYRYGGNKEGETGFKPCYLEVLKVVKGKLHQPDEIRGSSFYAFSYYYDRAADTNLIDYEQGGVLEVRDFERKAKEVCDNMERFSSASPFLCMDLTYITALLKEGFGFRDNTLLQLTKKVNNIETSWTLGATFHLLQSLGITY
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Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity).
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E1C2I2
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GWL_CHICK
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Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L)
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MSTVEPLSDEGVAAGPRRIEVPRPPSIEEFTIVKPISRGAFGKVYLGRKAGRLYAVKVMKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEAALALDYLHRHGIIHRDLKPDNMLISNQGHIKLTDFGLSRVTLNREINMIDILTTPSMAKPKHDYSRTPGQLLSLISSLGFYTPVGMKMPINPNSGGASDSLHEVISPLSMIEKENTPLSTKLFKTGLDTSPLTPVMPVRSLTPALLQSRERFGASTASSQSCMYLSSMESECCSSPRLEKDVKQTEDEMCSTGTSNSRPPLPSSREVLNSKDPKVLKKELESAISPISSNDCGSRQKLGTERSEITDTPVTTLDTKGIVRKCLSENKIWEEKLVARREMTNEMLETASSQQSPLFLKDPVQPVKEEEIFEKPGVKRSFELVDTSPCQELNYVKKTNAEYKRGCWISELSASKSTGLTTEIQSLMLSGEICESKEIMRCIDRQQTEKPLVPTVAKNLLCDLDADHEKDKEYMNSSLLCADDEKPLGALSADSDLSFPETSVSESHLEKQLVDLDKGVKDLSFEEPKAEDLLTMSPNCQEASRNGVEADVVQNCTMLCCEQDNHQKHTEETDTISSPSEKMTETVHLFRKNNVVFRSYNSPINVSNVSDPCSMASLDIMDLSPACSGSYPTAITPLQKTPRQGDAGTPYRTPKSVRRGAAPVEGERILGTPDYLAPELLLTKPHGSAVDWWALGVCLFEFLTGIPPFNDETPAQVFQNILKRDIPWPEGEEKLSDNAQNAIDILLTFDSTKRAGLKELKHHPLFHGVDWDNLQNQPMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL
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Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity).
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E1C3P4
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CBPC1_CHICK
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Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein 1) (Protein deglutamylase CCP1)
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MKVKKNLTCSVSTSSRTMSLLSQLEKINLDSVLGEADNARYVTAKILHLVQSQEKTKKEMTSKGSSAIEVILSTLENTRDPQTILNILSILIELVSVGGGRRASVLVTKGGTQILLQLLLNASKESPPNEELMVLLHTLLAKIGPKDKKIGMKARINGALNISLNLVKQNLQNHRLILPCLQVLRVYSTNSVNAVSLGKNGVVELMFKIIGPFSKKNTSLMKVALDTLAALLKSKTNARRAVDRGYVHMLLTIYVDWHRHDSRHRYMLIRKGVLQCIKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSAFHFQLPVIPASGPVAQMYNLPPDVDDVVDESDDNDDAETESEIETEDDKDQNFKNDDIETDINKLKPRQELGRPLEELKMYEQFFPELTENFQECDLVSKEPKPFVSNANLGGPIVVPTAGEEFSAETNPSVIGISLKEGNPLLTEEYNRRPAFLGLPKKDSIKASSLLQQNVQRNLLPSCQCLSQEIVTGLDRISLQNTSENDQYYATGCVIKKDNKTSLTPLACSKTCEHVSPCGSSLFEGSSVHLGKFCCTGVESEEEDSKSSSSGEQVVLEVSDVSPVHDCDLYIEMVKTTKSIPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKISQDIERLIHQNDIIDRVVYDLDNSICSAPEEVDVLKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMKTGIGYRFNIINCEKSNSQFNYGMQPLMYSVQEALNSRPSWTRVGTDICYYKNHFSRSSIAAGGQKGKSYYTITFTVTFQHKDDVCYFAYHYPYTYSTLKMHLQKLESMHNPQQIYFRQDALCETLGGNICPIVTITAMPESNYYEHICQFRNRPYIFLSARVHPGETNASWVMKGTLEYLMSSNPSAQSLRESYIFKIIPMLNPDGVINGNHRCSLSGEDLNRQWQNPNPDLHPTIYHAKGLLQYLAAIKRLPLVYCDYHGHSRKKNVFMYGCSIKETMWHTNVNTASCDLMEDPGYRVLPKILSQTAPAFCMGSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKGLQIGTKELEEMGAKFCVGLLRLKRMASPLEYNLPSGLLDIENELIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDDQDAELADNVGDYEANNQEDGLSDSDSTRILLS
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Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins.
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E1C3U7
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LOXL2_CHICK
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Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
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MEGFLGFNHNHCFIVLFFVSLSLAQYEHWPYLPGYPEPPPQVYQPPRRPADVPKIQLRLAGQKRKHNEGRVEVFYNGEWGTVCDDDFSIHAAHVICRELGYVEAVSWLPSSKYGKGEGKIWMDNVHCNGKEATLAACTSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLLNQIENMNIQVEDIRIRPILATYRKRVPVTEGYVEVKDEGTWKQICDKHWTMKNSRVVCGMFGFPSERKYNTKVYKMFASRRKQHYWAYSMDCTGNEAHISSCKLGNHLNVDTEKNATCDNGMPAVASCVPGRAFAPSSHSGFRKAFRQEQPLVRLKGGANTGEGRVEVLKNGEWGTVCDDNWNLVSASVVCRELGFGSAKEAITGARLGQGMGPIHLNEIDCTGFEKSLTDCKFNMESQGCNHEEDAAVRCNVPAMGFQNQLRLVGGRNPYEGRVEVLAERNGTLRWGTVCSQGWSTVEAMVVCRQLGLGFASHAFQETWYWHGDVSADSVVMSGVKCSGTEMSLAHCRHDGADVSCPRGGGRFGAGVSCSETAPDLVLNAELVEQTAYLEDRPMFMLQCAQEENCLASSAVNTSVTSGYRRLLRFSSQIHNNGQSDFRPKNGRHAWVWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEADVQKQYECANFGEQGITVGCWDVYRHDIDCQWIDITDVPPGDYLFQVVINPNYEVAESDYSNNVMKCRSRYDGQRIWMYNSVHNGANQDGDTEERFSAYWKLGNSILFSR
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Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
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E1C656
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HACE1_CHICK
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E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)
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MERAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKYLPDKNGITPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYEAQMKSLLRIVRIFCHVFRIGPSSPSNGNDMGYNGNKTPRSQVFKVRKVYDVVRKIDVKEMNFTKHAFINQTSHEQEPLELLWHSLDEWLVLIATELMKNKRDSANITSILLKQKGPDHQDATPTPSFAAAGTESRKELSTDTGDSKTYEVAGKQEAYADCQDVISMTANRLSAVIQAFYMCCSCQMPQGMTSPRFIEFVCKHDDVLKCFVNRNPKIIFDHFHFLLECPELMSRFMHIIKAQPFKDRCEWFYEHLHSGQPDSDMVHRPVNENDILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMGQGVVREWFDILSSEIVNPDYALFTQSADGTTFQPNSNSSVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGGSGLQNFTIAAVPYTANLLPTSSTCINMLKLPEYPSKEILKDRLLVALHCGSYGYTMA
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E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division.
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E1C7U0
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STING_CHICK
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Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
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MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP
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Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol. Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity).
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E1C8P7
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DSCL1_CHICK
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Cell adhesion molecule DSCAML1 (Down syndrome cell adhesion molecule-like protein 1 homolog)
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MWLVTFFLLYSLRKAHTEDVGTSLYFVNDSIQQVTFSSTVGVVIPCPAAGSPSAVLRWYLATGDDIYDVPHIRHVHANGTLQLYPFSPSAFNSFIHDNDYFCTAENSAGKIRSPNIRVKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSIIPENRFFITSYGGLYISDVQKEDALSTYRCITKHKYSGETRQSNGARLSVSDADPAESIPTMLDSFQSREVRAGRLVELPCIASGYPNPAIRWLKDGRPLPADGRWAKRITGLSIADLRVEDSGTYICEVTNTFGSAEVTGTLTVIDPLRVTLTPKKLKTGIGSTVILSCALSGSPEYVIRWYRNTDLVVVDDFISIRGISNETLLITAAQKSHSGAYQCFATRKSQTAQDFSIITLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPIPRDNGHRTNQYTMSDGTTVSHMNVTSPQIKDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMKNITAVAGRDTFINCRVIGYPYYSIKWYKDSLLLPDNHRQVVFENGTLKLMDVQKGMDEGEYLCSVLIQPQLSISQSVHVTVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIHITWRKDGHVILSGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPIPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKSMFLTVKIPAMITSHPNTTIAIKGQSKELNCTARGERPIIIRWEKGDTVIDPDRNMRYAIATKDNGDEVISTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPMTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRAISITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYMDGEWGEMQNITTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDIPGPPAGIKAVPSSASSVVVSWLPPAKPNGIIRKYTIFCSSPGSGQPAPSEYETSPDQLFYRIAHLNRGQQYMLWVAAVTSAGRGNISEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGEPVPAIKWTKDSEDSAIPVTVDGHRLIQANGTLVLRSVKAEDSGYYTCTATNTWGFDTIIINLLVQVPPDQPRLTVSKTSASSITLAWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLESLKCGTWYKVKLAAKNSVGAGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWSSGGCPITAIVLEYRPKGNWGWQSLRTNSSGEVFLTELREATWYELRMKACNSAGCGNESTQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIACPIILATLGVALLFIIRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDTEFSQAVNPQSFCTGVSLHHPALIQNTGPLIDMSDIRPGTNPVSRKSVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGITVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTTDNADSMTSMSTPSEPGICRFTASPPKPQDSERGKSVAVPIPHRASKSDYCNLPLYVKSDAFFRKPDSHEPCPVVPPREASIRSLARGYHPPARHLTLDPAAKPPGLPPPSSSSSSTTLPQRTLPMPTAASTAPAPAPAPAAPAEPPANTTTTTTTHSKVGGSRDSLLEMSTSGAGRAQKQGAGAYSKSYTLV
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Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.
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E1JIB2
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IYD_DROME
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Iodotyrosine deiodinase (EC 1.21.1.1) (Halotyrosine dehalogenase) (Protein condet)
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MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF
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Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine. Activity towards 3-fluoro-L-tyrosine is weak. Important for male and female fertility. May be involved in maintaining the viability of sperm, both during development in the testes and storage in the female spermatheca.
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E1JIT7
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PSD_DROME
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PH and SEC7 domain-containing protein (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6) (Exchange factor for Arf 6)
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MSEELKVVLRRSEQHSGFGFSLLGTTGPPHVIYDIVENSPAADCGAVEAGDVILKVNGTDVHRYTTKEVLKCLRLSEQLVTLELKRDPKLKARIKEQLANTQSPHYVDIESPNIYDYHSSSTNSSPNHRPNAGGKGAATTPSQTGLRYKSPTHLPSLRQNSSPLLASGSTTTTTTATHTHSHSRNSSASSTKIKVVETSITTSTTNVVGLTSPTGSVGGGVGGEATSPTFRPSRIPQALTKCAVPKPVPVLHSPQNKRPRPSQIPTKAANGNGNGHTAHLPPQSLQHSNSYSGSPVTRQRFADREPEREPEPNSAPPQPAKAPRFEAYMMTGDLILNLSRTPQTSNPLPAQAKKIDSLRDSPSRLVNPRINGALAPRASGESSPTSSSSVDSPTNTSSDSVKREAKLLQKQQQQQQQTYQQQQQRDSINNSYNRKDSLTNDTLLMCEELEPDEEGEYVLEEDNKQQRQRQQQQRYRQQQNQQRYEYYQNEDELEEQEEVEEEREEDQTHYDITNIETYQSGVGRGDDDDSDRQCLVDDDDDDDAYDDEENDAGDEDYSTNSLGSGSAKQRLRALKQRTATRQQQRNRDAVDCAGRSGSGSSSTTVKSEAGGLGLDETSFSVPTSPISLSTPLIDKETANSVPTSPEPSSLVPESSSGAGAGAVVVRRHNGHVVRKCDAAGFRTSKSEDHLQQIQREGIAAVIPIDIDEDVNSSLNTLLDTRQDSEDSQSMATVIVNNSSLASNNNEGEQTDNRSSSSSSNSSDNNNCSSNTGEPATSETATATATIITATSTRTMNCSSKLNYILCKKASDRDRIVWTYNAPLQPHQLAALQRQQQQQEQQFQQQQQQLHQQHLQQQQQLQQQHQQQQQQQQQQQQQQLYGQQSHSNSHSSSISSSPQHSAVGSPASPTSVSSSVMSSSGSKGALGLGSSSNGPMAAVQQQQLREREQGGQVAQPPSGIPGLLSCPGGGCGNNGGGGGIGGGGNNDQSVSEAISNISSPDYQDDDNLLSSRDILGGMVLSDPSDSDSTILVSDAAAHQRQQLKQQLRAQQQQQRERERDRDRDREQSEHKVVIQVRGLDSNSSGGNGTNGRSEEDVVTLTDEPLGTMTVGMRDASPPVSDDGSDVESLHSYHYSPKAVDMPSAIRLAKRLHSLDGFKKSDVSRHLSKNNDFSRAVADEYLKHFTFEKKSLDQALREFLQQFSLSGETQERERVLVHFSKRFLDCNPGTFNSQDAVHTLTCAIMLLNTDLHGQNINRKMSCAEFVDNLADLNDGENFPKDVLKSLYQAIKTKPLEWALDEEAGDLQQQRANNSALGNVGLNPFLDPPELATAVEYKKGYVMRKCCYDSSFKKTPFGKRSWKMFYCTLRDLVLYLHKDEHGFRKSQMSDNLHNAIRIHHALATKANDYTKKQHVFRLQTADQAEYLFQTSDSKELQSWVETINYVCAAISAPPLEGGVGSQKRFQRPLLPSKQSKLMLKEQLDSHEVQLAQLDQELNEHKKGPIPSKGLALQNYKEKESYLQYELRRYRTYVSILSAKMLADQQQLELQAQQPSPASHEEEADTFPVGTTACTPPTPQSINQKDQQKEQQQQQPTNRKEKKKK
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Guanine nucleotide exchange factor for Arf6. Regulates axon growth and branching by inhibiting microtubule polymerisation at the cortex. Together with shot, promotes axonal microtubule bundle integrity. Required for normal ethanol-induced tolerance and preference. Probably by activating Arf6, counteracts ethanol-induced sedation.
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E1U8D0
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SOGA1_MOUSE
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Protein SOGA1 (SOGA family member 1) (Suppressor of glucose by autophagy) (Suppressor of glucose, autophagy-associated protein 1) [Cleaved into: N-terminal form; C-terminal 80 kDa form (80-kDa SOGA fragment)]
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MLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSEHELDVTLSEDSCSVLSEPSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQRCDLASCQSTRPMLETDAEAGDSAQCVPAPLGETLEPHAARLCRAREAEALPGLREQAALVSKAIDVLVADANGFSVGLRLCLDNECADLRLHEAPDNSEGPRDAKLIHAILVRLSVLQQELNAFTRKADVALGSSGKEQPEPFPALPALGSQGPAKEIMLSKDLGSDFQPPDFRDLLEWEPRIREAFRTGDLESKPDPSRNFRPYRAEDNDSYASEIKDLQLVLAEAHDSLRGLQEQLSQERQLRKEEADSFNQKMVQLKEDQQRALLRREFELQSLSLQRRLEQKFWSQEKNILVQESQQFKHNFLLLFMKLRWFLKRWRQGKVLPSEEDDFLEVNSMKELYLLMEEEEMNAQHSDNKACTGESWTQNTPNECIKTLADMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHASQMELKAGKGASERPGPDWKAALQREREEQQHLLAESYSAVMELTRQLQLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPWVLKHSDMEKQDNSWKEARSEKTHDKEGVSEAELGGTGLKRTKSVSSMSEFESLLDCSPYLAGGDARNKKLPNGPAFAFVSTEPVEPEKDAKEKAGLSTRDCSHIGSLACQEPAGRQMQRSYTAPDKTGIRVYYSPPVARRLGVPVVHDKEGKILIEPGFLFTTAKPKESAEADGLAESSYSRWLCNFSRQRLDGGSGASTSGSGPAFPALHDFEMSGNMSDDMKEITNCVRQAMRSGSLERKVKNTSSQTVGVATVGTQTIRTVSVGLQTDPPRSSLHSKSWSPRSSSLVSVRSKQISSSLDKVHSRIERPCCSPKYGSPKLQRRSVSKLDSTKDRSLWNLHQGKQNGSAWARSTTTRDSPVLRNINDGLSSLFSVVEHSGSTESVWKLGMSEARTKPEPPKYGIVQEFFRNVCGRAPSPTTAAGEESCKKPEPLSPASYHQPEGVSRILNKKAAKAGGSEEVRPTMLSQVGKDGILRDGDGSLILPSEDAVCDCSAQSLASCFIRPSRNTIRHSPSKCRLHPSESGWGGEERAAPQ
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Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner.
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E1WAC8
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SCTB1_SALTS
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SPI-1 type 3 secretion system translocon protein SctB (SPI-1 T3SS translocon protein SctB) (Cell invasion protein SipC) (Effector protein SipC)
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MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLSAPAPGVLTQTPGTITSFLKASIQNTDMNQDLNALANNVTTKANEVVQTQLREQQAEVGKFFDISGMSSSAVALLAAANTLMLTLNQADSKLSGKLSLVSFDAAKTTASSMMREGMNALSGSISQSALQLGITGVGAKLEYKGLQNERGALKHNAAKIDKLTTESHSIKNVLNGQNSVKLGAEGVDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGIKDSNKQISPEHQAILSKRLESVESDIRLEQNTMDMTRIDARKMQMTGDLIMKNSVTVGGIAGASGQYAATQERSEQQISQVNNRVASTASDEARESSRKSTSLIQEMLKTMESINQSKASALAAIAGNIRA
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Component of the type III secretion system 1 (SPI-1 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). SipB/SctE1 and SipC/SctB1 are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells (By similarity).
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E1WKT5
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SOTC_BACF6
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N-succinylornithine carbamoyltransferase (EC 2.1.3.11) (N-succinyl-L-ornithine transcarbamylase) (SOTCase)
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MKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSLRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEAIPVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHPLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYEFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYTGDNYGQILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPEAANREISATVVLKRLLENLP
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Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-succinyl-L-ornithine to produce N(2)-succinyl-L-citrulline. Is essential for arginine biosynthesis. Has no activity with either L-ornithine or L-aspartate as substrate. Has also no detectable AOTCase activity, being unable to convert N(2)-acetyl-L-ornithine to N(2)-acetyl-L-citrulline.
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E1XUJ2
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LDI_CASDE
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Linalool dehydratase/isomerase (EC 4.2.1.127) (EC 5.4.4.4) (Geraniol isomerase) (Linalool dehydratase-isomerase) (Myrcene hydratase)
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MRFTLKTTAIVSAAALLAGFGPPPRAAELPPGRLATTEDYFAQQAKQAVTPDVMAQLAYMNYIDFISPFYSRGCSFEAWELKHTPQRVIKYSIAFYAYGLASVALIDPKLRALAGHDLDIAVSKMKCKRVWGDWEEDGFGTDPIEKENIMYKGHLNLMYGLYQLVTGSRRYEAEHAHLTRIIHDEIAANPFAGIVCEPDNYFVQCNSVAYLSLWVYDRLHGTDYRAATRAWLDFIQKDLIDPERGAFYLSYHPESGAVKPWISAYTTAWTLAMVHGMDPAFSERYYPRFKQTFVEVYDEGRKARVRETAGTDDADGGVGLASAFTLLLAREMGDQQLFDQLLNHLEPPAKPSIVSASLRYEHPGSLLFDELLFLAKVHAGFGALLRMPPPAAKLAGK
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Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol. Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene. Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene. In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol. Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates.
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E2AXC7
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BRCC3_CAMFO
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Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-)
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MDDSSLQKVELQTDVYMVCLQHALSTENFEVMGLLIGNFACGIAKISAVIILRRLDKKKDRVEISSEQLLKAAAEAERLTVELNRPMRVLGWYHSHPHITVCPSHVDVRTQATYQTMDHSFVGLIFSVFSEGKESKEHEIFLNCFQSDNGEATEIPLEIVHTPDISDRCLRTMTDLSKILVQEEEDMAEACKDHPDVLASIHNNAVRTRALIHITDIITKPLVQTFEKRIALNKLRATHLQRQLQELQKMCNG
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Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity. Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).
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E2BJ30
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ORCO_HARSA
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Odorant receptor coreceptor
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MMKMKQQGLVADLLPNIRVMKFFGHFVFNYYDDNSSKYLHKIFCCVNLFLLLLQFALCAVNLIIESADVDDLTANTITLLFFTHSIVKIIYFAVRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGATTVLSAIAWTVLTFFEHPIRKLVDPVTNETTIIELPQLLLRSYYPFDASKGIMHVIVLIYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSAEHLRESENQPPPPVPPQGDSMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEMLVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGVNVYAASTIGYIIYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK
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Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization. Required for pheromone sensing and mating behavior. Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli.
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E2DWQ7
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A3AKI_PHYIN
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RxLR effector protein Avr3a (Avirulence protein 3a)
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MRLAIMLSATAVAINFATCSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTKRADAKKLAKQLMGNDKLADAAYIWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY
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Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways. Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, further abolishes host cell death during the biotrophic phase of infection. Associates also with the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis. The Avr3A(KI) form is recognized by R3a which triggers R3a-mediated hypersensitivity and suppresses INF1-induced cell death.
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E2E2N7
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BCGS_ORIVU
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Bicyclo-germacrene synthase (EC 4.2.3.100) (Allo-aromadendrene synthase) (EC 4.2.3.-) (Geraniol synthase) (EC 3.1.7.11) (Limonene synthase) (EC 4.2.3.20) (Terpene synthase 4) (OvTPS4) (Terpinolene synthase) (EC 4.2.3.113)
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MEIYSPVVPAVKDVKRLDEIRKSAKFHPSIWGDFFLSYNSDNTQISEAEEEEVAKQKEAVRELLAQVPEGSTYKMELIDLIQRLGVNYHFEKEIHDSLNYIHENSQHNDDEVRTTALRFRLLRQQGYRVPCDVFRKFTDGEGNFATALTNDVEGLLELYEASHLATRGEEILDRAMEFSSSHLQALLNQHLVGSVSLSKRVDEALKMPIRKTLTRLGARKFISLYQEDESRNELLLNFAKLDFNMVQKMHQRELSDATRWWKKLEVAKRMPYARDRVVECFFWIVGVYFEPCYATARRILSKAINMASIVDDTYEYATLDELQILTDAIQRWDVNETLEDSPPHVQMCYKALIQAYAEIEDEVVENFGGEELYRVQYAIEHVKQSAVAFFEEAKWIYNNSIPTVEEYMKVAFVTCGYMMLSTTSLVGVGSDRVSKADFDWIVNEPLIVRASCVICRLMDDLVGDEYEEKPSSVLCYMKQYVVSKDEARARLEQQVKDAWKDMNEECIEPRPASMQILTRVLNLGRVIHLLYREGDSYTDPNRSKEWVKMVFVDPI
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Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is greatly favored while both alloaromadendrene and bicyclo-germacrene are produced in equivalent amounts in the presence of magnesium. Can also convert geranyl diphosphate (GPP) to terpinolene, limonene and geraniol, and this conversion is not affected by the presence of magnesium or manganese.
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E2E2P0
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GTPS_ORIVU
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Gamma-terpinene synthase, chloroplastic (EC 4.2.3.114) (Alpha-terpinene synthase) (EC 4.2.3.115) (Terpene synthase 2) (OvTPS2)
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MATLSMQVSILSKEVKNVNNIGMRASKPMVARRVSTTRLRPICSASLQVEEETRRSGNYQASIWNNDYVQSFNTNQYKDEKHLKKKEELIAQVKILLNTKMEAVKQLELIEDLRNLGLTYYFQDEVKKILTSIYNDHKCFKNEQVGDLYFTSLGFRLLRLHGFDVSEEVFDFFKNEDGSDFKASLGENIKDVLQLYEASFLIREGEVILEQARVFSTKHLEKKVDEGINDEKLLAWIRHSLALPLHWRIQRLEARWFLDAYRARKDMIPLIFELGKIDFHIIQETQLEELQEVSKWWTNSNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYGTLDELQLFTDAIRKWDFQSISTLPYYMQVCYLALYTYASELAYDILKDQGFNSIAYLQRSWLSLVEGFFQEAKWYYAGYTPTLAEYLENAKVSISSPTIISQVYFTLPNSTERTVVENVFGYHNILYLSGMILRLADDLGTTQFELKRGDVQKAIQCYMKDNNATEKEGAEHVKYLLREAWKEMNTAMADPECPLSEDLVDAAANLGRASQFIYLEGDGHGVQHSEIHNQMGGLIFEPYV
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Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:20419468, Ref.2, PubMed:30231481, PubMed:26156773). Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to gamma-terpinene and the minor products alpha-thujene, alpha-terpinene, myrcene, sabinene, (+)-R-limonene, alpha-pinene and alpha-phellandrene (PubMed:20419468, Ref.2).
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E2JF22
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PIEZ1_MOUSE
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Piezo-type mechanosensitive ion channel component 1 (Protein FAM38A)
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MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLLRALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTRLVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGAPALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTWWSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDLPNYSSPNALVLNTKHAWPIYVSPGILLLLYYTATSLLKLHKSCPSELRKETPREDEEHELELDHLEPEPQARDATQGEMPMTTEPDLDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLHGLGHLIMDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLYGLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFVKEKLLKKQKVPAALLEVTVADTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFAGRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPTYWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHVPPPGTRHPRWAHRQDAVSEAPLLEHQEEEEVFREDGQSMDGPHQATQVPEGTASKWGLVADRLLDLAASFSAVLTRIQVFVRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFALPYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEINQSLLYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQAVCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAILTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSKAIPMNSALIKWLYLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGINTDHLEPLRGEPNPIPNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVAGATRISIFGLGYLLACFYLLLFGTTLLQKDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYDPKEMMTRDRDCLLPVEEAGIIWDSICFFFLLLQRRIFLSHYFLHVSADLKATALQASRGFALYNAANLKSINFHRQIEEKSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSKDPQDPSQEPGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQMAYQAWVTNAQTVLRQRRERARQERAEQLASGGDLNPDVEPVDVPEDEMAGRSHMMQRVLSTMQFLWVLGQATVDGLTRWLRAFTKHHRTMSDVLCAERYLLTQELLRVGEVRRGVLDQLYVGEDEATLSGPVETRDGPSTASSGLGAEEPLSSMTDDTSSPLSTGYNTRSGSEEIVTDAGDLQAGTSLHGSQELLANARTRMRTASELLLDRRLHIPELEEAERFEAQQGRTLRLLRAGYQCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVMVVTKYLFQFGFFPWNSYVVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQLLCYGLWDHEEDRYPKDHCRSSVKDREAKEEPEAKLESQSETGTGHPKEPVLAGTPRDHIQGKGSIRSKDVIQDPPEDLKPRHTRHISIRFRRRKETPGPKGTAVMETEHEEGEGKETTERKRPRHTQEKSKFRERMKAAGRRLQSFCVSLAQSFYQPLQRFFHDILHTKYRAATDVYALMFLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLRKTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCGYPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYANIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKHTLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLGVRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGFLAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTRERE
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Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology. Acts as sensor of phosphatidylserine (PS) flipping at the plasma membrane and governs morphogenesis of muscle cells. In myoblasts, flippase-mediated PS enrichment at the inner leaflet of plasma membrane triggers channel activation and Ca2+ influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation.
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E2QWQ2
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NLK_CANLF
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Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase)
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MSLCGARANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPITNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
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Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner. Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes.
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E2QY99
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PALS1_CANLF
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Protein PALS1 (MAGUK p55 subfamily member 5) (Protein associated with Lin-7 1)
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MTTSHMNGHVTEESDNEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVKILEVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAVTVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLSAPHVQALLLAHDKVAEQEMQLEPFTDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHIISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRSRRDHEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSSWLR
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Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells. Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface. Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (By similarity). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing premature differentiation, and is required for cerebellar histogenesis, fissure formation, cerebellar layer organization and cortical development (By similarity). Plays a role in neuronal progenitor cell survival, potentially via promotion of mTOR signaling (By similarity). Plays a role in the radial and longitudinal extension of the myelin sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter (By similarity). May play a role in the T-cell receptor-mediated activation of NF-kappa-B (By similarity). Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). Required for the normal polarized localization of the vesicular marker STX4 (By similarity). Required for the correct trafficking of the myelin proteins PMP22 and MAG (By similarity). Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
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E2QYC9
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INADL_CANLF
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InaD-like protein (Inadl protein) (Channel-interacting PDZ domain-containing protein) (Pals1-associated tight junction protein) (Protein associated to tight junctions)
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MPENPAPDKLQVLQVLDRLKMKLQEKGDTSQNEKLSLFYETLQSPLFNQILTLQQSIKQLKGQLSHIPSDCSTNFDFSRKGLLVFTDSAITNGNAQRPSNNLTVSGLFPWTPKSGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGEVDIFVKEVQPGSIADRDQRLRENDQILAINHTPLDQNISHQQAIALLQQTTGSLHLVVAREPVHTKSRTSINLTDTTMPETVHWGHIEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGDTDVQGMTSEQVAQVLRNCGNSVRMLVARDPVGETSVTPPTPAALPVALPAVANRSPSTDSSLYETYGVELIKKDGQSLGIRIVGYIGTAHTGEASGIYVKSIIPGSAAYHNGQIQVNDKIVAVDGVNIQGFTNQDVVEVLRNAGQVVHLTLVRRKMCSSTSPLERSSDRGTVVEPSGTPARYVTGAVETETNLDGGDEETEERMDNLKNDNIQALEKLERVPDSPENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDALNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRTTETLLPEMEADHNVDINTEEEEEEELALWSPEVKIVELVKDHKGLGFSILDYQDPLDPTRSVIVIRSLVANGVAEKGGELLPGDRLVSVNEYCLENTTLAEAVEVLKAVPPGIVHLGVCKPLVDNDKEEESHYILHSNNNEDETELSETIHDINSSLILEAPKGFRDEPYYKEELVDEPFLDLGKAFQSQQKEIDNSKEAWEMQEFLPPRLQEMGEEREMLVDEECDLYQDHFQSMDLYPSSHLQEAAPVSSVKELHFGTQWLHDSEPPELQEARSMMNMYSQETQQYGYSTENMIKENFGIDSLPSISSSEGNSQQGRFDDLENLNSLTKSSLDLGMMIPNDVQGPGMLVELPAVAQRREQEDLPLYQLPRTRVVSKASAYTGASSSRYTAGACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNALKTGDKILEVSGVDLQNASHREAVEAIKNAGNPVVFVVQSLSSTPRVIPSVHNKANKIANNQDQNTEEKKEKRQGTPPPPMKLPPPYKAPSDDSDENEEEYAFTNKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAATDGRMRIGDELLEINNQILYGRSHQNASAVIKTAPSKVKLVFIRNEDAVNQMAVAPFPVPSSSPSSLEDQSGTEPVSSEEDGSLEVGIKQLPENESSKLEDISQVAGQGMVAGQQKALDCPTDNAVSQMKPQKYSTKVSFSSQEIPLAPAPSYHSTDVDFTSYGGFQAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGRDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGIDLRSASHEEAITALRQTPQKVRLVVYRDEAHYRDEENLEIFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDRRLIQGDQILSVNGEDMRNASQETVATVLKCAQGLVQLEIGRLRAGSWTSSRKTSQNSQGSQHSTHSSFHPSLAPVITSLQNLVGTKRATDPSLKSSGMDMGPRTVEIIRELSDALGISIAGGKGSPLGDIPIFIAMIQASGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRIILQVVADTNISAIATQLENMSTGYHLGSPTAEHHPEDTEEPLQMTAG
|
Scaffolding protein that facilitates the localization of proteins to the cell membrane. Required for the correct formation of tight junctions and epithelial apico-basal polarity. Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells. Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration. May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity).
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E2RAK7
|
APOA2_CANLF
|
Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II (Apolipoprotein A-II(1-76))]
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MKLLAVTVLLLVICSLEGAFVRRQAEEPNLQSLVSQYFQTVTDYGKDLMEKAKGPELQAQAKAYFEKTQEQLTPLVKKAGTDLLNFLSNFMDLKTQPATQ
|
May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
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E2RD63
|
PLD6_CANLF
|
Mitochondrial cardiolipin hydrolase (EC 3.1.4.-) (Choline phosphatase 6) (Mitochondrial phospholipase) (MitoPLD) (Phosphatidylcholine-hydrolyzing phospholipase D6) (Phospholipase D6) (PLD 6)
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MERFRWQVAAVAAVGLALALEALPSVLCWLRAGRRQQQRPPRRQVLFFPSQVTCTEALLQAPGEAPSGPPAGCRCSLPHGESSLSRLLRALLAARASLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDKKVLITGSLNWTTQAIQNNRENVLIMEDEEYVRLFLEEFERIWEEFNPTKYTFFPQKKTGTSLPPQVSCFGQLVSCHSKCSHHLSQV
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Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity).
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E2RDM9
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TSPO2_CANLF
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Translocator protein 2
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MQPQGAIFVALPHLGPILVSLLTRHRMIRWYDIPKKPPWCPPHKVLLAGWITIYFVMGYASYLVWKDLGGGFGRPLALPLGLYAVQLAVSWAVLIFFFAAHAHGLALLHMLLLYGLVVSTALIWHPINKLAAVLLLPYLAWLTVTASIAYHLWRDSLCPNHHQPLPMGEKRD
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Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum. Required to meet cholesterol demands during erythropoietic differentiation. May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-mediated ATP export, and import of the heme precursors protoporphyrin IX and 5-aminolevulinic acid (By similarity).
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E2RDP2
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ATG4D_CANLF
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Cysteine protease ATG4D (EC 3.4.22.-) (Autophagy-related protein 4 homolog D) [Cleaved into: Cysteine protease ATG4D, mitochondrial]
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MNSVSPAAAQYRSGSPEDARRPEGRRPRGPRVPDPNGPRPSGASGPALGSPAAAPGEPDEVDKFKAKFLTAWNNVKYGWAVKSRTSFSKISSVHLCGRRYRFEGEGDIQRFQRDFVSRLWLTYRRDFPPLAGGCLTSDCGWGCMLRSGQMMLAQGLLLHFLPRDWTWAEGPGLGPSEPAGLASPNRYRGPARWMPPRWAQGTPELEQERRHRQIVSWFADHPQAPFGLHRLVELGQSSGKKAGDWYGPSLVAHILRKAVESCSEITRLVVYVSQDCTVYKADVARLVARPDPTAEWKSVVILVPVRLGGETLNPVYVPCVKELLRSELCLGIMGGKPRHSLYFIGYQDDFLLYLDPHYCQPTVDVSQADFPLESFHCTSPRKMAFAKMDPSCTVGFYAGDQKEFETLCSELTRVLSSSSATERYPMFTLAEGHAQDHSLDDLCSQLSQPTLRLPRTGRLLKAKRPSSEDFVFL
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[Cysteine protease ATG4D]: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (By similarity). ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system. Compared to other members of the family (ATG4A, ATG4B or ATG4C), constitutes the major protein for the delipidation activity, while it promotes weak proteolytic activation of ATG8 proteins (By similarity). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (By similarity). [Cysteine protease ATG4D, mitochondrial]: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.
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E2RDZ6
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SIR5_CANLF
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NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5)
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MQPLQIAPCRLLYGLYRGLKSPASTGTRICPAMARPSSNMADFRKLFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPQAFARNPSLVWEFYHYRREVMLSKEPNPGHLAIAECEARLREQGRRVMVITQNIDELHRRAGTKNLLEIHGSLFKTRCTSCGIVAENYKSPICPALSGKGAPDPEAQDARIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDKELTLCDLCLVVGTSSVVYPAAMFAPQVSARGVPVAEFNMETTPATNRFRFHFQGPCGTTLPEALAPHETGNVS
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NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000255|HAMAP-Rule:MF_03160}.
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E2RG47
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STT3B_CANLF
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Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18)
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MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGVAPPKPAPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKRENPPVEDSSDEDDKRNPGNLYDKAGKVRKHVTEQEKTEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNESAAYKIMRSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV
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Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation.
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E2RH47
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RS3_CANLF
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Small ribosomal subunit protein uS3 (EC 4.2.99.18) (40S ribosomal protein S3)
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MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
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Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Has endonuclease activity and plays a role in repair of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA. Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS). Has also been shown to bind with similar affinity to intact and damaged DNA. Stimulates the N-glycosylase activity of the base excision protein OGG1. Enhances the uracil excision activity of UNG1. Also stimulates the cleavage of the phosphodiester backbone by APEX1. When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage. Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide. Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes. Represses its own translation by binding to its cognate mRNA. Binds to and protects TP53/p53 from MDM2-mediated ubiquitination. Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization. Involved in induction of apoptosis through its role in activation of CASP8. Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5. Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation.
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E2RK30
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PKHD1_CANLF
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Fibrocystin (Polycystic kidney and hepatic disease 1 protein) (Polyductin)
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MIVWLISLMSIEILLLAGPALSFHIEPKEGSLAGGTWITVIFDGLELEQLYPTNGSQLEIHLVNVAVPALPSIPCDVSPVFLDLPVVMCRTRSLLPEVHEGLYYLEAHAGGQVVGSPSPGLQDCCTFKFSREQTPIVYQVTPPSGVPGKMIHVYGWIITGRSETFDFDAEYIDSPLILEAQGDKWVTACSLINRQTGSCYPLQENHGLGTLQCRVEGNYIGSQNVSFSVFNKGKSMVHKNAWLVSAKLDLFLYQTYSEILSVFPETGSLGGKTDIIITGDFFDNPALVTIAGVPCDIRHMSPRKIECTTRAPGKRARLTAPQAGNRGLLFEVGEAVEGLDLTVATPGYRWQIVPNASSPFGFWFKEGQPFRARLSGFFVAPETNNYTFWIQADNQASLYFSQSEDPRMKVKVASIRVGTADWFDAWEQDRNEGVWQRKTPKLELVGGTRYYLEAEHYGRTPSRGMRIGVQIHNTWLNPDVVSTYLREKHQIRVRAQRLPEIQMLTVSGRGSFFLTWDNVTSQPIPENATAHQIQTAIEELLAVKCKLEPLSANILLWLGFEQGPEGSSFEGDLTSGTEPFCGRFSLHQPRRLVLTPPAAQKDYWLDRYTHLCIAYKGRMKNILKVTVFFTTDFQNFIKKNITCDWNLVGTRPNSWQFTCTDLWETCVHHSMYLQPPLVDSPVLVHRIDLFPLSQETSGFYVDEIIIADTNITVSQADSETAHPGGNLVESLCVVGSPPVYNISFWLVGCGQELPLITASIVPTGGEARRSGLVQVTTQRIQKTSPPLGGYFHIQLPTSVIPDVPVHISASHLRKLLQNNADNFTSRYLNSSDLTVMEDLKSCYEHEWTLSWSSQVGDLPNFIRVSDANLTGVNPAATVRVVYDGGVFLGPVFGDMLVTANQHTQVVVRVNDIPAHCSGSCSFQYLEGSTPQIHSAWYSLDGDISLLIYIFGINFSGDPQALEIMVNKTNCKVIFSNQTNVICQTDLLPVGMHRLFMVVRPFGRAINTSGEALFLSVEPRLDAVEPSRAAEIGGLWATIQGSGLEDVSLVLFGSQSCAINITTSNSRRIQCRVPPRGKDGPVVNLTVVSGDHSAVLPMAFTYVSSLNPVITSLSRNRSNIAGGDTLFIRMALLVNYTDLDVEVCIQNTLAPAHVQMPQGLEVVLPPLPAGLYSISVSINGISIRSPGVDLHIQYITEVFSIEPCCGSLLGGTILSISGIGFIRDPTLVWVFVGNRSCDILNSTETVIWCETPPAALLPDSNIPAIPVPMEIWAGNVSFARESLLNLSFTFLYEAAMTPVVTAMRGEIINNSLRFYVEGNNLSNSVILLGVSHCDLETQTLRNNVSLSGCSFPLHSLEAGFYPLQVRQKQMGFANMSAVPQQYVITPWIMAISPTHGSACGGTVLTVRGLALSSRKRSVQVDLLGPFTCVILSLGHQTILCQINKVNDSFPDVSFTLNVTVIVNGLPSECQGNCTLFLQEETTPIVDSLTTNISGSLTMVLIRGRKLGITAVEPMVFVDDHLPCIVTFFNASYVICWISDLTPGLHYVSVFHARNGYACFGNVSRHFYILPQVFHYFPKNFSIHGGSLLTVEGTALRGKNSTLVYVGQQACLTVSISTELIQCIVPAGNGSVGLVIEVDGLSYQMGVIGYSSAFTPRLLSISQTDDVLTFAVAQVSGAENVDIFIGMSPCVGISGNHTVLQCVVSSLPAGEYPVRGYDRMRGWASSVLVFTSTATISGVTENFGCLGGRLVHVFGAGFSPGNVSAAVCGAPCQVLANATVSAFSCLVLPLNVSLAFLCGLKHSEESCEASSSTYVQCDLTVTVGTETLPQSWPYLYICEESPQCLFAPDHWTESTFPWFSGLFISPKVERDEVLIYNSSCNIAMETEAKMECETPNQPITAKITEIRKSRGQSTQGNFSLQFCLRWSRTHSWFPERVPQDGDNVTVENGQLLLLDTNTSILNLLHIKGGKLIFMDPGPIELRAHAILISDGGELRIGSEDKPFQGKAEIKLYGSSHSTPFFPYGVKFLAVRNGTLSLHGLLPEVTFTHLQAAAYAGDTVLALEDAVDWHPGDEAVIISRIGVGGAKPMEEIVIVEAVHNTDLYLRSPLRYSHNFTENWVAGVLHILKVTVVLLSRSITIQGNLTAERMKHLASCQEASDSEGNLQDCLYSKSEKMLGSRDLGARVIVQSFPEEPSRVQLRGVQFRDLGQAFRKHVSALTLVGAMRDSYVQGCTVWSSFNRGLSMSMTLGLKVDSNIFYNILGHALLVGTDMDIKYISWEAAPEKKPDWSEQGNIIRNNVIISISGTEGLSSPEMLTPSGIYILNPTNVVEGNRVYVAGLGYFFHLVTSQTSQAPLLSFTQNIAHSCTRYGLFIYPQFQPPWDDGRGPTLFQNFTVWGSAGGARISRSSNLHLKNFQVYSCRDFGIDILESDANTSVTDSLLLGHFAHKGSLCMSAGIKTPKRWELIISNTTFVNFDLTDCVSIRTCSGCSRGQGGFTVKTNQLKFINSPNLVAFPFPHAAILEDLDGSLSGRNRSHILASMETLSASCLVNLSFSQIVPGSVCGEDVIFHHMSIGLANAPNVSYDLTITDSRNKTTTVNYVRDTLSNLYGWMALLLDQETYSLQFETPWISRSLQYSATFGSFAPGNYLLLVHTVLWPYPDILVRCGSQEGRSLPSLPLPGQDQGCDWFFNTQLRQLIYLVSGEGQVQVTLQVKEGVPPTISASTSAPESALKWSLPEAWTGIEEGWGGHNHTIPGPGDDILILPNRTVLVDTNLPFLKGLYVMGTLEFPVDRSNVLSVACMVIAGGELKVGTLDNPLEKEQKLLILLRASEGIFCDRLNGIHIDPGTIGVYGKVQLHGACPKKSWTRLAADIASGNERIIVEDAVDWRPHDKIVLSSSSYEPHEAEILTVKEVQAHHVKIYERLKYRHIGSVHVMEDGRCIRLAAEVGLLTRNIQIQPDISCRARLLVGSFRNSSSKEFSGVLQLSNVEIQNFGSPLYSSIEFTNASAGSWIISSSLHQSCSGGIRAAASHGIILNDNIVFGTVGHGIDLEGQNFSLSNNLVVLMTQSAWSTVWVAGIKANQAKDINLYGNVVAGSERIGFHIQGHRCSSPEARWSDNVAHSSLHGLHLYKENGLDNCTGISGFLAFKNFDYGAMLHVENSVEIENITLVDNSIGLLATVYVSSVPKSHIENVQIVLRNSVIIATSSSFDCIQDRVKPRSANLTSSDRAPSNPRGGRVGILWPIFTSEPNWWPQEPWHRVRNGHSTSGILKLQDVTFSNFVKSCYSDDLDICILPNVENTGIMHPIMAEGTRMLKIKDKNKFYFPPLQARKGLGILVCPESDCENPRKYLFKDLDGRALGLPPPVSVFPKTEAEWTGSFFNTGTFREEQKCTYRALIQGYICKQSDQAILILDNADATWAMQKLYPVVSVTRGFVDTFSSVNADAPCSTSGSASTFYSILPTREITKICFVDQTPQVLRFFLLGNRSTSKLLLAVFYHELQNPRVFIGESFIPPIMVQSTSSLLDESIGSNYFSILDNLLYVVLQGQEPIEIHSGVSIHLALTVMFSVLEKGWEIIILERLTDFLQVSQDQIRFIHEMPGNEATLKAIADNKAKRKRNCPTVTCASPYRVGQRRPLMTEMSSYRVPSPTIMETASKVIVIEIGDLPTIRSTRLISYLTSNKLQNLAHQIITAQQTGVLENVLNMTIGALLVTQPKGVTDYGNASSFKTGNFIYIRPYALSVLVQPSDGEVGKELTVQPRLVFLDKQNQRIESLGPPSEPWAISVSLEGTSDPVLKGCTQAESQDGYVSFSNLAVLISGSNWHFIFTVTSPPGANFTARSRSFTVLPAAPSEKSSIILAVSLCSVASWLALCCLVCCWFRKSKSRKIKSEDISEFKTNDQKSHIHMSSKHPRSQETKKEDTMMGEDMKIKVIMDKVNQLPHQSLNGVSRRKVSRRAVREEGSSREEDVVPAPRIISITSQGHTCVPGSPDQQIYLQEAGNWKEAQEQLVSYQLAGQDQRLLLCPDLRRERQQLQGQSQLGQEGGSVGLSQEKKASGGATQASCPHLVHPETIQEQL
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Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity). Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (By similarity). During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility. Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (By similarity). May act in collecting-duct and biliary differentiation (By similarity). May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity).
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E2RQ08
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RPN1_CANLF
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Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Ribophorin I) (RPN-I) (Ribophorin-1)
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MEVPTARLLLLLLLGAWAPAPESASPEAPLLVNEDVKRTVDLSSHLAKVTAEVVLAHPGGGSTARAASFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKVSVVVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDIPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGIASIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIQVDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETINRYKQSRDVSTLNSGKKSLETEHKALTSEIASLQSRLKTEGSDLCDKVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL
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Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
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E2RTQ7
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AURK_GIAIC
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Aurora kinase (EC 2.7.11.1) (gAK)
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MPQHLVPHTGTGKRTTIEDFEIGRFLGRGKYGLVYLAREQSSKLVVALKVLYKSYIKSERVEGQVRRELDIHLNVRHINIIRLYTWFQDETRVFLVLEVAPYGELYQRLQQFGKFPLPVVSKIIRDVAQAIQYLHRKNIFHRDLKAENILICKGKETKEHTDAHNSDDSISVHEHELVRMAHYTYKIADFGWSVHHPTHGGRRRTQCGTLDYLPPEVMLGQSYDKACDIWSLGALCYELICGTAPFYHDEIKITRQNIANVEYSFTKDFSPASKDFIQRMLIRSPEARISIEDILRHPFLRQTDHRSKVPK
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Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization.
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E2RTZ4
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HMP_GIAIC
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Flavohemoprotein (Flavohemoglobin) (FlavoHb) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)
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MTLSEDTLRAVEATAGLIAAQGIEFTRAFYERMLTKNEELKNIFNLAHQRTLRQPKALLDSLVAYALNIRRINELYELKGKGLPVPPEHWAELQGFFSAAERVANKHTSFGIQPAQYQIVGAHLLATIEDRITKDKDILAEWAKAYQFLADLFIKREEEIYAATEGCKGGWRQTRTFRVEEKTRVNEIICKFRLVPAEEGAGVVEHRPGQYLAIFVRSPEHFQHQQIRQYSIISAPNSAYYEIAVHRDEKGTVSRYLHDYVSTGDLLEVAPPYGDFFLRYLEADEQAPADTQASQEFQMLQSGAINFAAEKTMPIVLISGGIGQTPLLSMLRFLAQKEGKETARPIFWIHAAHNSRVRAFKEEVDAIRETALPSLRVVTFLSEVRATDREGEDYDFAGRINLDRISELTKLEADNANPHYFFVGPTGFMTAVEEQLKTKSVPNSRIHFEMFGPFKASH
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Flavohemoprotein involved in nitric oxide (NO) detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the protozoan parasite from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. May also be involved in O(2) detoxification.
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E2RU81
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PFP_GIAIC
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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)
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MSAFEVYRRKFKPALPRAIQGASYHLHTEEKTHPVADEQDIAALFPKTTHLPLLDIQPDTGAPKLLEPKRVGVIFSGGQAPGGHNVLCGLYDKLQQIAPKSVLLGFQNGPKGLMTNKYVELTEKFLEPFRNMGGFHAIGSGRDKIAKPEDFDAAAKTAKDNNLDIICIIGGDDSNTNACLLAEDFLKRGLKTAVIGVPKTIDRDLYSTKGIECSFGFDSSTKVYAELIGNICYDCLSAKKYWHFIRLMGRSASHITLECGLQTHANICLVGEEILSKKMTSRQLFEYLADCVTKRADSGKNYGVCLVPEGLIEFIPENNELFAYLNNTLLPHWTGELTADAVAAKLPDPLRTTFMAIPASIRTQLLLDRDPHGNIAISQIETEKFLGAGVQQVLRERGSKTKFTPLYHFFGYEGRCAAPSDFDCSLCYSLGAVAAILGCNGKTGYMASLRNLVRPPADWSPIGLPLTCLMNMEMRHGHKTPVIMKQMTDLNGNPYKLLARNRDTWLMNDDYQNPGPIQQIATESAEGTAVCARPTITLIEEARK
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Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346, ECO:0000269|PubMed:9242987}.
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E2RU97
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1433_GIAIC
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14-3-3 protein (GI-14-3-3) (g14-3-3)
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MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK
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Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts. Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation-independent binding motif. Involved in encystation. Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size.
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E3PJ86
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GSPD2_ECOH1
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Secretin GspD 2 (General secretion pathway protein D 2) (GspD) (GspD-beta secretin) (Type II secretion system protein D 2) (T2SS protein D)
|
MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR
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Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).
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E3PQQ8
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CCAP_CONVL
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ConoCAP [Cleaved into: ConoCAP-a (CCAP-vil); ConoCAP-b; ConoCAP-c]
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MVSLGHVLFVILLPVLLPVAADDPDDQMLSQISLPSSSRSEYDDNDVSKRVFCNGFTGCGGRHRDRSRRQERYGKRLIPVLAKRPFCNSFGCYNGKRSLSGAGPALSTPVDPSRNNKARTMARMLDAAASARHEQQQQLLQQREQRGLESRDPAASGDLSKRLFCNGYGGCRGGKRTLYSPWLERMNEVADDRSARNALCTRLGWRE
|
[ConoCAP-a]: In contrast to other members of the CCAP family which are cardio-accelerators, conoCAP-a decreases the heart frequency in Drosophila larvae (26%), rats and zebrafish embryos. It also reduces the blood pressure in rats. It decreases systolic calcium in ventricular cardiac myocytes, indicating that it may act via impairment of intracellular calcium trafficking. [ConoCAP-b]: Synthetic conoCAP-b decreases the heart frequency of 23% in Drosophila larvae. [ConoCAP-c]: Synthetic conoCAP-c decreases the heart frequency of 12% in Drosophila larvae.
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E3PRJ4
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KAME_ACESD
|
Lysine 5,6-aminomutase beta subunit (5,6-LAM) (EC 5.4.3.3) (D-lysine 5,6-aminomutase beta subunit) (L-beta-lysine 5,6-aminomutase beta subunit)
|
MSSGLYSMEKKEFDKVLDLERVKPYGDTMNDGKVQLSFTLPLKNNERSAEAAKQIALKMGLEEPSVVMQQSLDEEFTFFVVYGNFVQSVNYNEIHVEAVNSEILSMEETDEYIKENIGRKIVVVGASTGTDAHTVGIDAIMNMKGYAGHYGLERYEMIDAYNLGSQVANEDFIKKAVELEADVLLVSQTVTQKNVHIQNMTHLIELLEAEGLRDRFVLLCGGPRINNEIAKELGYDAGFGPGRFADDVATFAVKTLNDRMNS
|
Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
|
E3PRJ5
|
KAMD_ACESD
|
Lysine 5,6-aminomutase alpha subunit (5,6-LAM) (EC 5.4.3.3) (D-lysine 5,6-aminomutase alpha subunit) (L-beta-lysine 5,6-aminomutase alpha subunit)
|
MISVESKLNLDFNLVEKARAKAKAIAIDTQEFIEKHTTVTVERAVCRLLGIDGVDTDEVPLPNIVVDHIKENNGLNLGAAMYIANAVLNTGKTPQEIAQAISAGELDLTKLPMKDLFEVKTKALSMAKETVEKIKNNRSIRESRFEEYGDKSGPLLYVIVATGNIYEDITQAVAAAKQGADVIAVIRTTGQSLLDYVPYGATTEGFGGTYATQENFRLMREALDKVGAEVGKYIRLCNYCSGLCMPEIAAMGAIERLDVMLNDALYGILFRDINMQRTMIDQNFSRIINGFAGVIINTGEDNYLTTADAFEEAHTVLASQFINEQFALLAGLPEEQMGLGHAFEMDPELKNGFLYELSQAQMAREIFPKAPLKYMPPTKFMTGNIFKGHIQDALFNMVTIMTNQRIHLLGMLTEALHTPFMSDRALSIENAQYIFNNMESISEEIQFKEDGLIQKRAGFVLEKANELLEEIEQLGLFDTLEKGIFGGVKRPKDGGKGLNGVVSKDENYYNPFVELMLNK
|
Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively.
|
E3PY95
|
OAME_ACESD
|
D-ornithine 4,5-aminomutase subunit beta (EC 5.4.3.5) (D-ornithine aminomutase E component) (OAM-E)
|
MEKDLQLRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTPLENSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADHIMVIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRPINYHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDACESKTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGMKKSNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEASTREATVTHVLNLLISKLTRADIQSTITPDEGRNVPWHIYNIEACDTAKQALIGMDGLMDMVQLKREGVLGDTVRELKERAVLFMEEIIEAGGYFNAVEQGFFVDSGYYPERNGDGIARQINGGIGAGTVFERDEDYMAPVTAHFGYNNVKQYDEALVSEPSKLIDGCTLEVPEKIVYIDELDENDNVNVRMEETKEFRHSSMIKPEVEWQADGTVLLTMFLPTSKRVAEFAAIEFAKKMNLEEVEVINREVMQEAEGTRIELKGRVPFSIDINSLVIPPEPEILSEDEIREDIEKTPLKIVAATVGEDEHSVGLREVIDIKHGGIEKYGVEVHYLGTSVPVEKLVDAAIELKADAILASTIISHDDIHYKNMKRIHELAVEKGIRDKIMIGCGGTQVTPEVAVKQGVDAGFGRGSKGIHVATFLVKKRREMREGK
|
Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.
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E3Q1H1
|
GNA1_TRYBB
|
Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (Phosphoglucosamine acetylase) (Phosphoglucosamine transacetylase) (TbGNA1)
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MTDIVDLELRVLEESDLSSHLELLGHLTEAPPLSGVELANIADMRRRAGIVTKVFCHQPTGRIVGSASLMIQPKFTRGGRAVGHIEDVVVDPSYRGAGLGKALIMDLCEISRSKGCYKVILDSSEKSLPFYEKLGFRAHERQMRLDL
|
Involved in the biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. Catalyzes the formation of N-acetyl-D-glucosamine 6-phosphate from acetyl-coenzyme A (acetyl-CoA) and D-glucosamine 6-phosphate.
|
E3SCZ8
|
BIRC5_CAVPO
|
Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor survivin)
|
MGAPSLPRAWQLYLKEHRVSTFKNWPFVNGCSCTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNSKQKEFEETAAKVRQAMEQLAALE
|
Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (By similarity).
|
E3VNM4
|
TGA10_ARATH
|
Transcription factor TGA10 (Protein TGACG (TGA) motif-binding protein 10) (bZIP transcription factor 65) (AtbZIP65)
|
MQGHHQNHHQHLSSSSATSSHGNFMNKDGYDIGEIDPSLFLYLDGQGHHDPPSTAPSPLHHHHTTQNLAMRPPTSTLNIFPSQPMHIEPPPSSTHNTDNTRLVPAAQPSGSTRPASDPSMDLTNHSQFHQPPQGSKSIKKEGNRKGLASSDHDIPKSSDPKTLRRLAQNREAARKSRLRKKAYVQQLESCRIKLTQLEQEIQRARSQGVFFGGSLIGGDQQQGGLPIGPGNISSEAAVFDMEYARWLEEQQRLLNELRVATQEHLSENELRMFVDTCLAHYDHLINLKAMVAKTDVFHLISGAWKTPAERCFLWMGGFRPSEIIKVIVNQIEPLTEQQIVGICGLQQSTQEAEEALSQGLEALNQSLSDSIVSDSLPPASAPLPPHLSNFMSHMSLALNKLSALEGFVLQADNLRHQTIHRLNQLLTTRQEARCLLAVAEYFHRLQALSSLWLARPRQDG
|
Together with TGA9, basic leucine-zipper transcription factor required for anther development, probably via the activation of SPL expression in anthers and via the regulation of genes with functions in early and middle tapetal development. Required for signaling responses to pathogen-associated molecular patterns (PAMPs) such as flg22 that involves chloroplastic reactive oxygen species (ROS) production and subsequent expression of H(2)O(2)-responsive genes.
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E3VWI2
|
G3P2_STRAE
|
Glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH 2) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (PL-sensitive glyceraldehyde-3-phosphate dehydrogenase)
|
MTVRIGINGFGRIGRNVFRAAAARSSELEIVAVNDLGDVPTMAHLLAYDSILGRFPEEVTAEPGAIRVGDRTIKVLAERDPGALPWGDLGVDIVIESTGIFTDAAKARSHVDGGAKKVIIAAPASGEDFTVVLGVNDGDYDPERHTIISNASCTTNCLGVLAKVLHDAVGIDSGMMTTVHAYTQDQNLQDAPHKDLRRARAAALNIVPTSSGAAKAIGLVLPELAGRLDAFALRVPVPTGSVTDLTVTTRRGTSVEEVKEAYAAAASGPYKGLLSYVDAPLVSTDIVGDPASCVFDAGLTRVSGPQVKVVGWYDNEWGYSNRLIDLATLIGSSL
|
Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
|
E3W9M2
|
AA5GT_DIACA
|
Cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose) (AA5GT) (Dc AA5GT) (EC 2.4.1.299) (Acyl-glucose-dependent anthocyanin 5-O-glucosytransferase) (Beta-glucosidase like protein) (DcBGLUL)
|
MNMSCKFEIVLLVSWWLLLVLVFGVESSMFSEFDRLDFPKHFIFGASSCAYQVEGAAFEDGRTLSTFDIAAHSGHLPGNGDITSDEYHKYKEDVELMVETGLDAYRFSISWSRLIPNGRGPVNPKGLEYYNNLVNALLTKGTQPHVTLLHSDLPQALRDEYGGLFISPKFIDDFVAYADVCFREFGDRVLHWTTFNEANFLAFGDENTPASALYLSAHHLLLAHASATRLYRENYQASQRGFIGINVYAYDFIPETNTEVDVIAAKRARDFFIGWFVQPLMNGEYPLTMRKNGGPRLPKFTPNETELLTGSYDFIGLNYYTAKTVKDDPVMLTVEPRNYYTDQGLISSYLGNIDPYQGHPFFNTPWGLHDVLQQFKQVYGNPPVYIHENGEVGDHDADYDKLINDIPRVEYLQGHIRAVLDAVRNGSNVKGYFVWSFLDMYELMYGTKFTFGLYYIDFNDPKLTRHPKLSQKWYSRFLKGEKASTKASIHTPNEAETHTYFY
|
Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 5 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. Uses acyl-glucoses, but not UDP-glucose, as the glucose donor.
|
E3W9M3
|
AA7GT_DELGR
|
Cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose) (AA7GT) (Dg AA7GT) (EC 2.4.1.300) (Acyl-glucose-dependent anthocyanin 7-O-glucosytransferase) (Beta-glucosidase like protein) (DgBGLUL)
|
MCPSFLVTLLLLQLSSLVVVLVVWAEQLPEFNVRRDDFPSNFVFGAGTSALQVEGAIAEDGKTPNIWDVDSHMGHMPDKSTTDIACDSYHRYKEDVKIMSDIGLEAYRFSIAWTRILPYGRGFINPKGVEYYNNLIDTLLEHGIQPHATIYHIDHPQILEDEYGGWLSPRMIEDFTTYADVCFREFGDRVSHWTTINEPNIISLGAYDSGQIPPHRCTPPGAYNCTAGNSSVEPYKAMHHFLLAHASAVQIYRTKYQAKQKGLIGLNVYGFWCAPQTNSRADIEATKRATAFYTGWAADPLVFGDYPIIMKENVGSRLPSFTKNESELVKGSFDFIGLNHYFVFYIQDDPEEITTPISLRNFDSDMRVKASVKPGDSGDPSGLKNLLRYFKDNYGNPPVYVHENGFGSPQNETLDDDMGRIRYISGYIGSMLEAIKNGSDTRGYFVWSFMDAFEILSGYQTRYGIVHVDFDDKSLKRQLKPSAQWYSNFIKKKNTTEDEISYSSQ
|
Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 7 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color.
|
E3YBA4
|
MBCTN_METTR
|
Methanobactin mb-OB3b (Copper-binding compound) (CBC) (Hydrogen peroxide reductase) (EC 1.11.1.-) (Superoxide dismutase) (EC 1.15.1.1)
|
MTVKIAQKKVLPVIGRAAALCGSCYPCSCM
|
Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated levels of copper. Cu-mb contributes to the switchover from soluble methane monooxygenase (sMMO) to the membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO subunit A. It also stimulates the enzymatic activity of pMMO. In the absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+), Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active process, which may involve TonB-dependent transporters, and as such does not involve porins. Cu-Mb can be taken up by other methanotrophic bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like activity. Shows reductant-dependent oxidase and hydrogen peroxide reductase activities. Reduces copper-levels in liver in a rat model of Wilson disease.
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E4MYY0
|
HCS_KITSK
|
(2Z,6E)-hedycaryol synthase (HcS) (EC 4.2.3.187)
|
MAEFEIPDFYVPFPLECNPHLEEASRAMWEWIDANGLAPTERARDRMRRTGADLSGAYVWPRADLDTLTIGLKWIALTFRIDDQIDEDDTAERLPARMTAIDELRGTLHGLPVSGRSPTARALGALWQETALGRPATWCDAFIGHFEAFLQTYTTEAGLNAHGAGLRLDDYLDRRMYSVGMPWLWDLDELRLPIFLPGSVRTCGPMNKLRRAGALHIALVNDVFSVERETLVGYQHNAVTIIREAQGCSLQEAVDQVAVLVEAQLHTVLQARQELLEELDRQALPSRAREAAVDYAANVAANLSGQLVWHSSVERYAVDDLQSAADPRATPTTSSLGI
|
Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization.
|
E4NKF8
|
PUB1_MEDTR
|
U-box domain-containing protein 1 (EC 2.3.2.27) (Plant U-box protein 1) (MtPUB1) (RING-type E3 ubiquitin transferase PUB1)
|
MNDPRSKMMISPGLLPTESLLDSLILISNEVSSMQKFPLVQIKNVSSMIRRIKLLSSLFEEIQESDSPLPPSSILCFIEIFSVITRVKVLIQECTDGSSLWSLIQLDFISNQFFVLVKEMGRALDILPLNLLNVAQDIKEQVDLLHKQSKRVELELFIDPREVQRRENLFEVMSKNCLQNKKTNNNKGFIDFVKVEEIMCSIGLRTLSDYVEEISKLEVEAQNQAGTGGLIVVSNINNLMSLVSYTKSMVFRNDGESEECKPISMFLYNKSKIHDNDSSSSSSFSQSMMTVNIPDEFRCPISLDLMRDPVIVSSGHTYDRISIAEWINSGHHTCPKSGQRLIHTALIPNYALKSLVHQWCYENNVKMNEAITKNNNSSSKRHKNENAIDHISENKASKDAVKMTAEFLVGKLATGSTDIQRQSAYEIRLLAKTGMDNRRIIAEVGAIPFLVTLLVSKDSRIQEHVVTALFNLSIYDNNKILIMAAGAIDNIVEVLEFGKTMEARENAAAAIYSLSMIDDCKVQIGASSRAIPALVGLLKEGTIIGKRDAATALFNLAVYNPNKLSIVKSGAVTLLVELLMDDKAGITDDSLAVLAVLLGCSEGLEEIKNSKSLVPLLIDLLRFGSVKGKENSITLLLGLCKEEGELVAMRLLANPRSIPSLQSLAADGSLRARRKADALLRLLNRCCSQPHHSL
|
Exhibits U-box-dependent E3 ubiquitin ligase activity in vitro. Negatively modulates successive stages of infection and development of rhizobial (e.g. Sinorhizobium meliloti) and arbuscular mycorrhizal fungi (AM, e.g. Rhizophagus irregularis) symbioses, in an ubiquitin ligase activity-dependent manner. Negative regulator of the LYK3 signaling pathway leading to nitrogen-fixing symbiosis (eg. infection and nodulation) by rhizobia. May be involved in the discrimination of rhizobium strains producing variant Nod factors.
|
E4Q361
|
GH1A_CALOW
|
Multifunctional glycoside hydrolase (Multifunctional GH) (EC 3.2.1.21) (EC 3.2.1.23) (EC 3.2.1.37) (EC 3.2.1.74) (EC 3.2.1.91) (CoGH1A)
|
MSFPKGFLWGAATASYQIEGAWNEDGKGESIWDRFTHQKGNILYGHNGDVACDHYHRHEEDVSLMKELGIKAYRFSTAWARIFPDGFGNINQKGLEFYDKLINELVENGIEPVVTLYHWDLPQKLQDIGGWANPEIVNYYFEYAMLIINRYKDKVKKWITFNEPYCIAFLGHWHGIHAPGIKNFKVAMDVVHNIMLSHFKVVKAVKENNIDVEIGITLNLTPVYLQTERLGYKVSEIEREMVNLSSQLDNELFLDPVLKGSYPQKLLDYLVQKDLLDSQKVNNMQQEVKENFIFPDFLGINYYTRSVRLYDENSGWIFPIRWEHPAGEYTEMGWEVFPQGLFDLLIWIKESYPQIPIYITENGAAYNDKVEDGRVHDQKRVEYLKQHFEAARKAIKNGVDLRGYFVWSLIDNFEWAMGYTKRFGIIYVDYETQKRIKKDSFYFYQQYIKENS
|
Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p-nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.
|
E4QP00
|
HMFO_METS6
|
5-(hydroxymethyl)furfural oxidase (EC 1.1.3.47) (5-hydroxymethylfurfural oxidase) (HMFO) (Thiol oxidase) (EC 1.8.3.-)
|
MTDTIFDYVIVGGGTAGSVLANRLSARPENRVLLIEAGIDTPENNIPPEIHDGLRPWLPRLSGDKFFWPNLTIHRAAEHPGITREPQFYEQGRLLGGGSSVNMVVSNRGLPRDYDEWQALGADGWDWQGVLPYFIKTERDADYGDDPLHGNAGPIPIGRVDSRHWSDFTVAATQALEAAGLPNIHDQNARFDDGYFPPAFTLKGEERFSAARGYLDASVRVRPNLSLWTESRVLKLLTTGNAITGVSVLRGRETLQVQAREVILTAGALQSPAILLRTGIGPAADLHALGIPVLADRPGVGRNLWEHSSIGVVAPLTEQARADASTGKAGSRHQLGIRASSGVDPATPSDLFLHIGADPVSGLASAVFWVNKPSSTGWLKLKDADPFSYPDVDFNLLSDPRDLGRLKAGLRLITHYFAAPSLAKYGLALALSRFAAPQPGGPLLNDLLQDEAALERYLRTNVGGVWHASGTARIGRADDSQAVVDKAGRVYGVTGLRVADASIMPTVPTANTNLPTLMLAEKIADAILTQA
|
Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation. To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls.
|
E4TN31
|
TM175_MARTH
|
Potassium channel Ftrac_2467 (Transmembrane protein 175) (MtTMEM175)
|
MRKVFETVVGLNPNFSFRGKQQTRIETFSDAVFALAITLLVLSSTIPETFEDLWASMRDVIPFAICVALIIVIWYQHYIFFLKYGLQDKVTILLNTILLFVLLVYVYPLKFLARFLSEIYGGIFGIIETDLSRFGEYSHQNLKLLMVNYGLGAFAIFLVFSLMYWRAYKMKSLLDLNSYEIFDTKSSIIANLLMCSVPLLSLIITLIDPWGNFRTTILSGFLYFLYVPIMIVFGRITSKKSRRLLQD
|
Potassium channel forms a potassium-permeable leak-like channel with weak selectivity for potassium. The channel is permeable for K(+), Rb(+) and Cs(+).
|
E5D3Z8
|
A31_LOXLA
|
Dermonecrotic toxin (EC 4.6.1.-) (Phospholipase D isoform 1) (LlPLD1) (PLD1) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
|
MYVHLALILGCWTVVLQGAETDVGERADNRRPIWNLAHMVNAVKQIPTFLDLGANALEADVTFKGSVPTYTYHGTPCDFGRDCIRWEYFNVFLKTLREYTTPGNAKYRDGFILFVLDLKTGSLSNDQVRPAGENVAKELLQNYWNNGNNGGRAYVVLSLPDIGHYEFVRGFKEVLKKEGHEDLLEKVGYDFSGPYLPSLPTLDATHEAYKKAGVDGHIWLSDGLTNFSPLGDMARLKEAIKSRDSANGFINKIYYWSVDKYSTTRTALDVGVDGIMTNYPNVLIDVLNEDGYKDNYRLATYDDNPWETYKK
|
Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Shows complement-dependent hemolysis. Also induces dermonecrosis, vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
|
E5KGE0
|
BRIZ1_ARATH
|
BRAP2 RING ZnF UBP domain-containing protein 1 (EC 2.3.2.27)
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MFILRVHSVDSERPISVEEEESGFTYASKRAQPPLKLIQPSLKLTDRKGLIHLYRKSSHSSLPNPSSRSTTLFIVAVPNYLSSLDFIRFCDSRISQVSDILFIRNDGMEDRYSVLITFSDQSEADGFYNNLNGKKFAPSEAEVCHILYVMSVEHTEFDEVAAEAPTGFTELPTCPICLERLDPDTSGIVSTLCDHSFQCSCTSKWTYLSCQVCRLCQQQDEILNCSICGKTENVWACLVCGFVGCGRYKEGHSIRHWKETHHCYSLDLRTQQIWDYVGDSYVHRLNHSKIDGKSVEMSTSCLSHQGDCGLCECSEDTGISGAIFNSKVDSIVIEYNDLLASQLKGQRQYYESLIVEARSKQESSIAEAVEQIVVNTMQELQNKIEKCEEEKSGITEVNTKLIKEQDTWRKKAKEIEEREAALLGSKDEMITDLQEQIRDITVFIEAKKTLKKMSSDTDGIREGTVLPVPISPEPVSSVRRQKKSNRRK
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RING-type ubiquitin E3 ligase required for seed germination and post-germination growth.
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E5KIB6
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CYPA_STRSQ
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Cypemycin
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MRSEMTLTSTNSAEALAAQDFANTVLSAAAPGFHADCETPAMATPATPTVAQFVIQGSTICLVC
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Antibiotic peptide structurally related to lantibiotics. Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against mouse P388 leukemia cells (IC(50)=1.3 ug/ml).
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E5RQA1
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GHD7_ORYSJ
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Transcription factor GHD7 (Protein GRAIN NUMBER PLANT HEIGHT AND HEADING DATE 7)
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MSMGPAAGEGCGLCGADGGGCCSRHRHDDDGFPFVFPPSACQGIGAPAPPVHEFQFFGNDGGGDDGESVAWLFDDYPPPSPVAAAAGMHHRQPPYDGVVAPPSLFRRNTGAGGLTFDVSLGERPDLDAGLGLGGGGGRHAEAAASATIMSYCGSTFTDAASSMPKEMVAAMADDGESLNPNTVVGAMVEREAKLMRYKEKRKKRCYEKQIRYASRKAYAEMRPRVRGRFAKEPDQEAVAPPSTYVDPSRLELGQWFR
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Probable transcription factor involved in the regulation of flowering time under long day (LD) conditions. Plays a major role as repressor of flowering. Controls flowering time by negatively regulating the expression of EHD1 and HD3A.
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E5XP76
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CAR_SEGRC
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Carboxylic acid reductase (CAR) (EC 1.2.1.-) (ATP/NADPH-dependent carboxylic acid reductase)
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MTESQSYETRQARPAGQSLAERVARLVAIDPQAAAAVPDKAVAERATQQGLRLAQRIEAFLSGYGDRPALAQRAFEITKDPITGRAVATLLPKFETVSYRELLERSHAIASELANHAEAPVKAGEFIATIGFTSTDYTSLDIAGVLLGLTSVPLQTGATTDTLKAIAEETAPAVFGASVEHLDNAVTTALATPSVRRLLVFDYRQGVDEDREAVEAARSRLAEAGSAVLVDTLDEVIARGRALPRVALPPATDAGDDSLSLLIYTSGSTGTPKGAMYPERNVAQFWGGIWHNAFDDGDSAPDVPDIMVNFMPLSHVAGRIGLMGTLSSGGTTYFIAKSDLSTFFEDYSLARPTKLFFVPRICEMIYQHYQSELDRIGAADGSPQAEAIKTELREKLLGGRVLTAGSGSAPMSPELTAFIESVLQVHLVDGYGSTEAGPVWRDRKLVKPPVTEHKLIDVPELGYFSTDSPYPRGELAIKTQTILPGYYKRPETTAEVFDEDGFYLTGDVVAEVAPEEFVYVDRRKNVLKLSQGEFVALSKLEAAYGTSPLVRQISVYGSSQRSYLLAVVVPTPEALAKYGDGEAVKSALGDSLQKIAREEGLQSYEVPRDFIIETDPFTIENGILSDAGKTLRPKVKARYGERLEALYAQLAETQAGELRSIRVGAGERPVIETVQRAAAALLGASAAEVDPEAHFSDLGGDSLSALTYSNFLHEIFQVEVPVSVIVSAANNLRSVAAHIEKERSSGSDRPTFASVHGAGATTIRASDLKLEKFLDAQTLAAAPSLPRPASEVRTVLLTGSNGWLGRFLALAWLERLVPQGGKVVVIVRGKDDKAAKARLDSVFESGDPALLAHYEDLADKGLEVLAGDFSDADLGLRKADWDRLADEVDLIVHSGALVNHVLPYSQLFGPNVVGTAEVAKLALTKRLKPVTYLSTVAVAVGVEPSAFEEDGDIRDVSAVRSIDEGYANGYGNSKWAGEVLLREAYEHAGLPVRVFRSDMILAHRKYTGQLNVPDQFTRLILSLLATGIAPKSFYQLDATGGRQRAHYDGIPVDFTAEAITTLGLAGSDGYHSFDVFNPHHDGVGLDEFVDWLVEAGHPISRVDDYAEWLSRFETSLRGLPEAQRQHSVLPLLHAFAQPAPAIDGSPFQTKNFQSSVQEAKVGAEHDIPHLDKALIVKYAEDIKQLGLL
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Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. Catalyzes the reduction of a very wide range of carboxylic acids, including benzoic acids, heterocyclic, phenylacetic, phenylpropanoic and fatty acid substrates.
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E6LHV7
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CAS10_ENTI1
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CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (EiCas10)
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MNKKLELMYGSLLHDIGKIVYRSNSVDFAKGTHSKIGSQFLNKFKPFQLSGIVDSVSYHHYKELASSSLLDDSVAYITYIADNIASGTDRRASEGDYEGEGNRQRFDKRAPLASIFNVVNSETKGLANYTYSFEKEQVYRYPTDAKKEYTSSQYAALVNKMTDDLSNKLKVGPDSFSSLLQWTESLWSYIPSSTDTNQVMDVSLYDHSKITCAIASCIYDYLTEMNCVNYRKELFSPYEKTKQFYQEDVFLLVSLDMSGIQDFIYNISGSKALKSLRSRSFYLETMLESLVDDLLSDLELSRANLLYTGGGHAYLLLPNTERARDVLASFEGEMKEWFIKIFKTDLSVAIAYKACTGEDLMNSNGTYSDLWQTVSRKLSDKKAHKYSLNEIKLFNSTIHAGTQECKECLRSDIDISEDSLCKICEGIIAISNDLRDYSFFVVSPEGKVPLPRNRYLSVENQDGAERKIKMNKETRIYSKNQPFVGKQLVTNLWMCDYDFSTLNPETKKQGIASYVNREVGIPRLGVLRADIDNLGTTFIKGIPEQYRSISRTATLSRQLSMFFKFELSNILKGARISVIYSGGDDLFLIGAWDDVISKALVLRKAFTRFSAGKLTFSAGIGMYPVKYPISKMASETGVLEDLAKRGEKNQVALWNDSKVFGWSQLEEQILKEKMIPLQEALTNSQEHGKSFLYKMLELLRNEDQINIARLAYLLARSSLSEELTQSIFAWSQNKQQKVELITAIEYLVYQIREAD
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CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host the appropriately targeted Csm effector complex prevents growth of dsDNA phage phiNM1-gamma6. ssDNase activity is stimulated in the ternary Csm effector complex binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases. When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing (mostly) cyclic hexaadenylate (cA6). cA6 synthesis occurs in the Csm effector complex and requires cognate target RNA and ATP other NTPs are not incorporated. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids.
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E6MVD9
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NALP_NEIMH
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Neisserial autotransporter lipoprotein NalP (Autotransporter NalP) (NalP) (EC 3.4.21.-) [Cleaved into: NalP passenger domain; NalP translocator]
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MRTTPTFPTKTFKPTAMALAVATTLSACLGGGGGGTSAPDFNAGGTGIGSNSRATTAKSAAVSYAGIKNEMCKDRSMLCAGRDDVAVTDRDAKINRPPPPNLHTGDFPNPNDAYKNLINLKPAIEAGYTGRGVEVGIVDTGESVGSISFPELYGRKEHGYNENYKNYTAYMRKEAPEDGGGKDIEASFDDEAVIETEAKPTDIRHVKEIGHIDLVSHIIGGRSVDGRPAGGIAPDATLHIMNTNDGTKNEMMVAAIRNAWVKLGERGVRIVNNSFGTTSRAGTADLFQIANSEEQYRQALLDYSGGDKTDEGIRLMQQSDYGNLSYHIRNKNMLFIFSTGNDAQAQPNTYALLPFYEKDAQKGIITVAGVDRSGEKFKREMYGEPGTEPLEYGSNHCGITAMWCLSAPYEASVRFTRTNPIQIAGTSFSAPIVTGTAALLLQKYPWMSNDNLRTTLLTTAQDIGAVGVDSKFGWGLLDAGKAMNGPASFPFGDFTADTKGTSDIAYSFRNDISGTGGLIKKGGSQLQLHGNNTYTGKTIIEGGSLVLYGNNKSDMRVETKGALIYNGAASGGSLNSDGIVYLADTDQSGANETVHIKGSLQLDGKGTLYTRLGKLLKVDGTAIIGGKLYMSARGKGAGYLNSTGRRVPFLSAAKIGQDYSFFTNIETDGGLLASLDSVEKTAGSEGDTLSYYVRRGNAARTASAAAHSAPAGLKHAVEQGGSNLENLMVELDASESSATPETVETAAADRTDMPGIRPYGATFRAAAAVQHANAADGVRIFNSLAATVYADSTAAHADMQGRRLKAVSDGLDHNGTGLRVIAQTQQDGGTWEQGGVEGKMRGSTQTVGIAAKTGENTTAAATLGMGRSTWSENSANAKTDSISLFAGIRHDAGDIGYLKGLFSYGRYKNSISRSTGADEHAEGSVNGTLMQLGALGGVNVPFAATGDLTVEGGLRYDLLKQDAFAEKGSALGWSGNSLTEGTLVGLAGLKLSQPLSDKAVLFATAGVERDLNGRDYTVTGGFTGATAATGKTGARNMPHTRLVAGLGADVEFGNGWNGLARYSYAGSKQYGNHSGRVGVGYRF
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Major human immunogenic protein. Autotransporter with a secreted protease domain involved in processing other autotransporter proteins including App and IgA. Probably autoprocesses to release the about 70 kDa passenger domain. Processes the lactoferrin receptor lipoprotein subunit (LbpB) extracellularly, releasing it from the cell surface. LbpB release protects bacteria against complement-mediated killing by anti-LbpB antibodies. Processes NHBA. Lipidation slows its auto-processing, probably allowing it to act on endogenous substrates on the cell suface before the passenger domain is released into the medium. The C-terminal beta-barrel domain inserts into the outer membrane where it probably exports the N-terminal passenger domain. Both the cell surface protein (Neisserial autotransporter lipoprotein NalP) and the passenger domain cleave human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal (By similarity). Plays a role in extracellular-DNA (eDNA) mediated biofilm formation. In some strains (including cc32 strain H44/76 but not cc11 strain B16B6) eDNA stimulates biofilm formation. When NalP is not expressed (and no longer processes NHBA or IgA) biofilm formation increases. This is probably because the number of positively charged, DNA-binding peptides on the cell surface rises, resulting in increased biofilm formation (Probable). [NalP passenger domain]: Cleaves human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal. Does not act on mouse or rabbit C3. Cleavage causes C3b degradation by human CFI and CFH, decreases deposition of C3b on the bacteria surface and probably facilitates complement escape.
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E6Y2X0
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PILR2_LINUS
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Bifunctional pinoresinol-lariciresinol reductase 2 (PLR-Lu2) ((+)-lariciresinol reductase) (EC 1.23.1.2) ((+)-pinoresinol reductase) (EC 1.23.1.1)
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MAAGFLFHMGSLPAIATVGHKSKVLVIGGTGYLGKRLVTASLAAGHETYVLQRPEIGVDIEKIQLLLSFKKAGASLVSGSFNDYRSLVDAVKLVDVVICAVSGVHIRSHQILLQLKLVDAIKEAGNVKRFLPSEFGTDPATMENAMEPGRVTFDDKMVVRKAIEEAGIPFTYISANCFAGYFLGGLCQPGFILPSREQVTLLGDGNQKAVYVDEDDIARYTIKMIDDPRTLNKTVYIKPPKNVLSQREVVGIWEKYIGKELKKTTLSVEEFLAMMKEQDYAEQVGLTHYYHVCYEGCLTNFEIGDEAGEATKLYPEVGYTTVVEYMKRYV
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Reductase involved in lignan biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
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E6Y5X0
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UREA2_CANEN
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Urease 2 (EC 3.5.1.5) (Jaburetox) (Jack bean urease II) (Urea amidohydrolase)
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MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVIRDGMGQSSGHPPAMSLDTVITSAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFPNMIIGVNTEVICGEGLIVTAGGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF
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Urea hydrolase involved in recycling metabolically derived urea generated internally or externally (By similarity). Is able to impair growth of the phytopathogenic fungus Penicillium herguei, and shows entomotoxic activity by inhibiting diuresis in Malpighian tubules isolated from Rhodnius prolixus.
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E6Z0R3
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VBHT_BARSR
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Protein adenylyltransferase VbhT (EC 2.7.7.108) (AMPylator VbhT) (Toxin VbhT)
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MRKYEGSNDPYTDPETGVMYNLLGIKDQARLERVESAFAYIRSFELGRTSISGKFDLDHMKKIHKKLFGDVYEWAGKTRLVDIVKDNSKFAHYTQIESYAPQITQQLAREQHLRGLDANEFSQRAGYYMGELNALHPFREGNGRTLREFIWQLAREAGYHIDWDRVERQEMTRASIESYYGNSDLMSALIRRNLTEFTVNRRVDVSQGINERVLSHIDIDKEWPQKGFNIAIQTTQQAPYLSSYTDTSNLEEKAQNALRNEQSYVDTFKELNDHLKTIYKDPQAAALKIEQTILAGKGDKLPDILAKAPNKVGELRGSDRLIDKLKSAGKERKAALYNVPLAISTIRRLQSFYKNSYEKHMDKLTREREQLKVEVPSLSQEAVAYMKNVEVGRNNYSKIPENINKEFVQLESALNRRFGKDVIYKRNFNLSKEIASKQTYDKKLVNELQTAIKFLQQRHIQKQNNLAITRTPSKGITR
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Toxic component of type II toxin-antitoxin (TA) system VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells.
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E7CLP2
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SX12F_RHOJU
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Putative beta-neurotoxin RjAa12f
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MKILIFIIASFMLIGVECKEGYPMGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTNLPEDAQVWDSSTNKCGG
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Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to insects (A.domestica). It is not toxic to mice and does not affect mammal F11 sodium channels.
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E7EAU8
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GCY9_CAEEL
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Receptor-type guanylate cyclase gcy-9 (EC 4.6.1.2)
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MRLYLFFISSLLLAESRRSISKISHDEINQHVKTTLSSEGIVRIGHLHPTNPIIAHEPDVLKMCADDLKMRNILPQNYTLTVFTMESCNKYSGVEHAAFLHYLKNASVYFGPGCNNEMLVIGRLAPRWNVPIIAHMSGDDALSDRVQFPTLGSVALTSASEMAKATVTYLNLNNWDQIGIVRPSVGYERLSVYSLQHQIKKRDINLNVILDIEPFSSPEEIISTGKLTTLKSMARIIVVELGMDIHSVTNFMLAIHRSEIKNEEFVFVIPWLAHQNDHYPWEAANVDKQEVKLAFENTIIITAHGYDKKFFDDFQMKFSAVTGVLANHYATLSYMSLYDALFLYGLALRDAFEDGGGYNVHMNGSLIWSRMTNRQFIGMTGQVLMNNKAIRVPSYATYHAINGTLKIVVELEAKNNDRGQCEKNEEMCSEHVAHETIQYYWPSDSGKLPPAVPKCGFTGAECDYRPYFIGASLLAFILTVGPLSYFIYLKQKERLLYDMTWRIPRESIKMLEGKSKSEHSLASKSQSSGSFSGSMNSKQNGLIAAKQAVSNGVKLAIKRYQQVRNITFPKSELRLLKELKICENDNLNKFYGISFNQQNEFIVMWVLCSRGSLEDILFNDELKLGRNFQVSFAKDVVKGLNFLHTSPLLHHGMLCLQNCLVDSNWTVKLTNFATEAVIFEKLDHNELRPFINTDSESADDVSDPTKDFARKKYLQQAPEIIREIVTTKTIPEGSQSADIYALGMVLYQILFRVEPFHERNKSINKLMETLAMANDDDQLIRPTFPSSNTGEGYNLQLLSCIEACWLEIPEMRPPIKKVRTMVNANLKSTGKGSLVDQMMKMMEEYTANLENMVRDRTALLEEAQKQADRLLNSMLPKSIAEDLKIGKPVLPQLYSCATVLFSDIRGFTRISSTSTPLQVVTFLNDMFSGFDAIIAKHDAYKVETIGDAYMIVSGVPTENGNSHAQNIADVALKMRAFICNFKLAHRPEELMMVRIGFHSGPVAAGVVGLAAPRYCLFGDTVNTASRMESTGVANKIQISEGAYNLLHCFFPQFQMVERGKIEVKGKGECLTYYLEGRTGKQ
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Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Involved in the sensing of CO2 levels and acidity by the BAG neurons. May act as a direct receptor for CO2 and H+.
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E7EM37
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DOPR2_CAEEL
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Dopamine receptor 2 (Dopamine D2-like receptor dop-2)
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MEAGETWNVSLEWPPPSLDLSTITQTPSTIVGSGIPLNYAGLSLIVIPLITLLGNLLVIISVLRYRALQSAINFLILGLAVADLLVAIIVMPYAVYVYVTNGDWYLGNLMCDIYMASDVCCSTASILLLAVISFDRYRAVSLPIQYSRQSQNVKRVWTLIAVIWLVSLTLASPMVFGVNVRPPDANPYECRFYNAEFSILSSMISFVIPCFLVLFVYIRIIIALKKREKAAKMRREKNTIAHGLTMRPDTGEEQVDEEAAGRIVAGPVVNVMMAALPSMTRRMRQFERHRRAIELAGDEEWEEDELDVMDECCGGDDAGDDDDDYHADNGQGVVEASAPRTTSMLRRIINAASVGTANSTAQSVASASGMPAFFAQNISTTSPSSSSCARTTTTTSAIPKASGDLPLPMLLNEREFGNSSTPRSSLESLSENVNVITNDFVSENCTTFSRRSSYADDSQPTSSQTSSGDGRSYSIKGQKRFRNLSRNYSTKHHRKVVKVNRGNSRNNSRTASITNQSDDALIPAIIRTISRKSPRLFRRDKTDIKKHSMILANPITEPPKEYRRVSMPIHPTNSQTETETISASRDIENLPTTTISRSTTANSAELLGSPDDFEKFPALITETVLEDVLAETREGCFMQPTVSFALTVREMEGNALNNLKGCSVESSRRVSQVDPPLAIQILTRPSLPHLDLQRMDSIGTTCSSKTRADSLRSVDSKGSKKSNRNGIAVKLVKRAIKHEHSLKRKVSKAQRKEKRATKTLGVVVGVFLVCWVPFFVINILNAVCILLNKDSCQVGYDLFFYCTWIGYMNSFMNPIIYTIFNTEFRRAFKSIIFGRNSTRHHFSNKQAHV
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G-protein coupled receptor which binds to the neurotransmitter dopamine with high affinity leading to the activation of an associated G-protein and downstream signaling pathways. Couples to G-proteins to inhibit adenylate cyclase (AC) activity and cAMP production. Inhibits synaptic vesicle fusion to negatively regulate the release of dopamine at dopaminergic neuron synapses. Antagonizes octopamine signaling in response to food by promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons. This is most likely in association with the G(o)-alpha G-protein subunit goa-1. In association with the G-alpha protein gpa-14, modulates two types of learning behavior: touch habituation and chemosensory associative conditioning. May act partly via tsp-17 to negatively regulate dopamine reuptake transporter dat-1 activity. Plays a role in behavioral plasticity and regulates the decision-making process when conflicting alternatives are present. Promotes male mating behavior by antagonizing acetylcholine signaling to control the protrusions of copulatory spicules from the tail of males during hermaphrodite vulval location. Modulates unc-7 activity at gap junctions to promote inhibitory neuronal signaling transduction between chemosensory and mechanosensory neurons, and thus ensures spicule insertion attempts are confined to the hermaphrodite vulva during copulation.
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E7EZF3
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UHRF1_DANRE
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E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
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MWIQVRTMDGKETHRVDSLSKLTKVDELRVKIAELFNVEPERQRLFYRGKQMEDGHTIFDYNVGLNDIVQLLVRQAVAATVLPKDKEAELSDSDSGCGSAQSESDKGSTHGESDVQSAGASGQTDTADLIDPGFGFYKINEFVDARDLNMGAWFEAQIVKVTKTPAEDGGAEDIVYHVKYEDYPENGVVQLRGKDVRPRARTVYQWHQLEPGMIVMVNYNPDDPKERGYWYDAEIQRKRETRTQREVFGKILLGDAGDSLNDCRIMFVTEIYKIEEPGSAEGPGASSDSPLKKGSNGPECKVCKDDPKKNCRVCNCHVCGIKQDPDKQLLCDECDMAFHTYCLNPPLTTIPDDEDWYCPDCRNDASEVVLAGEKLKESKKKAKMASASSSSQRDWGKGMACVGRTKQCTIVPSNHYGPVPGVPVGTLWKFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDDGNEFTYTGSGGRDLSGNKRTAEQSCDQKLTNMNRALALNCNAAVNDKEGAEAKDWKAGKPVRVVRSSKGRKHSKYSPEDGNRYDGIYKVVKYWPEKGKSGFLVWRYLLKRNDEESAPWTRDGKERIKKLGLTMQYPEGYLEAVAAKEKEKENKNEDDIEETPTKGKRKRKSQSMEEKSSPTKGTPKKMKVEAYKLSKEQKALIKDDELNKKLWDEAMESLSLGPRFVNKVEEVFLCICCQEVVYQPITTECQHNVCRECLQRSFKAKVYTCPACRHDLGKNYQMAVNKPLQAILTQLFPGYSSGRC
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Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits dnmt1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins. However, it is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo (By similarity). Required for pregastrula and lens development. {ECO:0000250, ECO:0000269|PubMed:21126517}.
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E7EZG2
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MY9AA_DANRE
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Unconventional myosin-IXAa (Myosin IXAa)
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MSVHDVGGRRRFEDSELTLRIYPGIIAEGTIYCPVAARKITSAAEVIEQVIDRLQLDRTKCYVLAEVKEFGGEEWILNPTDYPVQRMMLWPRMALENRFSSEDYRFLLREKNLDGSIHYGNLQMWLQVTEERRRMVERGFLPQPLPKDFDDLCNLPDLNEKTLLDNLRSRFKQEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQSRQNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGTSEEERTAFHLKKPEEYHYLNQMTKKPHRPHWGNYYENEPDCFTVEGEDLKHDFERLQLAMEMVGFLPTTRKQIFSLLSAILHLGNIRYKKKIYRDDSIDICNPEVLPVVSELLEVKEEMLFEALTTRKTVTVGEKLIVPYKLAEAGTVRDSMAKSLYSALFDWIVFRINHALLNQRDLEESAKILSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRAEGITWHNIDYIDNTSCITLISKKPTALLHLLDEECNFPQATNQTLLDKFKRQHEGNSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLKSSKNAFICGLIGIDPVATFRWAVLRAYFRAMVAFRDAGKRHVEKRSGHDAAAPAVKSVDSFSFLHHPVHQRSLEILQRCKEEKYSVNRRNPRTPLSDLQGSNAINQREGWNGRPGRQNRLSSFGSFSEEEGIFINSTSSKLLERAHGILMRNKNYKMKPSLPKHLLDVKSLKYLSNLTLQDRITKSLLHLHKKKKPPSISAQFQASLNKLMETLGQSQPYFVKCIRSNSEKLPLRFNDSLVLRQLRYTGMLETVRIRQSGYSIKYTFQDFARHFHVLLPEGSNQASQEAIRQYLQQVDLTPEGFQVGRTMVFLREIERQRLQDLLHKEVLSRIVYLQRRFRALLERKNFLRVRQAACQIQNWWRSCQSLQRDSQLEYDMRVQEGAVVCIQSAWRGFRERRRLLLWREASVLIQRTWRLYRQRRAALQIQTAWRRHRARELFLRQRDATIRLQAVGRGYLARQRFRELQKQRLKITHLPNGKASLLTEEDKLEDMGLDASMLEDSFEEQDRSKQALSSAVEASGAGVLEEMEVEMMEGMAPAQPSPEVTIRERPRTLEDPNQRTRAKRESRRMRELEQAKFSLELLKVRSTGGTSPSDERRWSMELVSEIAHTPQGTPDSQSSKGSFELLNIDDYFKDKAPCAEPEDLGSPSSVPDQHNVLPSDTSTPDILSKPDDQSKPPRMQYSLPTFYTPPSESSSLVIKSTTNSVTPCPDGLSKPSKDKKESTRRPMVVVISMQKETLLNEADVKPLEVKDSAAQTSEPPSPAQPSTDSSYVLEKLEKLNEEKEERQKHQRQQNEKEMMEQIRQQTHILEEQRRNLVQNEREKLEKQRAETLRRIEQSRQESSGGRTDRPAPIAQPEPDLTSQRPAREKDGAPLILRDRPKDAQNLAEGWAPKLTLESRGDEARSRINKKPSNQNVNISMSERPGNIFFSPKTKIAYSKLNKDLANQEKTPGAQNEVSLLGYKSTKTEVGRPGHKKARMARTRSDFLTRSSSTQGEGESEEEEYDETPLYAGTPLPKQDSEESAVEACHSDSEMLTTAAEEQKNRCKTLPSGELGKHDTRKNSHGDGRVRGKMRFWGKAKNAEKKSSRERLLCGSDTLEGDYTEATLLMEEGVERLSPPHSPDLTLQREFKENKEPSPKVKRRRSVKISSVALEPVQWQNDALQILTCTSDYKSMNDFLMKKITDLDTEDGKKDTMVDVVFKKALKEFRVNIFNSYSTALAMDDGKSIRYKDLYALFEQILEKNMRQEQRDWSESPVKVWVNTFKVFLDEFMTEHKPLDSSLGKAPKPDRKKRRKKDTDVVEEHNGHIFKSTQYSIPTYCEYCSSLIWMMDKACVCKLCRYACHRKCCQKMTTKCSKKYDPELSSRQFGVELSRLTNDERTVPLVVEKLVNYIEMHGLYTEGIYRKSGSTNKIKELKQGLDTDVNGVNLDDYNINVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQDKKEVIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRCPDTIDPLRSVQDIGKTTACVELIICEQMNKYRARLKDINTLEFAENKAKSRLTFIRRSMGKGPVHRLRYRTPSPPTSPRSPTAPEVMQDSGEEEPGRDPEVSEQQQVAMQQEEKVLTEQIESLQKEKEELTFEMLALEPRASDDETLESEASIGTADSSENLNVDSEGATSDYSERGPALAATRPKKSEGKSRRVLRKQPESLDSIDSCSTVSSVSSSYMQPTSRTHKLSLRSKSPSKRLYLSSPSESLDQPEQDGEERPQFTSRGTFNPEKGKQRLQGAKSSPQRHREQKKDPELSPQQVVVYGSNEFMV
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons (By similarity). Required for the regulation of neurite branching and motor neuron axon guidance.
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E7F1H9
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YTHD2_DANRE
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YTH domain-containing family protein 2
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MSASSLLEQRPKGQANKVQNGAVTQKDTLNDDEFEPYLNAQPRQSNAYTAMSDSYMPSYYSPSIGFTYSLNEAAWSTGGDPPMPYLASYGQLSNGEHHFLPDAMFGQSGALGNNPFLGQHGFNFFPSGIDFPAWGNSSSQGQSTQSSGYSSSYAYAPSTLGGAMIDGQSPFAANEPLNKAVGMNSLDQGMAGLKIGAGDMAPKVVGSGLPGGPLSQVSTAPTMPPASMAPAKTASWADIASKPAKPQPKLKTKGGLGGTNLPPPPIKHNMDIGTWDNKGNMPKPAAPQQTSLPTNGQPPNQSSPQPGATAGGVPQLPLSNGQLVPPTGQLVQHPLPPGGQPGAVPPQLSQGPPASQPSQPTRWVPPRNRANGFGDAAGGPGQSPPNSGMGGITVPAEPHPVLEKLRMVNNYNPKDFDWNPKHGRVFIIKSYSEDDIHRSIKYNIWCSTEHGNKRLDAAYRSLANKGPLYLLFSVNGSGHFCGVAEMRSPVDYNTCAGVWSQDKWKGRFDVRWIFVKDVPNSQLRHIRLENNENKPVTNSRDTQEVPLDKARQVLKIIASYKHTTSIFDDFSHYEKRQEEEESVKKVEVQGSDPYSNNSSRSHYRMQDRQGRVK
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Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (By similarity). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs (By similarity). The YTHDF paralogs (ythdf1, ythdf2 and ythdf3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (By similarity). Plays a key role in maternal-to-zygotic transition during early embryonic development, the process during which maternally inherited mRNAs are degraded: acts by binding m6A-containing maternal mRNAs and promoting their degradation. More than one-third of maternal mRNAs can be modified by m6A. Binding to m6A-containing mRNAs results in mRNA degradation (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A-containing mRNAs, such as notch1a, and promote their degradation. The decreased Notch signaling following notch1a degradation promotes endothelial to hematopoietic transition. Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (By similarity). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (By similarity).
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E7F3F0
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MY9AB_DANRE
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Unconventional myosin-IXAb (Myosin IXAb)
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IMSCHDVGGRRRFEDSEFTLRVYPGSLSESTIYCPVSARKVTTAAEVIERVIERLQLDRTRLYVLAEVKEFGGEEWILNPSDCPAQRMMLWPRMALENRLLGEDYRFLLREKNLDGSIHYGSLQMWLRVTEERRRMVERGLLPQPPAAQFVADLCSLPDLNEHTMLENLRGRFRQENIYTYVGSILIAVNPFKFLPIYNPKYVKMYDKHRLGQLEPHIFAVADAAYHAMLQRHRNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQESGTVRGAYVEKYLLEKSRLVYQEHNERCSCVNIFSKLVCHELKVCVCMCVQDCFSVEAEDLKHDFERLQLAMEMVGFLPTTRKQIFSLLSAILHLGNIRYKKKTFRDDSIDICNPEVLPIVSELLEVKEEMLFEALTTRKTVTVGERLIVPYKLAEVRKGTSHQLIQTFRTSHSLLHQRYFHIHTSPTRILSIGVLDIFGFEDYENNSFEQFCINFANETLQHYFNQHVFKLEQEEYRSEGINWHMIDYIDNTACINLISKKPTALLHLLDEECNFPQASNQTLLDKFKRQHEGNAYMEFPAVMEPAFIIRHYAGKVKYSVKDFREKNTDHLRPDIVSLLKSSRKAFICGLMGLDPVASFRWAVIRAFFRALVAFRHAGLQHRDNRSSSDVHLQPQKSVDSFSFLHHPVHQRSLEILQRCKDDRYNSCVSRRSPRTPLSDLQGANTFSSNGRGWRSERVSSFAHEDEGIFVNSVNNRLLERAQGILMRNKNYKPKPSLPKHLLDVKSLKYLSSLTLHDRITKSLLHLHKKKKPPSISAQFNVSLNKLMETLGQSEPYFVKCIRSNAEKLPLRFNDALVLRQLRYTGMLETVRIRQSGYSVKYSFKDFAHHFHVLLPAGFSASQMGIREFLRSADLEPSGYQVGRSMVFLHERLRQRLQDELHQEVLRRIVCLQRSFRTQRDRKHFCRQRRAARLIQRWWRSCISQADGSVCALELQQGAALRLQAVWRGFRARRLYLQQRRAVLIIQRCWRRVLNTRNTAATLIQAVWRTRTHRRSFLQQRRAAVTLQAACRGQQSRQRCRILREQQCREQSKHPSTVTKSLHQNTEEAEKLEEVWEKQTTDPPPKAVDDSTLKSRNKRESRRQRELEQATFSLELLKVRSGSNTEDAQIPPSKHHPPHQASTDSQESFELLENEDSASAKLELSKSEPMEVNQTSPAASFKPHFYIPDEDGSPINSAPQTPNRAKQIREKKESVVVIISMQKENPVDRSSLQTLEAQDVPLSNGESASDCSIIPEPRTNHELDTGSSFSVSSKPLQLDLRSAASNEEPSEPKADVQKKFVSQSISISMKETAANVAFPPKRSRLTFSKSDKDLVNQERSLAIQREAGFRSLKNRDVTRAGCKKKARMARTRSDFLSRACSTEADCEEDEDDEYEDTPVLSCTRPPHSPSSPDIDCVFHSDSEMSSQKEQKRIQKTMSSGDLGKMDSLRKSMSQTDSRVRGKMRFWSKSKHGDKKISSRGRSADSELTDRRNDSPPGSPEHAGVSERRRDSKENREPMLGMMSMKRRRSLKISSVSLESTAWQNDALHILTSTADYRSMNDFLMKKISDLDAEDGQKDTAVDVVFKKALKEFRLNIFNSYSTALAMDDGRSIRYKDLYALFEHILEKSMRLEQRDWSESPVKVWVNTFKVFLDEFMTEYKPMDGTISKAPKPERKKRRKKESDTVEEHMGHIFKSTQYSIPTYCEFCSSLIWMMDKACVCKLCRYACHKKCCLRMTTKCSKKFDPELSSRQFGVELSRLTSDERSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELKQGLDTDANSVNLDDYNIHVIASVLKQWLRDLPNPLMTFELYEEFLRAMGLQDKREVVQGVYSIIDQLSRTHLNTLERLIFHLVRISFQEETNRMSANALAIVFAPCILRCPDTTDPLQSVRDISKTTACVELIICEQMRKYKARLKDINTLEFAENKAKSRLTHIRRSMGKSRARKSGHHTPSPPLSPRASEREEPVDEGAEPVLSEQQQAAMQQEEKVLTQQIENLQKEKEELTYEMLALEPRASDDEMLESEASIGTADSSENLMESEGAASDPWEKSPGAVSASRWRKSESKSRRCLRRQPESLDSVDSAVASLSSVSSTPHYRFRSSSSGPLFSSSSPTGDLHILPDPESCEQASLSARCASSSEKTRPRPRANRSCPPKPREPGDTGGRRREHEFGSSQPLVLYGSNEFMV
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons (By similarity). Required for the regulation of neurite branching and motor neuron axon guidance.
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E7F3I6
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CLP1_DANRE
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Polyribonucleotide 5'-hydroxyl-kinase Clp1 (EC 2.7.1.78) (Polyadenylation factor Clp1) (Polynucleotide kinase Clp1) (Pre-mRNA cleavage complex II protein Clp1)
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MTAEAAEKSVEEGLSSSGSAGSSGTRFDLDKETELRFEVEAGERVQLELLSGLAEIFGSELNRNKKYTFGPGSKIAVFTWQGCGVALSGKTEVAYVSKDTPMLLYLNTHAALEQMRRQAEKDNERGPRVMVVGPTDVGKSTVCRMLLNYAVRLGRRPTLVELDVGQSSVSVPGTMSALCIERPADVEEGFSVQAPLVFHFGSTTPGTNIKLYNKLTSSLADAFSQRCEVNRRASVGGCIINTCGWVKGSGYQALVHCASAFQVDVVLVLDQERLYNELKRDLPHFVRVVLLPKSGGVVERSKDCRRETRDEKIREYFYGFRGTSFYPHAFDVRFSDVRIYKIGAPSIPDSCLPLGMSQDDTQLKLVPVSPGRDLTHHVLSVSSVDDEAEVGQSRGILESPACGFIVVTAVDTQAQVMTVLSPAPRPLPRHTLLIMDIRFIDLK
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Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Its role in tRNA splicing and maturation is required for cerebellar development. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by dicer1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing.
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E7F4N7
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STING_DANRE
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Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
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MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRMSEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSFYIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKITHNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSRELFQNLKQQDGEIFMDPTNEVHPVPEEGPVGNCNGALQATFHEEPMSDEPTLMFSRPQSLRSEPVETTDYFNPSSAMKQN
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Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and irf3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. In addition to promote the production of type I interferons, plays a direct role in autophagy. Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation. Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity).
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E7F568
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COBL_DANRE
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Protein cordon-bleu
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MNLGDATTRPPVGRRMKAQAPPPPRPPQPAPRRIFRNAVPDGGGSSGGDCKENMLRSYVDLHISLPTGYQTTINVDGRKALMDLLVDLCSQYHLNPAYHTLELLSPDAQPVSFKPNALLGALDVSCALIKERVLEDRVIRKPPPKVPEKTVRLVVNYHRSQKAVVRVNPLAPLQTLVPVICQKCEFDPAHVLLFKDNINHQQLDLDKSLSDLGIRELYVLDQTLVLQPKMASTPALNYSAESLRSNSLSGSEKKGLLGFLKFNRRKSKGMSVVASGPCVEARPSTLGQSQSVMNISKMSPKVELKKRRAPAPPPAPTQTLPPTSQISLGSPSSHNLLKKRKAPAPPPTPPPSTPEPDISTYVPTATVQEHYIPASVERTPRASTPADDSDLSHSIEDSEPARSICSSSSGDDAAAVGSSSSSLAEEPVTHRADVIAPFTTSTPEPEPKPEYEPELKKEASPRSTPELEPGPRPEVPAAEDLEVEMELKMEETENNRHSGIAWLHSAHESVLERRVQQEVETVSVASSESFADHGYAASEDMAEESGPVSPSERMQSVSPMDIMSLNSDSTLPVKQSKESSSDSDEGCATWGSRQSSGHIQDGQKSIKRQNGYEEDPEITAQIHLTLADLDANLADLNHSDGASVFVDDEIPVSIVDMDIPVTAIDEVLDDDQCSASECESVLLRSTQSISSKPCTPCGVIQNKNNNACLTEEKHRSPFPDIEKQLQTATLTVIDKPTIQSPTSKKPSQDAKITDNMEQKTTFNSEAKSKSETVELTSQKDTVLQKSQSFVRPDVQSVQKERTSSTRVLPTQGKITLSSFSRFGMKTFTVIPPKPAVSQTKPAGSLVTGAIKIDEQGNMVTQRQISSGPEKNNTPSVDTTRADKTPLVKAKAFWSTTEKQEKLTTAKTEPIVNNGDTDVFKASAVTGSFKLSPPEETHKEVIIVERKPISGVASKPSFSENHAEKRDLSFLIPSRRTSSQYVASVIAKNNKNSSIPKTKIDTTPAPLSISGVQNPVNQLLNNEVKPTSIHKPAVTVKPTENPVPSFRPKCLQSYVAEKPTSSERISTLHGGDKTKSLDSQPLSIKIQPFPHVSAHIKSFSEEATSINNFPDTSSARQTPTDTTHPPLAKKPELHKSEIPSEPNQGNVFGPVKKFKPVIFKPVQQETSIHSSLMEAIQSGEGIERLRKVSDLPTSCTVKKPSYNDPENERSALLSAIRASSTSAKLKKTKSVASKELEQLRKVEEDRNVHTEVISPRPTSPDFVPPLPPSFSPPPPPPPPLAPAKPPVVLPPGGNPEAAREALLEAIRSGSGAQQLRKVPVTQTRRQVNGRLGTIQATSPLSYGH
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Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain, heart and kidney development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior. {ECO:0000250, ECO:0000269|PubMed:21129373, ECO:0000269|PubMed:23203810}.
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E7F587
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ZD20B_DANRE
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Palmitoyltransferase ZDHHC20-B (EC 2.3.1.225) (Acyltransferase ZDHHC20-B) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 20-B)
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MAPTHVLRCCQRGLAWIPVIFIALVVCWSYYAYVVELCLLVYLVVFHLSFVMFVWSYWKTIFTKPANPSKEFCLPKSEKEQYEKEQRPETQQEILKKVATSLPLYTRTGAGAIRYCDRCQVIKPDRCHHCSACDMCVLKMDHHCPWVNNCVGFSNYKFFILFLTYSLVYCLFIAASVLQYFIKFWTSDLPESHAKFHVLFLFFVAAMFCISILSLFTYHLWLVGKNRSTIEAFRAPVFRNGPDKNGFSLGFSKNIAQVFGDEKKYWLLPVFTSQGDGLSFPTRLVTIDPEQPTECLQPGGAISSLIIVEYCFCKQAKKKKTDE
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Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains.
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E7F590
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VPS41_DANRE
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Vacuolar protein sorting-associated protein 41 homolog
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MAEVEEQGRKLSEESTDESEEEDTEEEPKLKYERLTNGVTEILQKDAASCMTVHDKFLALGTHFGKVFLLDIQGNVTQKFEISSVKINQISLDESGDHVGICSEDGKVQVFGLYTREGFHENFDCPIKVVALHPQFSKSNNKQFVTGGNKLLLYERNWLNRWKTSVLHEGEGNITSVKWRGNLIAWANNVGVKIYDIGSKQRITNVLRDNTSLRPDMYPCSLCWKDNTTLIIGWGCSVKICAVKERDPTEMRDLPSRYVEIVSAFETEFFISGLAPLADQLVTLYYVKENSDHMEEEFRTRPRLDIIQPLPEGCEEISSDALTVRNFQENQCRDYRLEHSEGESLFYIISPKDIVVAKERDQDDHIDWLLEKKKYEEALMAAEISFKNIKRHDVQKIGMAYINHLVEKGDYDTAARKCQKVLGKNMDLWENEVYRFKTIGQLKAISQYLPRGDLRLRPAIYEMILHDFLKTDYEGFATLIREWPGELYNNMAIVQAVNEHLKKDPTNSILLTTLAELYTYDQRYDRALEIYLRLRHKDVYQLIHKHNLFSSIKDKIVLLMDFDKEKAVDMLLDNEDKISMDKVVEELKDRPELLHVYLHKLFKRDHHKGQKYHERQISLYAEFDRPNLLPFLRESMHCPLEKALEICQQRHFVEETVFLLSRMGNCRRALQMIMEELANVDKAIEFAKEQDDRELWEDLISYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILHDYNLQILLREGCKKILVADSLSLLQRMHRTQKKGVRVDEENICESCHTPILPSDTAQAFGVVVFHCRHMFHKECLPSPGSIPGIQYCNICSAKRRGPGSGILEMKK
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Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes.
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E7F594
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G137B_DANRE
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G protein-coupled receptor 137Ba
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MQKDSLPTLSPAVPPYVMLGLTVAYTIFYCLLFVFVYVQLWLVLRYRHKRFSYQTVFLFLCLLWAALRALLFSFYFKNCVTANTLGPFCFWLLYCFPVCLQFFTLSLMNLYFAQVIFKAKSKYSPELQKYRLPLYLLFLSISLLFLLVNLTCALLVKINRANTETVVLVRVTVNDSLFVLCAVSLSLCLYRIAKMSLANIYLEAKGTSVCQVTLIGVTVVLLYSSRACYNLVVLALTKIKSINSFDYDWYNVSDQADLKSTLGDAGYVVFGVILFVWELLPTSLVVYFFRVRKPTLDRSASVIPGHMFSSRAYFFDNPRRYDSDDDLAWSIIPQNIQASFTSDSYDWSCRNNSFTAYTEAEESHLAPEELNPY
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Lysosomal integral membrane protein that regulates the localization and activity of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (By similarity). Interacts with Rag GTPases and increases the lysosomial localization and activity of Rag GTPases and thereby regulates mTORC1 translocation and activity in lysosome. Acts also as a negative regulator of osteoclast activity. May be involved in interleukin-4-induced M2 macrophage polarization (By similarity).
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E7F6F7
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ABCB7_DANRE
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Iron-sulfur clusters transporter ABCB7, mitochondrial (ATP-binding cassette sub-family B member 7, mitochondrial)
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MAPLLVPLKCGFHMQRRKLSLLLQRSSAVQAWTFHDHRAANKRKERNTYLLSDPSRESSTWANNRGQNSQQILEAVKHLHLQERQCWHGNAGGGLSADPKNVLKEVNSSKILGAMFTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMLNLSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANLWNTQNSRILSNGSKPEPVPERVSQKEEERKKLQEEIMNSVKGCGNCSC
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Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). May play a role in cadmium, zinc and mercury detoxification.
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E7F7X0
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LMOD3_DANRE
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Leiomodin-3
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MSERTEQESYTDKIDEDEILAGLSAEELKQLQSEMDDIAPDERVPVGLRQKDASHEMTVRDCTEPESEEEIDEDEILAGLSAEELKQLQSEMEEIAPDERVPVGMRQRDQTDKPPTGSFDHRSLVEYLYWEKESKRMLEEERVPTTLLPSQKTNEEHEAKNEDKVEELELVYEEIVEEVEGGQGDAVVDEVIEEVIMEVEEEDKVCDKPVKTDLDATDPTVTSEDGLQRPSESADANVEAKTDQSGLDTETKVNEEKKEDSTEPAPSSYENWVPEKEERVISKLKIPKLALGGNTFVKKTARPSGNETNLESTLDKIRNNNPSVTDVNLNNIENIPKEMLLDYVNSLKKNRHVKTFSIANTGADENVAFTLANMLKENRSITTLNIESNFITGKGIVAIIRCLQFNETLTELRFHNQRHMLGHHAEMEVSRLLKANNTLLKMGYHFELPGPRMVVTNLLTRNLDRQRQQRMEEQKLQQMKEQRKVMEMYEDSLNLPPGMLEMLGGYIPLSLLQNCQNGAEDIPEDSPEPSPQPSPPHQLCKTQHLAPQQHPPNLSTGNLFEEVQLKKTPKRRDPLLEWNQCDERKDGRPNVHLRSVPKKRSIAREGPVDERANLKDMIKTLKPVPRRREPPKVDLTPRDHLLSEIRQSNVAYLKAVPLPKILESQETSLF
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Essential for the organization of sarcomeric thin filaments in skeletal muscle.
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E7F9L8
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MYO1D_DANRE
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Unconventional myosin-Id (Myosin 1d) (Myosin1D)
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MAEHESLEFGKADFVLLDNVSLEEFMANLKLRFEKGRIYSYIGEVVVSVNPYRAMNIYGRDVIEQYKGRELYERPPHLFAIADAAYKAMKRRNKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIFQQEGERSFHSFYQLVKGAPDAQLRSLHIQRDPTAYNYIKVGGQLKSSINDSAEFKAVADAMKVIGFTTEEIQTVYKILATILHLGNLKFGTDGDVTLIENSKLVSVLGDLLSTKEENVEKAMLYRTVATGRDVIDKQHTHQEASYGRDALAKAIYERLFCWIVGRINDIIEVKNYDARVHGKNTVIGVLDIYGFEIFQNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIFAVLDEACMNVGKVTDEMFLQALNGKLAKHAHYTSRKLSPTDKNLEFERDFRIRHYAGDVTYSVVGFIDKNKDTLFQDFKRLLYNSSNPVLKAMWPEGKLSITEVTKRPLTAATLFKNSMISLVEKLASKEPYYVRCIKPNDVKSPLLFEHERCKHQVEYLGLLENVRVRRAGFANRQTYPRFLQRYKMISEFTWPNHDLSSDKEAVKRLLQGCGFEHDVAYGKTKVFIRTPRTIFSLEEQRAEMVKRIVLFLQKVWRGTLARMRYRRMRAALIIIRAYRRYKVKSYIREVIRRFKNVRDMKDHGKHVKWPTPPKVLRKFEEALRSIYNRWWAWTLIKPLSPEKTVQIRAKVATLECLKGQRADLGLQRAWEGNYLKKDSPGTASSFTLVSSDLQRKDKFMRVLFSSNVRKINRFNKAEDRALLITDRHLYKMDPLKQYKPMKSIPLYNVTGVSISPGKDQLVVFHTKDNRDLIVCLQGMVPAGDSRIGELVGTLLSHFKSEKRKLQVNTVSPIHCSMNGRKCTVVVETKISQSQPDFTKSRSGYILSVPGN
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Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in the formation of Kupffer's vesicle, an organ that functions as left-right organizer during embryogenesis. Plays a role in vesicular trafficking events that are required for normal lumen expansion of Kupffer's vesicle. Required for normal orientation of cilia in Kupffer's vesicle, and thus for normal, unidirectional circular flow and normal angular flow velocity, which then mediates asymmetric gene expression and left-right asymmetric development. Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement (By similarity).
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E7FAG6
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AMR1A_DANRE
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Activating molecule in BECN1-regulated autophagy protein 1A
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MKLGQRNSVCILSSRERGAPGLASYRVLQQLVEEKTQRMKWQSQKVELPDSPRSTFLLAFSPDRSLMASTHVNHNIYITEVKSGKCVHSLVGHRRTPWCLTFHPIIPGLIASGCLDGEVRIWDLHGGSESWLTESNSAIASLAFHPTAQLLLIATNNEVHLWDWSRKEPFTVVKTASETERVRLVRFDPLGHYLLTAIVNPSNQPNDDDPEIPMDSVEMPHLRQRSFLQSQPARRTPILHNFLHILTSRNSVPQAGGAHSASTDGSSDSSGPYTLMCVQPLGMVCFCSRCSAARVPSPPDEDPSDSASLEAQAHTFSSARTEPLQMSRFSVESRAANRSSAFSSVYGGGSNMRNHSSSSGRRGVTGMAPVPHFRQHPPGREGGGRHPGADWTVSGLNGQSSSMTPQRTGASSVSLLSVLRQQETSFQSPVYTSASDRWGSTPGTSSSRHRPPEEEGQSSSSSIHSVLRCNLYRYFMDYEGTQDTVQPLDGSRQDQQTQEMLNNNMDPEQPGPSHYQSPYSGENPPHSHMNRCRVCHNLFTYNQGSRRWDRTGQPSSTERNTPWQPSSSAFHSVAPVSQSNEHLLEHRPIESTPNTPEPHVPFSQRTDTGQHEEQAVGLVFNQETGQLERVYRQSASSRSANISQGALNQEMPEDTPDNDYLRRLSPAAYYAQRMIQYLSRRDSVRQHSHRPPSRPRPLSSNPSSLSPSPVPNAESSEVDFEEFEENGSRYRTPRNARMSAPSLGRFVGTRRFLLPEFLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVPNCKIYNDASCDISADGQLLAVFIPSSQRGFPDEGILAVYSLAPHNLGEMLYSKRFGPNAISVSLSPMGRYVMVGLASRRILLHQISDHMVAQVFRLQQPHAGETSMRRVFDVVYPMAPDQRRHVSINSARWLPDPGLGLAYGTNKGDLVICRPVDVHSDGSSTSEHSERMFTINNGGGVGPSSSRSGDRAGSSRTDRRSRRDIGLMNGVGLQPQPPAASVTSQGTQTQNQRLQHAETQTDRDLPDDPQQPSTSQGSQVTDATESLDFETLPEDSGSEVVPETPPHSRPQEDEGSDPSEPSTDSTGQAEYVSRIRRLMAEGGMTAVVQREQSTTMASMGSFGNNIIVSHRIHRGSQTGADAQNRTRLSPIPGPSSGAPESLAAASYSRVLTNTLGFRGDTAQGIDLTEQERLHTSFFTPEFSPLFSSAVDATGPSSSIGADSVLEGEDFHDFASLPPSLLSSSPSLSPVNNSNYSNSDSSYLGDEYGR
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Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy. The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins (By similarity). Acts as an upstream master regulator of the transition from G1 to S cell phase: ambra1a specifically recognizes and binds phosphorylated cyclin-D (ccnd1, ccnd2 and ccnd3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation (By similarity). Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (eloc) component of CRL5 complexes (By similarity). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation (By similarity). In normal conditions, ambra1a is tethered to the cytoskeleton via interaction with dyneins light chains (By similarity). Upon autophagy induction, ambra1a is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (By similarity). Also acts as an activator of mitophagy (By similarity). Required for skeletal muscle development.
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E7FAM5
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LIN41_DANRE
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E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)
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MCEVILWSSAQMASFPDSDLQTCPLCKELCGCSAPISSNSSTSSSSSQTSNSSSTSSTRRLHVLPCLHAFCRQCLEGQRSPGDPLKLRCPTCDQKVSLSESGVDALPSSNFLFSNLLDVVVSAEEQGKNGRSSAVVHHGGLLRPQHLSDPQCSSCDEGNPATSHCLDCQEYLCDNCVRAHQRVRLTKDHFIEGLLESLHLANRTNNSNTPVSISQSFHNSFSMLNVFQERMDFCQHHDDAVLRFFCDSCTVPICRECSLGRHAGHSFTYLQDALQDSRALTIQLLADAQQGRQAIQLSIEKAQAIAEQVELKAKVVQSEVKTITLRHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLHQNLTKLDSTIATVTQVLEEGRSIDVLLAREHMLNQLQELKSLRCILQPQEDDRIMFTPPDQALLIAIKSLGLISSGAFATASKAHGEGIKRALQGKPASFTVVGYDHDGEPRLSGGDSVSVVLMSPDGNLSSAEVSDHQDGTYTVSYLPKGEGEHLLSVLICNQHIEGSPFKVMVKSGRSYGGVGLPMASFGGEGDGDGQLCRPWGICVDKEGYVVVADRSNNRVQIFKPCGTFHHKFGTLGSRPGQFDRPAGVACDSQRRIIVADKDNHRIQIFTFDGQFLLKFGEKGTKNGQFNYPWDVAVNFEGKILVSDTRNHRVQLFGPDGTFLNKYGFEGALWKHFDSPRGVAFNQEGHLVVTDFNNHRLLVIRPDCQSARFLGSEGTGNGQFLRPQGVAVDQEDRIIVADSRNHRIQVFEPNGNFLCKFGTHGNGFGQMDRPSGIAVTPDGVIVAVDFGNNRILMF
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E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and participates in post-transcriptional repression of transcripts. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development.
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E7FB98
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UBIA1_DANRE
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UbiA prenyltransferase domain-containing protein 1 (EC 2.5.1.-) (EC 2.5.1.39) (Protein barolo) (Protein reddish)
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MQEMKPAALSGSNGLNGASGSSVRVPCSRLSRAGRMALDLQSKCAAYVLALRPWSFSASLTPVALGSALAYKLEGSVDLLLLLVCAVAVLLVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILKPQDVVMFGAVLYSAGCLCATLLYFLSSLKLEHLALIYFGGLSSSFLYTGGIGLKYVALGDVVILITFGPLAVMFAHAVQVGYLSVLPLVYAVPLALNTEAILHSNNTRDMDSDKQAGIVTLAILLGPTLSYVIYNLLLFVPYLLFCILATRYTISMALPLLTLPMAFPLERQFRCRCYAKIPQKTAKLNLLMGLFYVFGIILAPQGSLPLL
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Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development (By similarity). Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4 (By similarity). Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from nos3/eNOS-dependent oxidative stress.
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E7FBY6
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AGRA2_DANRE
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Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124)
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MSGPCVRIPFWVRVFLLLLLYRIAAGCPELFSSGCSCTEDRSKAHPTPGTRRKVSCGGKELTETPEVSLLPNRTVSLNLSNNRIRMLKNGSFAGLSSLEKLDLRNNLISTIMPGAFLGLTALRKLDLSSNRIGCLTPEMFQGLTNLTKLNISGNIFSSLDPNVFMELHSLKLVNFHSEFLSCDCGLRWVPSFFRSGSARLGDETLCAYPRRLQNKPLRLLRESDLSCEGPLELHTLSLLPSQRQVVFKGDRLPFHCTASLVDKITALHWRQNGQPVTSDPTKGIHLEESVQHDCTFITSELILSNVHVEASGEWECVVSTGRGNTSCSVEIVVLENSASFCPEQKVNNNRGEFRWPRTLAGITSYQHCLQLRYPSLTLGGGVEQKKASRNCDRSGRWEEADYSQCLYTNDITRILHTFILMPVNASNAVTLAHQVRSYTLEAAGFTDTVDVLYVAQMMHKFMDYVTELRELSEVLVEMGSNLMQVDDQILARAQREERACSSIVYTLETLAWPQLHSHAQDLSRYSRNIVMEAHLIRPAHFTGISCTVYQRREGAAGSQVHDGADLSLEQQLRFRCTTGTHNTSLNAFHLKNAVALATVSLPATLFPPNAPPDCKLQFVAFRNGRFFPFTSNFTGHSDLARRRGISTPVIYAGLDGCSMWNQSDPIIVSLRHTSPGHDPVAAHWNSQALGHHGSWSLDGCQLIHSDVSISTLRCSVLSNYAVLQEIPDFPGSPSIPVEVLHPVIYTCTAVLLLCLFTIIITYILHHSSIRITRKSWHTLLNTSFHVAMTSAVFAGGITLTGYPIVCQAVGIVLHYSSLSTLLWIGVSARVIYKEALLRTPQQLEGESAVQPTQRPMLRFYLIAGGVPLIICGITAAVNINNYGDNIPYCWLVWQPSFGAFYIPAGLIILVTWIYFLCTVFCLRQRNFQESKDLQCSASDPSNLPESQPALSGSTSLLSTDSGVSPVHAGTTVEDQYSLKVQCLALMATQFVFVGLWCCGAMAVWHVDRERKLFSCLYGGTATGLGIFLVLHHCFKRLDVQAAWLGCCPGYHRSQPMPAYSHPCTVTVGVQSASERGSQLFVACHPPTDPNHYSSSARSSSTQSGTASITVVPSKLTNLLQVSQDNANNASRAPAGTNTNTSTSTENNKPTNNLLPSLLPVQQPQRRKACSRTKGGNTQYHHRGDARSHYRLKALRAGGGGSMGALGPSGTEHSNIYHVHKHASSENGSLRNSHSEGQNGLLTNGRHRGEGLATSPSEGSDGGSSGSRKPFPLLPSVARRAAMQQNAQCRSASKDNLKLAAAAERESKRSSFPLNMSSNVTATASLSTVSAPNGTLKGSVVELDTSGTDQSQGSVGMKSRVWKSETTV
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Endothelial receptor which functions together with reck to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b). Plays a key role in Wnt7-specific responses: Required for normal central nervous system (CNS) vascularization where it functions cell-autonomously in the tip cells of sprouting vessels. Has a role in development of dorsal root ganglia. Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Adgra2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly.
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E7FCP8
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NAGS_DANRE
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N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) [Cleaved into: N-acetylglutamate synthase, mature form (NAGS-M); N-acetylglutamate synthase, conserved domain form (NAGS-C)]
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MAKVNSGSSGCRAMVMAGQFWTKPFALSSQRSGPHRRSAAEVNRRMSSSRTAGHGSKTPLWSQQESYNHSSLGERSAWSNRTLIYRDVKAFLREIGGDPREARYWLTHFQRAGSTPAFAVLEVDPSVFDSHEMVQSLAFGLSFLQRMDMKLVVVMGLPAEITEDDHTRSATDSPLARTVMVKHCQALTEALQDNSANVMPFFSSEALLQLQDNPLDGSSSGPSVVVDSALLQWTLDCRVIPLVCPVGRDTTGRSSVLRSIQVTTAISQTLQPLKVIFLNSSGGIRNQNHKVLGLVSLPGDLPALSCAEWLNEVEQKRIGSIAELLNLLPVESSAVLTSANTLLTELFSHKGSGTLFKNGDPIRRYSSLEDIDVDRLLALINKSFEKNLREDYIASLEGRLHSVYLSEGYSAAAIITTEPVNSGTPYLDKFVVSSSKQGQGTGQILWECIRQDFSKLFWRSRTTNRINPWYFKHCDGSFVNGHWIVFWLGLSDIRESYELVEFAKSHPDSFCSLSTTETKPLQQHHGS
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Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (cps1) activity.
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E7FE13
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LGR4_DANRE
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Leucine-rich repeat-containing G-protein coupled receptor 4
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MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTGTINLESLTLTGTKIRSIPADLCEDLTVLRTVDLSYNDIEDLPSFQGCVRLQDINLQHNQIKQIDRGTFQGMTSLRVLDLSRNQIKFIHRDAFLSLSALTNLDLSLNSLASVPTAGLSALNQLKLTGNMELRNGLMSKTLPKLRSITVPYAYQCCAFVAYDSAVNPAEDDERRNAFGGEEDMERIPMVMHCSPLPGAFKPCEHLLGSWMIRLTVWFICLVALLFNCLVLAATFSPRTSSLSPSRFLVALLASANLLTGVYVAALTLLDTVTWGSFAEYGVWWETGAGCQVVGFLAVFSSEWAVLLLALAAVERCLAVRALMGKAGALRSRGERRERRRRFAIAALLLGLVSVAAACLSLYHGSAMGSPLCLPFSEGSSPGLGFTVALVLMNTLAYLLSAVVYTRLYCRLGRAQLADPEQAGSVRHIAWLIFTNCIFFCPVAAFSFAPLLAGTSNAVGGPEMAKSVTLIFFPLSACLNPVLYVCFSPSFRYDWLHLRGRGRTGGCGRLVAKTVTKGTVAGGSPVSDDGEGLSSDCGMYTKLHGDSRGMCEHCDAALHIRTSSSSGSSSSSACRHLVKSHSCPALMGNVPQCLSSEGYWPDTGTLSAQSEYGDEGDSFVSDSSEQVQACGRACFCQSRGLPLVHYSYNIPRMTD
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Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids. Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland.
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E7FHC4
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HYD2A_PYRFU
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Sulfhydrogenase 2 subunit alpha (EC 1.12.1.5) (Hydrogen dehydrogenase (NAD(P)(+))) (Hydrogenase-II subunit alpha) (H-II alpha) (NADP-reducing hydrogenase subunit ShyA) (Sulfhydrogenase II subunit alpha)
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MIIELDEFTRVEGNGKAEIVIENGEVKDARVKIVEGPRFFEILTLGRDYWDVPDLEARICAICYIAHSVASVRAIEKALGIDVPESVEKLRELALWGEIIESHALHLYLLALPDVFGYPDAISMIPRHGELVKEGLTIKAFGNAIRELIGGREIHGINIKPGGFGRYPSEEELEKIAEHSKSLIKFARRIVGIFASQEAGGAVGEVLMATSDYLWGDELIINGERVQYYEVDEVPVGYSFAKHSYYKGNPVFVGALPRLLLKGESIEGEAARMLEEYRDKLESKYVIYNNLAQAIELLYALERVPQLVEEILSEGIERGNGEISQESGEGVGYVEAPRGVLVHHYRIENGKVVWSNTITPTAFNQRLMELSLLEEAKRLYGSESEENMKKRLEVIVRAFDPCISCSVHFVKL
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Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.
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E7FHF8
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HYD2D_PYRFU
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Sulfhydrogenase 2 subunit delta (EC 1.12.1.5) (Hydrogen dehydrogenase (NAD(P)(+))) (Hydrogenase-II subunit delta) (H-II delta) (NADP-reducing hydrogenase subunit ShyD) (Sulfhydrogenase II subunit delta)
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MKLGVFELTDCGGCALNLLFLYDKLLDLLEFYEIAEFHMATSKKSREKIDVALVTGTVSTQRDLEVLRDARNRSEYLIALGTCATHGSVQGVIENSKEAYRRVYGNGKPPVKLLNPKPVTDYVPVDFAIPGCPYDKEEVFQVLIDIAKGIEPVAKDYPVCLECKLNEYECVLLKKRIPCLGPVTAGGCNAKCPSYGLGCIGCRGPSLDNNVPGMFEVLKEILPDEEIARKLRTFARW
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Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.
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E7FHP1
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ACDB1_PYRFU
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Acetate--CoA ligase [ADP-forming] I subunit beta (EC 6.2.1.13) (ADP-forming acetyl coenzyme A synthetase I subunit beta) (ACS I subunit beta)
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MDRVAKAREIIEKAKAENRPLVEPEAKEILKLYGIPVPEFKVARNEEEAVKFSGEIGYPVVMKIVSPQIIHKSDAGGVKINIKNDEEAREAFRTIMQNARNYKPDADLWGVIIYRMLPLGREVIVGMIRDPQFGPAVMFGLGGIFVEILKDVSFRVAPITKEDALEMIREIKAYPILAGARGEKPVNIEALADIIVKVGELALELPEIKEIDINPIFAYEDSAIAVDARMIL
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Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.
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E7FHU4
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HYD1D_PYRFU
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Sulfhydrogenase 1 subunit delta (EC 1.12.1.3) (Hydrogenase I small subunit) (NADP-reducing hydrogenase subunit HydD) (Sulfhydrogenase I subunit delta)
|
MGKVRIGFYALTSCYGCQLQLAMMDELLQLIPNAEIVCWFMIDRDSIEDEKVDIAFIEGSVSTEEEVELVKKIRENAKIVVAVGACAVQGGVQSWSEKPLEELWKKVYGDAKVKFQPKKAEPVSKYIKVDYNIYGCPPEKKDFLYALGTFLIGSWPEDIDYPVCLECRLNGHPCILLEKGEPCLGPVTRAGCNARCPGFGVACIGCRGAIGYDVAWFDSLAKVFKEKGMTKEEIIERMKMFNGHDERVEKMVEKIFSGGEQ
|
Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.
|
E7FHX4
|
HJC_PYRFU
|
Holliday junction resolvase Hjc (Hjc) (EC 3.1.21.10)
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MYRKGAQAERELIKLLEKHGFAVVRSAGSKKVDLVAGNGKKYLCIEVKVTKKDHLYVGKRDMGRLIEFSRRFGGIPVLAVKFLNVGWRFIEVSPKIEKFVFTPSSGVSLEVLLGIQKTLEGKS
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A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Cleaves both mobile and immobile junctions. Binds 4-way junction DNA, a synthetic Hj, binding is not competed by dsDNA. {ECO:0000255|HAMAP-Rule:MF_01490, ECO:0000269|PubMed:10430863, ECO:0000269|PubMed:11005813, ECO:0000269|PubMed:11071944}.
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E7FI44
|
HYD1A_PYRFU
|
Sulfhydrogenase 1 subunit alpha (EC 1.12.1.3) (Hydrogenase I large subunit) (NADP-reducing hydrogenase subunit HydA) (Sulfhydrogenase I subunit alpha)
|
MKNLYLPITIDHIARVEGKGGVEIIIGDDGVKEVKLNIIEGPRFFEAITIGKKLEEALAIYPRICSFCSAAHKLTALEAAEKAVGFVPREEIQALREVLYIGDMIESHALHLYLLVLPDYRGYSSPLKMVNEYKREIEIALKLKNLGTWMMDILGSRAIHQENAVLGGFGKLPEKSVLEKMKAELREALPLAEYTFELFAKLEQYSEVEGPITHLAVKPRGDAYGIYGDYIKASDGEEFPSEKYRDYIKEFVVEHSFAKHSHYKGRPFMVGAISRVINNADLLYGKAKELYEANKDLLKGTNPFANNLAQALEIVYFIERAIDLLDEALAKWPIKPRDEVEIKDGFGVSTTEAPRGILVYALKVENGRVSYADIITPTAFNLAMMEEHVRMMAEKHYNDDPERLKILAEMVVRAYDPCISCSVHVVRL
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Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.
|
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