entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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D3ZF77
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AK1CA_RAT
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Aldo-keto reductase family 1 member C15 (EC 1.1.1.-) (EC 1.1.1.216) (RAKc)
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MDLKHSRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY
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Catalyzes the NADPH-dependent reduction of a variety of substrates including aromatic and aliphatic aldehydes, quinones, ketones, dicarbonyl compounds and 17-ketosteroids. Catalyzes the NADP(+)-dependent oxidation of aromatic, alicyclic and aliphatic alcohols, and 17beta-hydroxysteroids. To a lesser extent, can also catalyze the reduction of some aldoses and ketoses and the oxidation of some sugar alcohols. In the stomach, lung and colon tissues, mediates the reduction of farnesal and geranylgeranial into farnesol and geranylgeraniol respectively. By reducing 4-hydroxy-2-nonenal (HNE), produced during lipid peroxidation, into 1,4-dihydro-2-nonene (DHN), protects vascular endothelial cells from damage elicited by oxidized lipoproteins.
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D3ZF92
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TNR21_RAT
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Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358)
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MGTSASSITALASCSRIAGQVGATMVAGSLLLLGFLSTITAQPEQKTLSLTGTYRHVDRTTGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPSGTFTRHENGIERCHDCSQPCPRPMIERLPCAALTDRECICPPGMYQSNGTCAPHTVCPVGWGVRKKGTENEDVRCKQCARGTFSDVPSSVMKCRAHTDCLGQNLMVVKQGTKETDNVCGVHLSSSSTTPSSPGIATFSHPEHTESHDVPSSTYEPQGMNSTDSNSTASVRTKVPSDIQEETVPDNTSSTSGKESTNRTLPNPPQLTHQQGPHHRHILKLLPSSMEATGEKSSTAIKAPKRGHPRQNPHKHFDINEHLPWMIVLFLLLVLVLIVVCSIRKSSRTLKKGPRQDPSAIMEKAGLKKSLTPTQNREKWIYYRNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNVKLENSTLLTVEPSPLDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHILNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL
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Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21 this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation (By similarity). Negatively regulates oligodendrocyte survival, maturation and myelination. {ECO:0000250, ECO:0000269|PubMed:21725297}.
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D3ZFB6
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PRRT2_RAT
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Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3)
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MAASSSEVSEMKGVEDSSNTHSEGPRHSEEGMGPVQVVAENLDQPEALQSGPDTTAAPVDSGPKAELAPETTETPVETPETVQATDLSVNPGEDSKTCPSPKEACQEPASRPEVNREATAEQGAEQQSAAPPEPTSEQALQLNTQSDPQPTSQPPPKPPLQAEPPTQENPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
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As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
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D3ZFD0
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MY18A_RAT
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Unconventional myosin-XVIIIa
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MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSMRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSIILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLMQHSGLGIPRPGPRSRVPELVTKRFPADLRLPALVPPPPPALRELELQRRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRTGEGHRREPTDAKTEEQIAAEEAWYETEKVWLVHRDGFSLASQLKSEELSLPEGKVRVKLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSSQHLVQYLATIAGTSGNKVFSVEKWQALATLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASVQTMLLEKLRVARRPASEATFNVFYYLLACGDSTLRTELHLNHLAENNVFGIVPLSKPEEKQRAAQQFSKLQTAMKVLAISPEEQKACWLILASIYHLGAAGATKAVFSCGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGLGEGTGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQKLFHERTFLQELERYKEDNIELAFDDLEPVTDDSVAAVDQASHQSLVRSLAHADEARGLLWLLEEEALVPGATEDTLLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQNSVVECLPSKRKALGSVLSSEKKKRKKKKKKKCPESANSVAHTYSLSTQTLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRSASSRRVSSSSELDLPPGDPCEAGLLQLDVSLLRAQLRGSRLLDAIRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIMVDEKRAVEELLESLDLEKSSCCMGLSRVFFRAGTLARLEEQRDEETSRHLTLFQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDEEIQQLRNKLEKVEKERNELRLNSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEAMDMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQNRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLRQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQLEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLESMASRLKENMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKRKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDGSLKSSSPTSHWKSLAPDLSDDEHDPVDSISRPRFSHNYLSDSDTEAKLTETNA
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May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (By similarity). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking. Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages. Strongly enhances natural killer cell cytotoxicity (By similarity).
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D3ZFJ3
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3BP1_RAT
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SH3 domain-binding protein 1
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MMKRQLHRMRQLAHTGSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYANYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAAPFSRVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTSDLYDDWMRAASLKEPGARLEALHDVCSRLPQENFNNLRYLMKFLALLAEEQDVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEVLIQNADTLFPGDINFSVSGIFSGLAPQEKPNSQQVSEELAPVAVPATAATPTPTPAPTPAPASMTVKERTESELPKPASPKVSRSPTDTTALAEDMTRKTKRPAPARPTMPPPQPSSSRSSPPALSLPAGSVSPGTPQALPRRLVGTSLRAPTVPPPLPPAPPQPARRQSRRLPVSPCPASPVISNMPAQVDQGAATEDRGGPEAVGGHPPTPVLPPQPRPRGLISETD
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GTPase activating protein/GAP which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (By similarity).
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D3ZG27
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UBIA1_RAT
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UbiA prenyltransferase domain-containing protein 1 (EC 2.5.1.-) (EC 2.5.1.39)
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MAAVQAPGEKINIQAGETTQVGDTDQQRNDWPEEDRLPERSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSQGVLDPRLLLGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVRFGVFLYTLGCVCAAYLYYLSTLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLVILITFGPLAVMFAYAVQVGSLAIFPLVYAIPLALSTEAILHSNNTRDMESDREAGIVTLAILIGPTLSYILYNTLLFLPYLIFTILATHCSISLALPLLTSPMAFSLERQFRSQAFNKLPQRTAKLNLLLGLFYVFGIILAPAGSLPRL
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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. 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. 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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D3ZG83
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M3K10_RAT
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Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25)
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MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPTDLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREGSSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGSSGGSGTWSRSGPPKKEELVGGKKKGRTWGPSSTLQKERAGGEERLKALGEGSKQWSSSAPNLGKSPKHTPMAPGFASLNEMEEFAEADEGNNVPPSPYSTPSYLKVPLPAEASPCAQPPWEPPAATPSRPGHGARRRCDLALLGCATLLSAVGLGADVAEARAGDGEEQRGWLDGLFFPRPGRFPRGLSPTGRPGGRREETAPGFGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPTAPSPPPSLLPPSPSTNPLVDVELESFKKDPRQSLTPTHVTAAHAVSRGHRRTPSDGALRQREPPELTNHGPRDPLDFPRLPDPQALFPTRRRPLEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLSISPPSRPDTPESPGPLSVQPTLLDMDMEGQSQDNTVPLCGAYGSH
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Activates the JUN N-terminal pathway.
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D3ZGB1
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NFAT5_RAT
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Nuclear factor of activated T-cells 5 (NF-AT5) (T-cell transcription factor NFAT5)
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MPSDFISLLSADLDLESPKSLYSRDSLKLHPSQNFHRAGLLEESVYDLLPKELQLPPPRETSAASMSQTSGGEAGSPPPAVVAADASSAPSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTGNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLDSQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRGSVKDRTQQGFPTVKLEGHNEPVVLQVFVGNDSGRVKPHGFYQACRVTGRNTTPCKEVDIEGTTVIEVGLDPSSNMTLAVDCVGILKLRNADVEARIGIAGSKKKSTRARLVFRVNITRKDGSTLTLQTPSSPILCTQPAGVPEILKKSLHSCSVKGEEEVFLIGKNFLKGTKVIFQENVSDENSWKSEAEIDMELFHQNHLIVKVPPYHDQHITLPVSVGIYVVTNAGRSHDVQPFTYTPDPAAGALSVNVKKEISSPARPCSFEEALKAMKTTGCNVDKVTILPNALITPLISSSMIKTEDVTPMEVTSEKRSSPIFQTTKTVGSTQQTLETISNIAGNASFSSPSSSHLSPENENQQQLQPKAYNPETLTTIQTQDISQPGTFPAVSASSQLPSSDALLQQAAQFQTRDAQSRDTMQSDSVVNLSQLTEAPQQQQSPLQEQAQIPSNIFPSPNSVSQLQSTIQQLQAGSFTGSTASGSNGSVDLVQQVLEAQQQLSSVLFSTPDGNENVQEQLNADIFQVSQIQNSVSPGMFSSTESAVHTRPDNLLPGRADSVHQQTENTLSSQQQQQQQQQQQQQQQVIESSAAMVMEMQQSICQAAAQIQSELFPSAASANGSLQQSPVYQQPSHMMSALPTSEDMQMQCELFSSPPAVSGNETSTTTTPQVATPGSTMFQPPNSGDGEETGAQAKQIQSSVFQTMVQMQHSGDSQPQVNLFSSTKNIMSVQSNGTQQQGNSLFQQGSEMLSLQSGSFLQQSSHSQAQLFHPQNPIADAQSLSQETQGPMFHSANPIVHSQTSTASSEQLQPSMFHSQSTIAVLQGSSVPQDQQSPNIYLSQSSISNLQTNTVAQEEQISFFSAQNSISPLQSTSNTEQQAAFQQQPPISHIQTPLLSQEQAQPSQQGLFQPQVALGSLPANPMPQNQQGPIFQTQRPIVGMQSNSPSQEQQQQQQQQQQQQQQQQQQSILFSNQNAMATMASQKQPPPNMIFSPNQNPMASQEQQNQSIFHQQSNMAPMNQEQQPMQFQNQPTVSSLQNPGPTPSESPQTSLFHSSPQIQLVQGSPSSQEQQVTLFLSPASMSALQTSINQPDMQQSPLYSPQNNIPGIQGSTSSPQPQAALFHNTTGGTINQLQNSPGSSQQTSGMFLFGIQNNCSQLLTSGPATLPEQLMAINQPGQPQNEGQSSVTTLLSQQMPESAPLASSVNNSQNMEKIDLLVSLQSQGNNLTGSF
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Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes. Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3'. Mediates the transcriptional response to hypertonicity. Positively regulates the transcription of LCN2 and S100A4 genes optimal transactivation of these genes requires the presence of DDX5/DDX17. Also involved in the DNA damage response by preventing formation of R-loops R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
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D3ZGQ5
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NEK8_RAT
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Serine/threonine-protein kinase Nek8 (EC 2.7.11.1) (Never in mitosis A-related kinase 8) (NimA-related protein kinase 8)
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MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNIHTDVGSVRMRRAEKCLTPGTPMAPGSTGSRATSARCRGVPRGPVRPAIPPPLSSVYAWGGGLSIPLRLPMPNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGTGGGTLLPGAVELPQPQFVSRFLEGQSGVTIKHVACGDLFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSADGELFAWGRGDGGRLGLGTRESHNCPQQVPMVPGQEAQRVVCGIDCSMILTSPGRVLACGSNRFNKLGLDCLSLEEEPVPHQQVEEALSFTPLGSAPLDRETLLCVDLGTAHSAAVTASGACYTFGSNQHGQLGTSSRRVSRAPCRVQGLEGIKMVMVACGDAFTVAIGAEGEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP
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Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia. Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway (By similarity).
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D3ZGS3
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OCRL_RAT
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Inositol polyphosphate 5-phosphatase OCRL (EC 3.1.3.36) (EC 3.1.3.56) (Inositol polyphosphate 5-phosphatase OCRL-1) (OCRL-1) (Phosphatidylinositol 3,4,5-triphosphate 5-phosphatase) (EC 3.1.3.86)
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MEPRLPIGAQPLACLHMVAGLEMKGPLREPCVLTLARRNGQYELIIQLHGKEQHVQDIIPINSHFRCVQEAEETLLIDIASNSGCKIRVQGDWTRERHFEIPDEERCLKFLSEVLAAQEAQSQLLVPEQKDSSNWYQKLDTKDKPAYSGLLGFEDNFSSMNLDKKMNTQNPPTGIHREPPPPPSSNRMLPREKEALNKEQPKVTNTMRKLFAPNSQSGQREGLIKHILAKREKEYVNIQSFRFFVGTWNVNGQSPDSSLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWAMAVERGLPSKAKYKKVQLVRLVGMMLLVFAKKDQCQYIRDIATETVGTGIMGKMGNKGGVAMRFVFHNTTFCIVNSHLAAHVEEFERRNQDYKDICARMSFSVPNQTLPQVNIMKHDVVIWLGDLNYRLCMPDANEVKSLINKNELQKLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYDSKTDRWDSSGKCRVPAWCDRILWRGINVNQLHYRSHMELKTSDHKPVSALFHIGVKVVDERRYRKVFEDIVRIMDRMENDFLPSLDLSRREFMFENVKFRQLQKEKFQISNNGQVPCHFSFIPKLNDTQYCKPWLRAEPFEGYLEPNETIDISLDVYVSKDSVTILNSGEDKIEDILVLHLDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQMVPLDEGTSERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETIPGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAHDPRICKQVISQLPRCHRNVFRYLMAFLRELLKFSDYNNVSTNMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLVFLLGSEED
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Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2. Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of inositol 1,3,4,5-tetrakisphosphate. Regulates traffic in the endosomal pathway by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with endosomes. Involved in primary cilia assembly. Acts as a regulator of phagocytosis, hydrolyzing PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K signaling.
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D3ZHA0
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FLNC_RAT
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Filamin-C (FLN-C) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)
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MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNVGMALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDNTFRCTYRPVMEGPHTVHVAFAGAPITRSPFPVHVAEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVIPGKYVVTITWGGYAIPRSPFEVQVSPEAGAQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDRGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHIQPAPPDCFPDKVKAFGPGLEPTGCIVDRPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTVIISWGGVNVPKSPFRVNVGEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGHYTIMVLFANQEIPASPFHIKVDPSHDASKVKAEGPGLSRTGVEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNVAPPLDLSKVKVQGLNSKVAVGEEQAFLVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGSGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEGVLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATIQPVFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPIPKFPTRVHVQPAVDTSGIKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGVTEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYVPFTPGDYDVNITFGGQPIPGSPFRVPVKDVVDPGKVKCSGPGLGTGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKVLPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHALPTGDASKCLVTVSIGGHGLGACLGPRIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLACDPLPHVEEPAEVLQLHQPYAPLRPGTCPTHWATEEPVVPVEPLESMLRPFNLVIPFTVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVDAINSGHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKITGDDSMRTSQLNVGTSTDVSLKITEGDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILVGPSEIGDASKVRVWGKGLSEGQTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKVTGEGRMKESITRRRQAPSIATIGSTCDLNLKIPGNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEGEASSQDMTAQVTSPSGKTEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTVGPLGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPVASLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNVP
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Muscle-specific filamin, which plays a central role in sarcomere assembly and organization. Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events.
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D3ZHH1
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DLL4_RAT
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Delta-like protein 4 (Drosophila Delta homolog 4) (Delta4)
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MTPGSRSACRWALLLLAVLWPQQRAAGSGIFQLRLQEFANERGMLANGRPCEPGCRTFFRICLKHYQATFSEGPCTFGNVSTPVLGTNSFVIRDKNSGSGRNPLQLPFNFTWPGTFSLNIQAWHTPGDDLRPETSPGNSLISQIIIQGSLAVGKNWKSDEQNNTLTRLRYSYRVVCSDNYYGDSCSRLCKKRDDHFGHYECQPDGSLSCLPGWTGKYCDQPICLSGCHEQNGYCSKPDECNCRPGWQGPLCNECIPHNGCRHGTCTIPWQCACDEGWGGLFCDQDLNYCTHHSPCKNGSTCSNSGPRGYTCTCLPGYTGEHCELELSKCASNPCRNGGSCKDHENSYHCLCPPGYYGQHCEHSTLTCADSPCFNGGSCRERNQGASYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRTCRCRPGFTGTHCELHISDCARSPCAHGGTCHDLENGPVCTCPAGFSGRRCEVRITNDACASGPCFNGATCYTGLSPNNFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLVVLLVLLVMVAVAVRQLRLRRPDDDSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKLQNHTLDYNLAPGFLGRGSTPGKYPHSDKSLGEKVPLRLHSEKPACRISAICSPRDSMYQSVCLISEERNECVIATEV
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Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate (By similarity).
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D3ZHP7
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ULK3_RAT
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Serine/threonine-protein kinase ULK3 (EC 2.7.11.1) (Unc-51-like kinase 3)
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MAGSGWGLPRLDGFILTERLGSGTYATVYKAYAKKATREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPSHRISFQDFFAHPWVDLEHMPSGESLAQATALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTTGQELLREMARDKPRLLAALEVASAAMAKEEEAGKEQDALDLYQHSLGELLLLLAAEAPGRRRELLHTEVQNLMARAEYLKEQIKIRESHWEAESLDKEGLSESVRSSCTLQ
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Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy (By similarity).
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D3ZHR2
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ABCD1_RAT
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ATP-binding cassette sub-family D member 1 (EC 3.1.2.-) (EC 7.6.2.-) (Adrenoleukodystrophy protein) (ALDP)
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MPVLSTPSRPSRVTTLKRTAVVLALTAYGVHKIYPLVRQCLTPARGPQVPAGESTQEASGATTAKAGMNRVFLQRLLVLLRLLFPGVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDMVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYAESDSEAMKKAALEMKEEELVSERTEAFTIARNLLTAAADATERIMSSYKEVTELAGYTARVYEMFQVFEDVQHCRFKRTGDLEEAQAGPGSMVHSGVHIEGPLKIQGQVVDVEQGIICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGISLLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQGRLQELRQILGEAAAPVQPLVPGIPT
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ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen. Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (By similarity). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation. Involved in several processes namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Controls also the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (By similarity).
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D3ZHS6
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BAP1_RAT
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Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1)
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MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNSMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRVKYEARLHVLKGNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPFGLEAGRTPAASECTHTDGAEEVAGSCPQTTTHSPPSKSKLVVKPSGSSLNGVPPTPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPQQYSDDEEDYEDEEEDVQNTSSAIRYKRKGTGKPGSLSNSSDGQLSVLQPNTINVLTEKLQESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSTRSSQGSQGSSSLEEKEVVEVTDSRDKSGLNRSSEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
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Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. Acts as a tumor suppressor.
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D3ZHV2
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MACF1_RAT
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Microtubule-actin cross-linking factor 1 (Actin cross-linking family 7)
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MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQKKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGESGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFPKVPEGGEGISATEVDSRWQEYQSRVDSLIPWIRQHTILMSDKSFPQNPVELKALYNQYIHFKETEILAKEREKGRIKELYKLLEVWIEFGRIKLPQGYHPNHVEEEWGKLIVEMLEREKSLRPAVERLELLLQIANKIQNGALNCEEKLTLAKNTLQADAAHLESGQPVQCESDVIMYIQECEGLIRQLQVDLQILRDEKYYQLEELAFRVMRLQDELVTLRLECTNLYRKGHFTSLELVPPSTLTTTHLKAEPLNKTTHSSSTSWFRKPMTRTELVAISSSEDEGSLRFVYELLSWVEEMQMKLERAEWGNDLPSVELQWETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYVETLGKLETQYCKLKETSSFRMRHLQSLHKFVSKATAELIWLNGKEEEELACDWSDSNPNISAKKAYFSELTMELEGKQDVFRSLQDTAELLSLENHPAKQTVEAYSAAVQSQLQWMKQLCLCVEQHIKENAAYFQFFSDARDLESFLRNLQDSIKRKYTCDHNTSLSRLEDLLQDSMDEKEQLIQSKSSVASLVGRSKTIVQLKPRNPDHVLKSTLSVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCLLIPPPNTEAIDVASRVEQSYQKVMALWHQLHINTKSLISWNYLRKDIDAVQTWNLEKLRSSAPGECHQVMKNLQAHYEDFLQDSHDSALFSVADRLRIEEEVEACKTHFQQLMESMENEDKEETLAKVYISELKNIRLRLEECEQRLLKQIQSSASSKTDRDARQDVALRIAEQEHVQEDLKHLRSDLDAVSVKCTTFLQQSPSGSSATTLRSELNLMVEKMDHVYGLSIVCLNKLKTIDVIVRSIQDAELLVKGYEIKLSQEEAVPADLSALESHRTTLQHWLSDVKDKNSVFSVLDEEISKAKAVAEQLHHRAAEPNLDLERYQEKGSQLQERWHRVIAQLETRQSEVESIQEVLRDYRACHGTLIKWIEETTAQQEMMKPGQAEDSRVLSEQLSQQTELFAEIERNQTKLDQCQKLSQQYSTTVKDYELQLMTYKAFVESQQKSPGKRRRMISSSDAITQEFMDLRTRYTALVTLTTQHVKYISDALRRLEEEEKVVEEEKQEHVEKVKDLLGWVSTLARNTQGTTTSSRTSASTDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEREKEQISEQLCALNKTYHDLCDGSANQLQQLQSELAQQTEQKTLQKQQDTCHKKLEDLRSWVRQAERALERHRGRASQQELSALQQNQSDLKDLQGDIQNHSTSFATAVKDIEGFLEENQNKLSPQELTALREKLYQAKEQYEGLQDRTREAQKELEEAVTSALQQETEKSKAATELAENRRKIDALLDWVTSVGSSDRQPQTSLPGTEQFSGACLEKQTLDATDGCVDVNQVPEKLDRQYELMKARHQELLSQQQNFIVATQSAQSFLDQHSHNLTPEERQMLQEKLGELKEQYAASLAQSEAKLRQTQTLRDELQKFLQDHREFENWLERSENELDGMHTGGSSPEALNSLLKRQGSFSEDVISHKGDLRFVTISGQKVLETENNFEEGQEPSPTRNLVNEKLKDATERYTTLHSKCTRLGSHLNMLLGQYQQFQSSADSLQAWMLTCEASVEKLLSDTVASDPGILQQQLATTKQLQEELAEHQVPVEKLQKAAHDLMDIEGEPSLDCTPIRETTESIFSRFQSLSCSLAERSALLQKAIAQSQSVQESMESLLQSMKEVEQNLEGEQVAALSSGLIQEALANNMKLKQDIARQKSSLEATREMVTRFMETADGNSAAVLQDRLAELSQRFHRLQLQQQEKESGLKKLLPQAETFEQLSSKLQQFVEHKNRLLASGNQPDQDIAHFSQHIQELTLEMEDQKENLGTLEHLVTALGSCGFALDLSQHQEKIQNLKKDFTELQKTVQEREKDASNCQEQLDEFRKLIRTFQKWLKETEGNVPPAETFVSAKELEKQIEHLKGLLDDWAGKGVLVEEINTKGTALESLIMDITAPDSQAKTGSVLPSVGSSVGSVNGYHTCKDLTEIQCDMSDVNSKYDKLGDALRERQESLQTVLSRMEEVQKEASSVLQWLESKEEVLKGMDASLSPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLEAYPNSQEAENWRKMQEDLNSRWEKATEVTVARQKQLEESASHLACFQAAESQLRPWLMEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLTEAAQGILTGPGDVSPSASQVHKDLQSISQKWVELTDKLNSRSTQIDQAIVKSTQYQDLLQDLSEKVKAVGQRLSGQSAISTQPDAVKQQLEETSEIRSDLGQLDDEMKEAQTLCQELSLLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDEKQSQQAKNCPISAKLERLQSQLQENEEFQKNLNQHSGSYEVIVAEGESLLLSVPPGEEKKTLQNQLVELKSHWEDLNKKTVDRQSRLKDCMQKAQKYQWHVEDLVPWIKDCKSKMSELQVTLDPVQLESSLLRSKAMLNEAEKRRSLLEILNSAADILINSSEIDEDEIRDEKAGLNQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLKAQREVLQALDPQVDYLRDFTRGLVEDAPDGSDASPLVHQAELAQQEFLEVKQRVNSSCLTMENKLEGIGQFHCRVREMFSQLADLDDELDGMGAIGRDTDSLQSQIEDIRLFLNKIQALRLDIEDSEAECRKMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYSKLKALNDAATAAEEGEALQWIVGTEVDVINQQLADFKMFQKEQVDPLQVKLQQVNGLGQGLIQSAGKTCDVQGLEHDMEEVNTRWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLTDTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQAAELADREKITGQLESLECRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIHQQIIRHKALEEEIENHAADVQQAVKIGQSLSSLICPAEQGIMSEKLDSLQARYSEIQDRCCRKASLLEQALFNARLFGEDEVEVLNWLAEVEDKLSAVFVKDYRQDVLQKQHADHLALNEEIINRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFHSTYEELTGWLREVEEELAASGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSHALLELVPWRAREGLDKLVSDANEQYKLVSDTVGQRVDEIDAAIQRSQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRGEIFSTCGEEQKAVLQEKTECLIQQYEAVSLLNSERYARLERAQVLVNQFWETYEELSPWAEETLALIAQLPPPAVDHEQLRQQQEEMRQLRESIAEHKPHIDKILKIGPQLKELNPEEGKMVEEKYQKAENMYAQIKDEVRQRALALDEAVSQSAQIAEFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNKSATMELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFFWEDIKARSEEREIKFLDVLELAEKFWYDMAALLTTIKDTQEIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVKKSIDEMNNAWENLNRTWKERLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIRLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEELMGWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTLQQAQGFHSEIEEFLLELNRMESQLSASKPTGGLPETAREQLDAHMELHSQLRAKEEIYNQLLDKGRLMLLSRGDSGSGSKTEQSVALLEQKWHVVSSKVEERKSKLEEALSLATEFQNSLQEFINWLTLAEQSLNIASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWKKLIDWLEDAESHLDSELEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTLLADDAQKLDNLLGEVRDKWDTVCGKSVERQHKLEEALLFSGQFMDALQALVDWLYKVEPQLAEDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIESSRDDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQALKQAEEFRDTVHMLLEWLSEAEQTLRFRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNAAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELLAWIQWAETTLIQRDQEPIPQNIDRVKALITEHQSFMEEMTRKQPDVDRVTKTYKRKNIEPTHAPFIEKSRSGSRKSLNQPTPPPMPILSQSEAKNPRINQLSARWQQVWLLALERQRKLNDALDRLEELKEFANFDFDVWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALHPNKDAYRPTTDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRARGRTNIELREKFILPEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR
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F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity).
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D3ZI76
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GPAT2_RAT
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Glycerol-3-phosphate acyltransferase 2, mitochondrial (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase GPAT2) (EC 2.3.1.51)
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METMLKSNPQMQQRNNHSGQETSLWSSGFGMKMEAITPFLGKYRPFMGRCCQTCTPKSWESLFHRSIMDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPTSSDASQMIMENTGVQNILLGKVPGAAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEANLSLDSSEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPGPRLSALGQAWLGLVVQAVQAGIVPDATLVPVATAYDLVPDAPCNMTHDLAPLGLWTGALAIFRRLCNCWGCNRRVCVRVHLAQPFSLQEYTINARSCWGSRQTLEHLLQPIVLGECSVVPDTEKEQEWTPPTSLLLALKEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRVHQGDLVVVPRPGPGLTHLARLSMELLPTFLSEAVGACAVRGLLAGRVPPEGPWELQGIELLSQNELYRQILLLLHLLPQDLLLPQPCQSSYCYCQEVLDRLIQCGLLVAEETPGSRPACDTGRQHLSAKLLWKPSGDFTDSESDDFEEPGGRCFRLSQQSRCPDFFLFLCRLLSPILKAFAQAATFLHLGQLPDSEVGYSEKLLQFLQACAQEEGIFECADPNLAISAIWTFKDLGVLQQIPSPTGPQLHLSPTFASRDNQDKLEQFIRQFICS
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Transfers an acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate producing a lysophosphatidic acid (LPA), an essential step for the triacylglycerol (TAG) and glycerophospholipids. In vitro also transfers an acyl-group from acyl-ACP to the LPA producing a phosphatidic acid (PA). Prefers arachidonoyl-CoA as the acyl donor. Required for primary processing step during piRNA biosynthesis. Molecular mechanisms by which it promotes piRNA biosynthesis are unclear and do not involve its acyltransferase activity.
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D3ZIE4
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FYB1_RAT
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FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein)
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MDGKTDVKSLMAKFNTGSNPTEEVSTSSRPFKVAGQNSPSGIQSKKNLFDNQGNASPPAGPSNMSKFGTTKPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPEDKDHGTPSSPFAGVVLKPAASRGSPGLSKNSEEKKEERKTDIPKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKDSATPKQKPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNIKPPLDLKHPINEENQDGVMHSDGTGNLEEEQESDGEMYEDIESSKERDKKREKEEKKRLELERKEQKEREKKEQELRKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVKIDYDSLKRKKNTINAVPPRPVEEDQDVYDDVAEQDAPNSHSQSGSGGMFPPPPADDDIYDGIEEEDADDGSVPQVDEKTNAWSWGILKMLKGKDERKKSIREKPKVSESDSNEGSSFPSPHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGKTKAEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
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Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
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D3ZJ25
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AAAT_RAT
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Neutral amino acid transporter B(0) (ATB(0)) (ASC-like Na(+)-dependent neutral amino acid transporter ASCT2) (Insulin-activated amino acid transporter) (Sodium-dependent neutral amino acid transporter type 2)
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MAVDPPKADPKGVVAVDPTANCGSGLKSREDQGAKAGGCCSSRDQVCRCLRANLLVLLTVAAAVAGVVLGLGVSAAGGAEALGHARFTAFAFPGELLLRLLEMIILPLVVCSLIGGAASLDPSALGRLGAWALLFFLVTTLLSSALGVALALALKPGAAFAAINSSVVDSSVHRAPTKEVLDSFLELLRNMFPSNLVSASAAFRIFATSYVSKDINTSGIHPCGACPQRSNATMDQPHCEMKMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPIGILFLVAGKIVEMKDIRQLFIGLGKYIVCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEEKNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLNGMSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAISLPVKDISLILAVDWLVDRSCTVLNVEGDAFGAGLLQSYVDRTKMPSSEPELIQVKNDVSLKPLPLATEEGNPLLKQCREPSGDSSATCEKESVM
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Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (By similarity). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (By similarity). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (By similarity). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (By similarity).
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D3ZJ86
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SL9A6_RAT
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Sodium/hydrogen exchanger 6 (Na(+)/H(+) exchanger 6) (NHE-6) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 6)
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MTSPKPWARSAGSCQTQRAVRTRKKECREEGESDTEKGPAASSASAQCSFPKRVSFFGWAGALDSSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTCHVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFIAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGTSTEDALDRELTFGDHELVIRGTRLVLPMDDSEPALNSLDDTRHSPA
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Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo (By similarity). Plays a critical role during neurodevelopment by regulating synaptic development and plasticity (By similarity). Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH (By similarity). Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane (By similarity).
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D3ZJ96
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UBP28_RAT
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Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)
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MTAELQQDDAAGAADGHGSSCQMLLNQLREITGIQDPSFLHEALKASNGDITQAVSLLTDQRVKEPSHDTAATEPSEVEESATSKDLLAKVIDLTHDNKDDLQAAIALSLLESPNIQTDSRDLNRIHEANSAETKRSKRKRCEVWGENHNPNNWRRVDGWPVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNILENCRSHTEKRNIMFMQELQYLFALLLGSNRKFVDPSAALDLLKGAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSNPRTKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYHNLDECLEGAMVEGDIALLPSDRSVKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQVIYMDRYMYKSKELIRSKRESIRKLKEEIQVLQQKLERYVKYGSGPSRFPLPDMLKYVIEFASTKPASESCLSGSVEHMTLPLPSVHCPISDLTAKESSSPKSCSQNAEGSFSSPEDALPNSEVMNGPFTSPHSSLEMPAPPPAPRTVTDEEMNFVKTCLQRWRSEIEQDIQDLKNCISSTTQAIEQMYCDPLLRQVPYRLHAVLVHEGQASAGHYWAYIYNQPRQIWLKYNDISVTESSWEELERDSYGGLRNVSAYCLMYINDKLPHCSAEAAHGESDQTAEVEALSVELRQYIQEDNWRFEQEVEEWEEEQSCKIPQMESSPNSSSQDFSTSQESSAASSHGVRCLSSEHAVIAKEQTAQAIANTAHAYEKSGVEAALSEVMLSPAMQGVLLAIAKARQTFDRDGSEAGLIKAFHEEYSRLYQLAKETPTSHSDPRLQHVLVYFFQNEAPKRVVERTLLEQFADRNLSYDERSISIMKVAQAKLMEIGPEDMNMEEYKRWHEDYSLFRKVSVYLLTGLELFQKGKYQEALSYLVYAYQSNAGLLVKGPRRGVKESVIALYRRKCLLELNAKAASLFETNDDHSVTEGINVMNELIIPCIHLIINNDISKDDLDAIEVMRNHWCSYLGKDIAENLQLCLGEFLPRLLDPSAEIIVLKEPPTIRPNSPYDLCSRFAAVMESIQGVSTVTVK
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Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBXW7) complex. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells.
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D3ZJP6
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MYO10_RAT
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Unconventional myosin-X (Unconventional myosin-10)
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MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEQYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQHSLDLCLQEKSSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVIEAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQISFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHNQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHISSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRDLALPEDIRGKCTVLLQFYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKRFLHLKKAAIVFQKQLRGRLARKVYRQLLAEKRELEERKRLEEEKKREEEERERKRAQREADLLRAQQEAETRKQQELEALQKNQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGELSELAENASGEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASVQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRSAKEIIDNTNKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTLHTSVPPLEEVYSLQRLKARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGTVARQKVEEEQMLDMWIKEEICSARASIIDKWKKLQGVSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSLSSQGSSR
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts (By similarity).
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D3ZKB9
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TSH3_RAT
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Teashirt homolog 3 (Zinc finger protein 537)
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MAAYVSDELKAAALVEDDIEPEEQVADGEPSAKYMCPEKELSKACPSYQNSPAAEFSSHEMDSESHISETSDRMADFESSSIKNEEETKEVQVPLEDTTVSDSLEQMKAVYNNFLSNSYWSNLNLNLHQPSSENNGGGSSSSSSSSSSSCGSGSFDWHQSAMAKTLQQVSQNRMLPEPSLFSTVQLYRQSSKLYGSIFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNHETDNNNPKRWSKPRKRSLLEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVTPVAAKIIPAARKKPSLELELPSSPDSTGGTPKATLSDASDALQKNSNPYITPNNRYGHQNGASYAWHFEARKSQILKCMECGSSHDTLQELTAHMMVTGHFIKVTNSAMKKGKPIMETPVTPTITTLLDEKVQSVPLAATTFTSPSNTPASVSPKLTVEIKKEVDKEKAVLDEKPKEKEKASEEEEKYDISSKYHYLTENDLEESPKGGLDILKSLENTVTSAINKAQNGTPSWGGYPSIHAAYQLPNMMKLSLGSSGKSTPLKPMFGNSEIVSPTKTQTLVSPPSSQTSPMPKTNFHAMEELVKKVTEKVAKVEEKMKEPDSKLSPPKRATPSPCSSEQSEPIKMEASSGSGFKSQENSPSPPRDVCKEASPSAEPVENGKELVKPLSGGSLSGSTAIITDHPPEQPFVNPLSALQSVMNIHLGKAAKPSLPALDPMSMLFKMSNSLAEKAAVATPPPLQAKKAEHLDRYFYHVNNDQPIDLTKGKSDKGCSLGSGLLSPTSTSPATSSSTVTTAKTSAVVSFMSNSPLRENALSDISDMLKNLTESHTSKSSTPSSISEKSDIDGATLEEAEESTPAQKRKGRQSNWNPQHLLILQAQFAASLRQTSEGKYIMSDLSPQERMHISRFTGLSMTTISHWLANVKYQLRRTGGTKFLKNLDTGHPVFFCNDCASQIRTPSTYISHLESHLGFRLRDLSKLSTEQINNQIAQTKSPSEKMVTSSPEEDLGTTYQCKLCNRTFASKHAVKLHLSKTHGKSPEDHLLFVSELEKQ
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Transcriptional regulator involved in developmental processes. Functions in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter (By similarity). Involved in the modulation of glutamatergic synaptic transmission and long-term synaptic potentiation (By similarity).
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D3ZKD3
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ALKB5_RAT
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RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5)
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MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGTTKRKYQEDSDPERSDYEEHQLQKEEEARKVKSGIRQIRLFSQDECSKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSTLPPSYASDRLSGNTRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCPEAASSPTRKVKMRRH
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Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (By similarity). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro). Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export (By similarity). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity).
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D3ZKX9
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LOXE3_RAT
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Hydroperoxide isomerase ALOXE3 (Epidermis-type lipoxygenase 3) (Epidermal LOX-3) (e-LOX-3) (eLOX-3) (Hydroperoxy dehydratase ALOXE3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Hydroperoxy icosatetraenoate isomerase) (EC 5.4.4.7)
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MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCLNGRQQYVTAPLCLLWLNPQGVLLPLAIQLSQIPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRRGLIYLMSTGLAHFTYTDFCLPDSLRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPNDACVQQDSELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGNTTMESYLETLPEVNTTCSNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQKCLAQISKDIRARNESLALPYAYLDPPLIENSVSI
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Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia.
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D3ZLB7
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FOSB_RAT
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Protein FosB (Transcription factor AP-1 subunit FosB)
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MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTSTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGSQRTSGSEQPSDPLNSPSLLAL
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Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (By similarity). Exhibits transactivation activity in vitro (By similarity). As part of the AP-1 complex, facilitates enhancer selection together with cell-type-specific transcription factors by collaboratively binding to nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex to establish accessible chromatin (By similarity). Together with JUN, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Involved in the display of nurturing behavior towards newborns (By similarity). May play a role in neurogenesis in the hippocampus and in learning and memory-related tasks by regulating the expression of various genes involved in neurogenesis, depression and epilepsy (By similarity). Implicated in behavioral responses related to morphine reward and spatial memory (By similarity).
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D3ZLH5
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PLXB3_RAT
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Plexin-B3 (Protein Plxnb3)
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MLTDFLQAPVMAPWSPFSLHLLLLFLLLLPLTRAHRFSVPNASFNHLVLAPDQGKLYVGAVNHLFQLSPELEMESVAITGPVIDSPDCVPFRDLAECPQAQLTDNANQLLLVSSRAQELVACGQVRQGVCEKRRLGDVTQVLYQAEDPGDGQFVAANTLGVTTVGLVVPLPGRDLLLVARGLAGKLSAGVPPLTVRQLAGPQPFSSEGLGRLVVGDFSDYNNSYVGAFSDAHSAYFVFRRRGARAQTEYRSYVARVCLGDVNLYSYVEVPLTCHGQGLIQAAFLAPDTLLGAFSAGTSQAQAALCAFPLADLDGSMEQARRLCYTTGGQGPNGMEEATVEYGVTSRCVTLPPDSPESYPCGDEHTPSPIAGRQPLEAQPLLQLGQPISAVAALQTDGHTIAFLGDTEGQLHKVFLNSSHGQVYHSQQVGPPGSAISPDLLVDNSGDYLYVLTAQQVDRILVAACPQFPNCTTCLQARDPLCGWCILQGRCTRRAECGRAVQPNQWLWSYEDNHCLHIQSLLPAQHPRQEHGQITLSVPGLPNLAMDEYFYCAFGDYNSLAQVEEHHVVCATPPQDRMPPNPPGSDHVTLPLALMFEDVVLAATTFSFYDCSAIQALEVAAPCRTCVSSLWRCHWCPQSSHCVYGERCPEGEKAVYSAQEVDILVRGPEACPQVKGLASPQLVPVGWESHVTLHIENLHYFRGLPALYYCWLELPGKLRKLPAFLEETSRNSGLIHCQAQQFHPSMSQWELPVPIYVTRGEIQRLDNTGDLHVTLYDCAMGHPDCSHCQAANGSLSCLWCGDGQPACRYGPLCPPGAVEQLCPIPSIDVIEPLTGPPEGGLAITILGSNLGQAFNDVRNAVTVAGQPCNPDPSLYRISARIVCVTSPAPNGTSGPVQVAIKSRPPGISAQHFTYQDPVLLSLNPQWGPQAGGTQLTIHGQYLQTGGNVSAFVGDQPCPIQEPVCPEAIICHTMPQMEPGEAVVFVVFGHVERKLLTTPFRYTANPQLVEAEPSVSFRGGGRVIRVRGTGLDVVWQPLLSVWLEDEFQVKALGVQAQDVNPRRSCGAPAADPQACIHLESGLLQCSTLCSVNSSSLLLCHSPAVPDGALPKRVFFALDNMQVDFASASGGQGFLYQPNPRLAPLSHEGITHPYRLKPGHVLDVEGEGLNLGISKEEVQVHIGDGKCLVKTLTLTHLYCEPPQQAPQPTNGSGTLPQFVVQMGNVRLALGPVQYEAEPMISTFPVEAQVGLGMGAAMLIAAVLLLTLMYRHKSKQALRDYQKVLVQLENLETGVGDQCRKEFTDLMTEMTDLTSDLEASGIPFLDYRTYAERAFFPGHVGCPLQPGLEGPGEEGRRVTVCQGLTQLSNLLNSKLFLLTLIHTLEEQPSFSQRDRCHVASLLSLALHSKLEYLTDIMRTLLGDLAAHYVHKNPKLMLRRTETMVEKLLTNWLSICLYAFLKEVAGEPLYMLFRAIKYQVDKGPVDAVTGKAKRTLNDSHLLREDVEFRPLTLMALVGPGAGGAAGNSEVHRVPARVLDTDTITQVKEKVLDQIYKGTPFSQRPSVHSLDLEWRSGLAGHLTLSDEDLTSVTQNHWKRLNTLQHYKVPDGATVVLIPQLHNGGTVSQSLEQTGCHSGENTPMLEDGEEGGVRLWHLVKATEETEGAKVRRSSLRERERERARAKAIPEIYLTRLLSMKGTLQKFVDDTFQAILSMNRPVPIAVKYLFDFLDELAEKHGIEDPETLHIWKTNSLLLRFWVNALKNPQLIFDVRVSDNEDAILAVIAQTFIDSCMVSEHKVGRDSPVNKLLYAREIPRYKQMVEKYYADIRQSSPASYQEMNSALAELSGNYTSAPNCLEALRELYNHIHRYYDQIISALEEDPVAQKMQLACRLQQVAALVEYKVTDL
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Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1.
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D3ZMK9
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PRAG1_RAT
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Inactive tyrosine-protein kinase PRAG1 (PEAK1-related kinase-activating pseudokinase 1) (Pragma of Rnd2)
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MSACSDFVEHIWKPGSCKNCFCLRSDHQLTAGHPKARASSLPAGARLPARPEICRLEDEGVNGLAYSKPTIAVKPTMMTSETADLWTEASLSAEVPKVNWRRTPGKLLLQKQEDGPIVYLGSFRGMQKAAGPLACTDSNSRCPPAYTMVGLHNLEARVDRNTALQPVNFQEEKAGREELPSAQESFRQKLAAFTGMTSSCLKGPRPCTSPQPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCRPESRDAVHNTEGSGRRRGDCSPICWEQGTCTRPTEEEKQALNFPRECCGQGSTANPPHLGPKKPSLNSEAASSSDGLSCGSSRSGANSPFAPHLENDYCSLVKEPTSVKQQDSGCHLVNSGKYVGQAVDLQPPALPREAVQPEPIYAESAKRKKAAPVPQRPEPKKEQVSSGQVWTGDTWSQKTPSGWSQEREGPNAAPQVATTITVIAAHPEEDHRTIYLSSPDSAVGVQWPRGSLNQDLHGSGEEPLVVQGLSSRESHPHNMTENSSKEKPAIPPKLSKSSPGGSPVSPAAPPLTDHSDGNTSGSSVGSQPSSRVPTNLTSSCQTNGVAAGDPAKCPPQANSSVLDQRRPRYQTGAWSRQCRIEEEEEVGQELLSQSWGRELENGIADHSNSSTWHRLHPIDGASGQNGKTNSGMSKSASFAFEFPKDRGRLESFSPPPPPPKSRHLLKMNKSSSDLEKVSQSSAESLSPSFRGAHVSFTTGSTDSLASDSRTCSDGGPSCEATHSPTISGKKLFAPVPFPSGSTEDVSPSGPAQPPPLPQKKIVSRAASSPDGFFWTQGSPKPRTASPKLNLSHSETNVCAHDEPPLSYSLNSGNHPHHVFSSSEPLEKAFKGSVPWAPALGPANSKGGCGSPNLQGRAATSTSSSQLSVSSQASTGSSQLQLHSLLSSISSKEGTYAKLGGLYTQSLARLVTKCEDLFMGGLKTELRFDENSWSLFKLICNKPCCDSGDAIYYGATCSKDPDSIYAVKICKTPEPKSASYCSPSVPVHFNIQQDCGHFVASVPSSMLAFPDTSSKDPAPAAPSHTPAQEQDCVVVITREVPHQTASDFVRDSVASHRAEPEVYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCNPQSSPGPSANPSVPTTTSRCPSAAPAATTACQGGPGEKHLPRLIISNFLKAKQKPGGTTNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRREDLPPLPTLSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVEQPCPSEEVLCNTLHNWIDMKRALMMMKFAEKAVERRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL
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Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth. Promotes Src family kinase (SFK) signallig by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism. Acts as a critical coactivator of Notch signaling (By similarity).
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D3ZML2
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BRSK2_RAT
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Serine/threonine-protein kinase BRSK2 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 2) (BR serine/threonine-protein kinase 2) (Serine/threonine-protein kinase SAD-A)
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MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELGHLQLFGNPVSKVRSVAMELVILVQTLAYTSFRLLGTFLPVRYLRHSVLSRPPERARLVLRGAPCTHMGPVWNMVGMAYTQNPPIMGETGVYGSQWVMSSAPSKHYTSLGLSVPSPSCSLSPSLFPFCAPDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP
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Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-175 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-261 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress (By similarity).
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D3ZMM8
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YLAT2_RAT
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Y+L amino acid transporter 2 (Solute carrier family 7 member 6) (y(+)L-type amino acid transporter 2) (Y+LAT2) (y+LAT-2)
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MEARELGSPTPTYHLLPKANQHTVKEDASSPSQGSPETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLKYTASYGLSLVVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLIVEPTSQAIIAITFANYIIKPSFPTCDPPYVACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQGHTEHFQDAFKGSSWNVGDLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNIQDVHKSDAVAVTFADQTFGMFSWTIPIAVALSCFGGLNASIFASSRLFFVGSREGHLPNLLSMIHIERFTPVPALLFNCTMTLIYLVVKDVFLLINYFSFSYWFFVGLSVVGQLYLRWKEPDWPRPLKLSLFFPIVFCICSLFLVAVPLFSDTINSLIGIGIALSGVPVYFMGVYLPEARRPLFIRKVLATVTRVTQKLCFCVLTELDVAEEKNVERKTD
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Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux routeby exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis. Also exchanges L-arginine with L-lysine in a sodium-independent manner. The transport mechanism is electroneutral and operates with a stoichiometry of 1: 1 (By similarity). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration. May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (By similarity). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity).
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D3ZMY7
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5NTC_RAT
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Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (EC 3.1.3.99) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77)
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MMTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLNFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE
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Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (By similarity). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (By similarity). Through these activities regulates the purine nucleoside/nucleotide pools within the cell.
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D3ZN95
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HCFC1_RAT
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Host cell factor 1 (HCF) (HCF-1) (C1 factor) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6]
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MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIETLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLVPQAAAAPPSTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPASVRMVVPTQSAQGTVIGSNPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTVAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSAANTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGAHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQEAAASLVTSAVGQQNGNVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTSTATTAMSSMGTGQQRDARRATNTPTVVRITVAPGALERAQGTVKPPCQTQQTNMTSTTMTVQATGAPCSAGPLLRPSVALETGSHSPAFVQLALPSVRVGLSGPSSKDVPTGRQPETYHTYTTNTPTTARSIMVAGELGTARVVPTSQYDCLQASSPSSTMTMTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGAGQPEGGQQPASGHPCETHQTTSTGTTMSVSVGALIPDATPSHGTLESGLEVVAVPTVTSQAGATLLASFSTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVASTQGDSTNITSASAITTTVSSTLPRAVTTVTQSTPVPGPSVPPPEELQVSPGPRQQLPPRQLLQSASTPLMGESAEVLSASQTPELQAAVDLSSTGDPSSVQEPTTSAVVATVVVQPPQPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMGTGEPMDTSEAAAAVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQQLQEAQAQAQQQHHLPTEALAPADSLNDPSIESNCLNELASAVPSTVALLPSTATESLAPSNTFVAPQPVVVASPAKMQAAATLTEVANGIESLGVKPDLPPPPSKAPIKKENQWFDVGVIKGTSVMVTHYFLPPDDAVQSDDDSGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQASGEPKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPASKRPMSSPEM
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Transcriptional coregulator. Involved in control of the cell cycle (By similarity). Also antagonizes transactivation by ZBTB17 and GABP2 represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By similarity). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together (By similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). Modulates expression of homeobox protein PDX1, perhaps acting in concert with transcription factor E2F1, thereby regulating pancreatic beta-cell growth and glucose-stimulated insulin secretion. May negatively modulate transcriptional activity of FOXO3.
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D3ZPG5
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UBP30_RAT
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Ubiquitin carboxyl-terminal hydrolase 30 (EC 3.4.19.12) (Deubiquitinating enzyme 30) (Ubiquitin thioesterase 30) (Ubiquitin-specific-processing protease 30) (Ub-specific protease 30)
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MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLSLLKALSCQEVTEEEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNPWKSQHPFHGRLSSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTQNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSQGTPLKRHEHVQFNEFLMMDFYKYRLLGHKPSQHGPKATESPGSALGVQDTQAAPKPGLSQPAAPKTQFFMNGACSPSLLPALPSPMAFPLPVAPDYSSSMYLFRLMAVVVHHGDMHSGHFVTYRRSPPSAKNPLSTSNQWLWISDDTVRKASLQEVLSSSAYLLFYERVLSRVQQQGREYRSEE
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Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (By similarity). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity).
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D3ZPX4
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PLXA3_RAT
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Plexin-A3
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MHTVCLLPLLFFTIGGCLGSSRPFRTFVVTDTTLTHLAVHRVTGEVFVGAVNRVFKLASNLTELRAHVTGPIEDNARCYPPPSMRVCSHRLVPVDNVNKLLLIDYAARRLVACGSIWQGICQFLRLDDLFKLGEPHHRKEHYLSGAQEPDSMAGVIVEQGQGPSKLFVGTAVDGKSEYFPTLSSRKLIDDEDSGDMFSLVYQDEFVSSQIKIPSDTLSLYPAFDIYYIYGFVSASFVYFLTLQLDTQQTLLDTAGEKFFTSKIVRMCAGDSEFYSYVEFPIGCSWRGVEYRLVQSAHLAKPGLLLAQALGVPADEDVLFTIFSQGQKNRANPPRQTILCLFTLSSINAHIRRRIQSCYRGEGTLALPWLLNKELPCINTPMQINGNFCGLVLNQPLGGLHVIEGLPLLADSTDGMASVAAYTYHQHSVVFIGTRSGNLKKVRVDGSQDAQLYETVSVVQGTPILRDLLFSPDHRHIYLLSEKQVSQLPVETCEQYLSCAACLGSGDPHCGWCVLQHRCCREGACPGASAPHGFAEELNKCIQVRVRPNNVSVTSSGVQLTVAMRNVPDLSLGVSCSFEEVTESEAILLPSGELRCPSPSLQELQTLTRGHGATHTVRLQLLSMETGVRFAGVDFVFYNCSALQSCMSCVGSPYPCHWCKYRHVCTSHPHECSFQEGRVHSPEGCPEILPRGDLLIPVGVMQPLTLRAKNLPQPQSGQKNYECVVRVQGRQHRVPAVRFNSSSVQCQNASYFYEGDEFGDTELDFSVVWDGDFPIDKPPSFRALLYKCWAQRPSCGLCLKADPRFNCGWCISEHRCQLRVHCPAPKSNWMHPSQKGARCSHPRITQIHPLTGPKEGGTRVTIVGENLGLTSREVGLRVAGVRCNSIPTEYVSAERIVCEMEESLVPSPPPGPAELCVGDCSADFRTQSQQLYSFVTPTLDRVSPTRGPASGGTRLTISGTSLDAGSRVTVIIRDGECQFVRRDAEAIVCISPISTLGPSQAPIILAIDHANISSTGVIYTYTQDPTVTHLEPTWSIINGSTSITVSGTHLLTVQEPRVRAKYRGIETTNTCQVINDTAMLCKAPGIFLGHPQPRAQGEHPDEFGFLLDHVQAARSLNRSSFTYYPDPSFEPLGPSGVLDVKPGSHVVLKGKNLIPAAAGSSRLNYTVLIGGQPCALTVSDTQLLCDSPSQTGRQPVMVLVGGLEFWLGTLHITADRALTLPAMVGLAAGGGLLLLAITVVLVAYKRKTQDADRTLKRLQLQMDNLESRVALECKEAFAELQTDINELTNHMDGVQIPFLDYRTYAVRVLFPGIEAHPVLKELDTPPNVEKALRLFGQLLHSRAFLLTFIHTLEAQSSFSMRDRGTVASLTMVALQSRLDYATGLLKQLLADLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLHKFLKECAGEPLFLLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLHCVCPESEGSAQVPVKVLNCDSITQAKDKLLDTVYKGIPYSQRPKAEDMDLEWRQGRMARIILQDEDITTKIECDWKRINSLAHYQVTDGSLVALVPKQVSAYNMANSFTFTRSLSRYESLLRAASSPDSLRSRAPMLTPDQEAGTKLWHLVKNHDHADHREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETVFSTAHRGSALPLAIKYMFDFLDEQADQRQISDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPNYKSWVERYYRDIAKMASISDQDMDAYLVEQSRLHANDFNVLSALSELYFYVTKYRQEILTSLDRDASCRKHKLRQKLEQIITLVSSSS
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Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity).
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D3ZQF4
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FKBP6_RAT
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Inactive peptidyl-prolyl cis-trans isomerase FKBP6 (Inactive PPIase FKBP6) (36 kDa FK506-binding protein) (FK506-binding protein 6) (Immunophilin FKBP36)
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MSVFSRLRNGIPPSRDDCQSPYERLSQRMLDISGDRGVLKDIIREGAGDPVTPDASVLVKYSGYLEHMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPTYAYGTLGCPPLIPPNATVLFEIELIDFLDSAESDKFCALSAEQQEQFPLQKVLKVAATEREFGNYLFRQNRFCDAKVRYKRALLLLHRRLAICEEQHLVEPAELLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYEQARDFLVRAQKEQPCNHDINNELKKLSSHYRDYVDREREMCHRMFAPCGSGSSVGGN
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Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity).
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D3ZQF9
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LX12E_RAT
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Polyunsaturated fatty acid (12S)/(13S)-lipoxygenase, epidermal-type (EC 1.13.11.-) (Arachidonate (12S)-lipoxygenase, epidermal-type) (12-LOX-e) (e(12S)-LOX) (EC 1.13.11.31) (Linoleate (13S)-lipoxygenase)
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MGKYKILVVTGDSLLAGSTNLVQLWLVGEHAEADLGKQLRPLRGRKTELEIDVPLHLGRLLVVKLRKHKGLLDSDWFCKWITVQGPGIQGEAFFPCYSWVQGKETIYLPEGTALKVNDDTKNLFRKYREQELEDRRNVYRWGSWKEGLILPIAGSTERDLPRNQRFMEDKDLDFSLSLAKVLKDFAIKGTLDFVSRVQHLEDYQKVFPHSKTALAGRVRDSWKEDALFGYQFLNGANPMLLRRSKRLPARLVLPPGMEDLQTQLEKELKAGSLFEADFSLLDGVKPNVIIFKQQHVAAPLVMLKLQSDGRLLPMVIQLQPPRHGCPPPLLFLPSDPPMAWLLAKIWVRSSDFQVHQLQSHLLRGHLMAEVISVATMRSLPSLHPIYKLLAPHFRYTMEINTLARNNLVSEWGIFDLVVSTGSGGHVDILQRATACLTYRSFCPPDDLADRGLLDVKSSLYARDALRLWEIISRYVGRMVELFYKNDREVKEDPELQVWCREVTEIGLLGAQDRGFPLSLESRAQLCRFVTMCIFTCTGQHASTHLGQLDWYSWIPNGPCTMRKPPPTSKNVTEGDILDALPCLQQARMQITFTKFLGRHQPVMVALGQHKEEYFSDPGARAVLKQFQEELAVMDKEIEVRNASLDLPYEYLRPSMVENSVTI
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Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Shows increasing catalytic activity within the series arachidonic acid < 5,8,11-eicosatrienoic acid < linoleic acid < 8,11,14-eicosatrienoic acid (By similarity).
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D3ZQL6
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MILK1_RAT
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MICAL-like protein 1
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MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFQSLSKENVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFTSSGQAAASPPKPGKDPAAPSPTSTSPAVQPGEEAQGDDLSPDSLSEQGKPQPPSSACAACGQRVHLVQRYLAEGRLYHRHCFRCRQCSSTLVPGSYSSGPEEGTFVCAERCTRLGLGGRSGTRPLSLQKQQPAAAAEAKDGEDSDLSKSVVVVAAEADGLQASSEVQPHTLTKPPLPSKPQDLASPPVSRPTPAPRKASESSALTPPTPRPRSSLQQDGMVEQSVSGDLVNGRLQELPVPKPRGTPKLSERMTAPRKDPPWITLVQTEPKKKPAPLPPSSGPGPLSQASRQVENGGLEEKTQKSPAAEPEPKPYNPFEEEEEEEEASVPAVPSPAPAPPETTPKSLHPWYNITPTSSPKTKKRPAPKAPSASPLVLHASRLSHSEPPSATPSPALSVESLSSESSSHTANTEPSEPPAVPKSSSDPAVHVPGTPGTSANSVTPSAHSSLSSSGELGQPSGEQMPQARTRGSPGTHSTKPFSGATPTPFLLAGDQKSPAPPMGSSSPQMLIKSSCKENPFNRKPSPSTSPTVRKATKGAKPVRPPAPGHGFPLIKRKVQADQYIPEEDIYGEMDSIERQLDALEHSGVLLEEKLRGGANEGSEDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEFELRCLLNKPEKDWTDDDRAREKVLMQELMTLIEQRDAIVNCLDEDRQREEEEDKMLETMIKKKDFQREAESDSKKKGKFKTMKVLKLLGNKRDAKSKAPTGKS
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Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.
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D3ZQL7
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TPPP_RAT
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Tubulin polymerization-promoting protein (TPPP) (EC 3.6.5.-) (25 kDa brain-specific protein) (TPPP/p25) (p25-alpha)
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MADSKAKPTKAANKTPPKSPGDPAKAAKRLSLESEGANEGAAAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK
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Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath. Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (By similarity). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity). Shows magnesium-dependent GTPase activity the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (By similarity). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis this process is regulated by phosphorylation by LIMK2 (By similarity).
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D3ZR10
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DCDC2_RAT
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Doublecortin domain-containing protein 2
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MNGPSPRSSHLSQPVVKSVLVYRNGDPFFAGRRVVIHEKKVSSFDIFLKEVTGGVQAPFGAVRNIYTPRTGHRIRKLDQIESGGNYVAGGQEAFKKLNYLDIGEIKKRPMEAVNTEVKPVIHSKINVSARFRKALHEPCTIFLIANGDLISPASRLLIPRKALNQWDHVLQMVTEKITLRSGAVHRLYTLEGKLVESGAELENGQFYVAVGRDKFKRLPYSELLFDKSAMRRPYGQKASSLPPMVGSRKSKGSGNYRQSKSTIGSSDNSSPQPLKRKGKKDSNSEKPTKVKQSVKSKNSHQAIPDNDEGIFKAGAERSETRGAAEVQEDEDTQVEVPVDQRPAEIVDEEEDGEKTSKDANQKDDFSAMNGEAEDRAGSKVADAPEEEEGIPDQGEKKASPSRVNGGTDEENGEELDQVTEELQPTVDEKGKAEGDNSAQDEAGLDAQRPPRPEVTVTSPQENEGNESNKASSAVA
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Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex. Involved in the control of ciliogenesis and ciliary length (By similarity).
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D3ZRC4
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PLPL8_RAT
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Calcium-independent phospholipase A2-gamma (EC 3.1.1.-) (EC 3.1.1.5) (Intracellular membrane-associated calcium-independent phospholipase A2 gamma) (iPLA2-gamma) (Patatin-like phospholipase domain-containing protein 8)
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MSINLTLDIYIYFLNNARSFCGKQRSKQLNFLCSKQYWRMNHVNVHREFHTSKKSCKWNRSEAHCSKHWHSSSNHGVHIGIVKLSTSAPKGLTKVSIHMSRIKSTLNSVSKAIFGSQNEMVSRLAQFKPSSRIFRKVSDRGWLKHKNVKQAIESLKNYSDKSAEKNSFAEQKSYFADKEEGSDKHSLYHYAYRITTRFGESFYFLANHINSYFKNKEKMSQIKEDRQLQDKPCLEESKSISPSPDILTDRPDSGPPLNVEDKLSSSTQLPEALPVSTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKSDPKSQPEEEEEPSKTDEPICKDKKAEEKKRVLLQREKIIARVSIDNRTRALVQALRRTTDPKLCITRVEELTFHLLEFPEGKGVAVKEKIIPYLLRLRQIKDETLQAAVREILALIGYVDPVKGRGIRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTQNVIVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGQTPKAFVFRNYGHFPGTNSHYLGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTTTYTSLKTKLSNVISSATDTEEVHIMLDGLLPADTYFRFNPVICENIPLDESRNEKLDQLQLEGMKYLERNDEKMKKLAKILSREKTTLQKISDWIKLKSDMYEGLPFFSKL
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Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors. Hydrolyzes phosphatidylethanolamine, phosphatidylcholine and probably phosphatidylinositol with a possible preference for the former. Has also a broad substrate specificity in terms of fatty acid moieties, hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal rates from either the sn-1 or sn-2 position in diacyl phosphatidylcholine. However, has a weak activity toward polyunsaturated fatty acids at the sn-2 position, and thereby favors the production of 2-arachidonoyl lysophosphatidylcholine, a key branch point metabolite in eicosanoid signaling. On the other hand, can produce arachidonic acid from the sn-1 position of diacyl phospholipid and from the sn-2 position of arachidonate-containing plasmalogen substrates. Therefore, plays an important role in the mobilization of arachidonic acid in response to cellular stimuli and the generation of lipid second messengers. Can also hydrolyze lysophosphatidylcholine. In the mitochondrial compartment, catalyzes the hydrolysis and release of oxidized aliphatic chains from cardiolipin and integrates mitochondrial bioenergetics and signaling. It is essential for maintaining efficient bioenergetic mitochondrial function through tailoring mitochondrial membrane lipid metabolism and composition.
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D3ZS74
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OMA1_RAT
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Metalloendopeptidase OMA1, mitochondrial (EC 3.4.24.-) (Overlapping with the m-AAA protease 1 homolog)
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MNFLYGLQSATRNQFLSGVNTLARRRTWTPPAGCPLASRLPAVNANWGLSTVSHCYSVILLPRNLHFCRTLKNKRSRCLSSAQSKEMGVLTYNWTVWGDASCSPNYAAIREVRSFHTSAPRQAAPVPLLMLILKPVQKLLAIIVGRGIRKWWQALPPDKKALFKDSVKRNKWRLLLGLSAFGLLFVVFYFTHLEVSPVTGRSKLLLVGKEHFRLLSDLEYEVWMEEFKNDLLPEEDPRYLTVKKVVYHLTQCNQDVPGVSEINWVVHVVHSPKVNAFVLPNGQVFVFTGLLNSVTDMHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLGMIFLTMIWAICPRDSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKIGLQLAAKACVDVRASSVFWQQMEFSESLHGYPKLPEWLSTHPSHGNRAEYLDRLIPQALKLREVCNCPPLSGPDPRLLFRLTVKHLLEDSEKEDLNITVKKQKPDALPIQKQEQIPLTYALGKRTAG
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Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion (By similarity). Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae. In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome. May also cleave UQCC3 in response to mitochondrial depolarization. Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (By similarity). Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Binds cardiolipin, possibly regulating its protein turnover. Required for the stability of the respiratory supercomplexes (By similarity).
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D3ZSI8
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PI51A_RAT
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Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha)
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MASASSGPAAAGFSPLDSGVPAGTAASGIKRGTVSEGPYASLMPVKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQREPMNSETQYSIDTRRPAPQKALYSTAMESIQGEARRGGTVETEDHMGGIPARNNKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPTKKFRSGPSFSRRSGPSGNSCTPSQPTASGEHKAQVTTKAEVEPDIHLGRPDVLPQTPPLEEISEGSPVPGPSFSPAVGQPLQILNLSSTLEKLDVAESELTH
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Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (By similarity). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps. Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (By similarity). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes. Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane. Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (By similarity).
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D3ZSZ3
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NLK_RAT
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Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase)
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MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
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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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D3ZTD8
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SEM5A_RAT
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Semaphorin-5A (Semaphorin-F) (Sema F)
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MKGACILAWLFSSLGVWRLARPETQDPAKCQRAEHPVVSYKEIGPWLREFRAENAVDFSRLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVQWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTIRSLSNLTEIHDQISGMARCPYSPQHNSTALLTASGELYAATAMDFPGRDPAIYRSLGTLPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGRDTLVHIIYLATDYGTIKKVRAPLSQSSGSCLLEEIELFPERKSEPIRSLKILHSQSVLFVGLQEHVVKIPLKRCHFHQTRGACIGAQDPYCGWDAVMKKCTSLEESLSMTQWDQSVPTCPTRNLTVDGSFGPWSPWTPCTHTDGTAVGSCLCRSRSCDSPAPQCGGWQCEGPRMEITNCSRNGGWTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHLLCPPHVFWTGWGPWERCTAQCGGGIQARRRTCENGPDCAGCNVEYQPCNTNACPELKKTTPWTPWTPVNISDNGGHYEQRFRYTCKARLPDPNLLEVGRQRIEMRYCSSDGTSGCSTDGLSGDFLRAGRYSAHTVNGAWSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEFQECNILPCPVDGVWSCWSSWSKCSATCGGGHYMRTRSCTNPAPAYGGDICLGLHTEEALCNTQTCPENWSEWSEWSVCDASGTQVRTRQCILLFPVGSQCSGNTTESRPCVFDSNFIPEVSVARSSSVEEKRCGEFNMFHMMAVGLSSSILGCLLTLLVYTYCQRYQQQSHDATVIHPVSPAALNSSITNHINKLDKYDSVEAIKAFNKNNLILEERNKYFNPHLTGKTYSNAYFTDLNNYDEY
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Bifunctional axonal guidance cue regulated by sulfated proteoglycans attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis.
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D3ZTE0
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FA12_RAT
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Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Coagulation factor XIIa light chain]
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MTALLFLGSLLMSLDLTLSAPPWKSKEFKDGAGDPSVVLTVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYCLEPKKVKDHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQREKCFESQLLKFFHENEIWFRTGPGGVARCQCKGPQAVCKLLTSQVCRVNPCLNGGTCLLVEDHRLCHCPAGYAGPFCDLDLKATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDNDTRPWCYVWSGDRLSWDYCDLEQCQMPTLTSPVSPESHDMLKPRPPILQSSPRDSTRNQNVVSRTSTVVCGQRFRKRLSSLRRVVGGLVALPGSHPYIAALYWGDSFCAGSLIDPCWVLTAAHCLQKRPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLHEGFSSKTYQHDLALLRLRGRKNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLDRCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQEHTAF
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Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity).
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D3ZTL1
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PO4F3_RAT
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POU domain, class 4, transcription factor 3
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MMAMNAKQPFGMHPVLQEPKFSSLHSGSEAMRRVCLPAPQLQGNIFGSFDESLLARAEALAAVDIVSHGKNHPFKPDATYHTMSSVPCTSTSPTVPISHPAALTSHPHHPVHQGLEGDLLEHISPTLSVSGLGAPEHSVMPAQIHPHHLGAMGHLHQAMGMSHPHAVAPHSAMPACLSDVESDPRELEAFAERFKQRRIKLGVTQADVGAALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPVLQAWLEEAEAAYREKNSKPELFNGSERKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAVH
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Acts as a transcriptional activator. Acts by binding to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Involved in the auditory system development, required for terminal differentiation of hair cells in the inner ear.
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D3ZTT2
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LYPD6_RAT
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Ly6/PLAUR domain-containing protein 6
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MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL
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Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).
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D3ZTV3
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FLRT2_RAT
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Leucine-rich repeat transmembrane protein FLRT2 (Fibronectin-like domain-containing leucine-rich transmembrane protein 2)
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MGLQTAKWPSHGTFVLKFWLIMSLGLYSHVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIADGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANLRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNMNLLSCPTTTPGLPVFTPAPSTVSPTTQSPTVSVPSPSRGSVPPAPAPSKLPTIPDWDGRERATPPISERIQLSIHFVNDTSIQVSWLSLFTVMAYKLTWVKMGHSLVGGIVQERIVSGEKQHLSLVNLEPRSTYRICLVPLDAFNYRTVEDTICSEATTHASYLNNGSNTASSHEQTTSHTMGSPFLLAGLIGGAVIFVLVVLLSVFCWHMHKKGRYTSQKWKYNRGRRKDDYCEAGTKKDNSILEMTETSFQIVSLNNDQLLKGDFRLQPIYTPNGGINYTDCHIPNNMRYCNSSVPDLEHCHT
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Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis.
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D3ZU57
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RIOX1_RAT
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Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Histone lysine demethylase NO66)
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MDELPNGNGAAPLKRGRGRRRRQPQPRGASVLALPLRPRKVRRHRKSAASRVAALRARALLSEDSDSNVESVRGKRERPAELPEASRSAEPRPVPVRPRPASATLPRRVEGRAALSRNLGKPAPLPGSHVDDPERPWDSPLQQVLAELNGIPSSRRRAARLFEWLLAPLPPDHFYRRLWEREAVLVRRQDHSYYEGLFSTSDLDWMLRYEDVHFGQHLDAARYIDGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSPTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRDPSEELALTSSPNFSQEDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAVLPLAMQAAIEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVHGLPIRWEAGEPVNVGAQLTTETQVHMLQDGIARLVGEGGRLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLRSYPEFVRVGDLPCDSVEDQLSLATMLYDKGLLLTKTPLVLS
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Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis. Participates in MYC-induced transcriptional activation (By similarity).
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D3ZUA0
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MTD2L_RAT
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Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial (NADP-dependent methylenetetrahydrofolate dehydrogenase 2-like protein) (MTHFD2-like) [Includes: Methylenetetrahydrofolate dehydrogenase, mitochondrial (EC 1.5.1.15) (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase, mitochondrial (EC 3.5.4.9)]
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MATRARGLSLLRGRLGRGPARAPGVAERAWRGFGSSSRRHEAVIISGTEMAKQIRRELQQGVESWLALGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELIVKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRHTPREQLKAHTQLAEIIIVAAGIPGLITADMVREGATVIDVGINYVQDPVTGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNITY
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[Isoform 1]: Bifunctional mitochondrial folate-interconverting enzyme that has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities.
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D3ZUE1
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GA2L2_RAT
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GAS2-like protein 2
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MSQHVGHGRKPRTPGPPVRSIRPFKSSEQYLEVMKEDLAEWLRDLYGLDIDAANFLRVLETGLVLCRHANTVTEAALAFLAEAPERVQKIPMPQVGVFCNGAAQPGTFQARDNISNFIQWCRKEMGIQEVLMFETEDLVLRKNVKSVVLCLLELGRRAWRFGVAAPSLVYLEEEIEEELRRDLDLPSPDPPPPVPPARRPCHFHNLDQMVQSLVSHCTCPVQFSMVKISDGKYRVGDSNTLIFIRILRSHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPGPPVQHEVKVQDGPSQPQPLMTISRSQSPLPPVDWKTYTSSSRKLRPPTPSSSGPRSEFPARARTPREMAPFLRSQEKPTLSQRMSSPGPQLSSPCRGPDLQSTLSERRVNRSPGELPRGRTPTSWVPKEADSQGAHTKAPIPQRLQIPETTSKKTPARGPSPPPRSSSLASPHTIWLPDQGASPEISEPMSAQSSSPGKGLTKIPIRLSPARPPTPGRGSLGTEGGGSMQRGSLSSRALAGNLDRSTHGHHSVDVSKDHQKVIQISSGTEDPRSLGTQERKERYTSLPLGRTREPALYDNLKEELVANMKLLEVGAACTQGTRSQAIPRSGVYVPSLGGMWPEPRGPYDKVIQELVQGPPRLLKVDLKAWKVGSECLPRPIVNPGSPKEEQVSRERGTRRKARPSAQGTTVKTTSPARGQDCSTLPVSANLKAPTHSCSDPSSDKAKVCLGKGKRTLRKPQKVPSIYKLKLRPRIRPRRDHRPEKRPSRIPKPLVYPFLGPARTAPGSRLLKATLGGTGGDVNGVGKKEEEKKKETSISLESSIQPSESREPMQLDGTPLPPEEESWV
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Involved in the cross-linking of microtubules and microfilaments (By similarity). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (By similarity). Enhances ADORA2-mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity).
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D3ZUI5
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COBL_RAT
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Protein cordon-bleu
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MKARAPPPPGKPAAQNVHSEQKLPHDATLGSQQSLVHLKEALHNSTLDITVVLPSGLEKQSVVSGSRAVMDLLVELCLQNHLNPSHHVLEIWSSETQQPLSFKPNTLIGSLNAHTVFLKEKVPEEKGKPGLTKAPEKSVRLVVNYLRTQKAVMRVSPEVPLQNILPVICAKCEVSPDHVVLLRDNIAGEELELSKSLNELGIKELYAWDNRREMLRKSSLGNDETDKEKKKFLGFFKVNKRSNSKAEHLGLSGADSDEDPSKSASGGDLNGCVTTPNSPSLHSRSLTLGPSLSLGNISGMSMKSDMKKRRAPPPPSPGLLGQDKVSEKASLSSQADLQKKKRRAPAPPPPQPPPPSPVVPNRKEDKEENRKSTVGMEENYETDTSSLTSSVNGVSNHSLQEAIIPDSGVDDIPVTFIGEVSDEPFDSGLFFSGSNNAAALNQGGIASQRSHLPPYQTEQSQPFIRTNRKEPDPSLPSQDYRKRNQPILANTSENENPVGIDPRVTSFVSKPSTDDPKAKDKDKMCGSGPSEKTQTGHRVNSLPVNPRVGEDENSNSALPPWSHHGQASGGSYGLKYGLTTYKIVPPKPEMRCYDRDVSLSTGAIKIDELGNLMSPHMNGSRTISKPSAVAETEAPPIGKVKEFWRRNSMEKYLNGPAECTVKKAPSTTITATSEKPQRDETKAGFTLTTPEQQPASQEYGAPPEEDRSRPHSAVSCPVKVPAPNPTDITFLKPQRRTSSQYVASAIAKKMGPPKVHADVVRPHKKTAEQGHEEAKLARPPPAWKDSAVPNLCSEAGQCEHGTNQGSVRLPSNPGGQLPADHPKVEVNSTYGKSATHNSPAAVHRNSYFLPGRSSQRDRVSVGQSCGFHEKQTISNQKMNSTSNPSQALDKAHPAPLLLTEARDSGRILVNGSAQTPGNCEPPHSQKESTLTSYIILQTEEKPSPLSADGQNSDDALPSSIFGPKKKFKPVVQRPLPKDISLHSALMEAIHTSGGRDKLRKTAEQASEGRPKKPSYVEAESERSALLAAIRGHSGTLSLRKVSSLASEELQSFRDAALMAPGVDKPQQEDRGLPPPPALPPPSTPASQVPSASIPVSRFSIGTLSNPVNARQALMDAIRSGTGAARLRKVPLLV
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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 dendrite branching in Purkinje cells (By similarity). Regulates neuron morphogenesis and increases branching of axons and dendrites. {ECO:0000250, ECO:0000269|PubMed:21725280, ECO:0000269|PubMed:23223303}.
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D3ZUM2
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SARM1_RAT
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NAD(+) hydrolase SARM1 (NADase SARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and TIR motif-containing protein 1)
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MVLTLLFSAYKLCRFFIMSGPRPGADRLTVPGPDRSGGTSPWWAAGGRGSREVSPGVGTEVQGALERSLPELQQALSELKQASAAQAVGAGLAEVFQLVEEAWLLPAVGREVAQGLCDAIRLDGGLDLLLRLLQAPELETRVQAARLLEQILVAENRDRVARIGLGVILNLSKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCALHGGQTVQRCMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVEHSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQSLVLLLDSSRLEAQCIGAFYLCAEAAIKSLQGKTKVFSDIGAIQSLKRLVSYSTNGTTSTLAKRALRLLGEEVPRRILPCVASWKEAEVQTWLQQIGFSQYCENFRDQQVDGDLLLRLTDEELQTDLGMKSSITRKRFFRELTELKTFASYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRTRILSAAREMLHSPLPCTGGKPSGDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVMAARNFVLVLSAGALDKCMQDHECKDWVHKEIVTALSCSKNIVPIIDGFEWPEPQALPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRPSQDSSAGSDTSLEGATSMGLP
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NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site. Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide NAD(+) cleavage promoting cytoskeletal degradation and axon destruction. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules. Can activate neuronal cell death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38.
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D3ZUQ0
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RIPL1_RAT
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RILP-like protein 1 (GAPDH's competitor of SIAH1 protein enhances life) (GOSPEL) (Rab-interacting lysosomal-like protein 1)
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MEEPLGSPPAALSALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRVERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLNHKDVGFSEEELQKHEGMSERERQVMKRLKEVVDKQRDEIRAKDRELVLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEEAEIPPQPDGEESISDAEKAALDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEIEEENRIPQPPPITHPRTSPQPESGIKRLFSFFSRDKRRLANTQRPTHIHESFGQWAITHRDDGYTEQGQEALQHL
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Plays a role in the regulation of cell shape and polarity (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH. Does not regulate lysosomal morphology and distribution (By similarity). Binds to RAB10 following LRRK2-mediated RAB10 phosphorylation which leads to inhibition of ciliogenesis (By similarity).
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D3ZVK1
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MCM8_RAT
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DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8)
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MSGAYRGRGFGRGRFQNWKRGRGGGNFSGRWRDRTDLSKAAGNHASEQASQPLLQQSTLDQFIPYKGWKLYFSEVYSNNSPLTEKIQAFEKFFTRHIDLYDKDEIERKGSILVDFKELTKDNEITNLIPDIENALRDAPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLCNGGGTMVNVPHIYARVYNYEPLTHLKNIRATCYGKYISIRGTVVRVSNIKPLCTKMAFQCAACGEIQSFPLPDGKYNLPTKCPVPACRGRSFTPLRSSPLTVTMDWQLIKIQELMSDAQREAGRIPRTIECELVHDLVDSCVPGDTVTVTGIVKVSNSEEGSRSKNDKCMFLLYIEANSVSNSKGQKAQTAEDGCKHGTLMEFSLKDLYAIQEIQAEENLLKLIVNSLCPVIFGHELVKAGLMLALFGGSQKYADDKNRIPIRGDPHVLIVGDPGLGKSQMLQAACNVAPRGVYVCGNTATSSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGVVCSLPARTSIIAAANPVGGHYNKARTVSENLKMGSALLSRFDLVFILLDTPNEQHDHLLSEHVIAIRAGKQRAVSSATVSRVLSQDSNTSVLEVVSEKPLSERLKVAPGEKTDPIPHQLLRKYIGYARQYVHPRLSTEAAQALQDFYLELRKQSQRVGSSPITTRQLESLIRLTEARARLELREEATKEDAEDIIEIMKHSMLGTYSDEFGNLDFERSQHGSGMSNRSTAKRFISALNSIAERTYNNIFQFHQLRQIAKELNIQVADFENFIGSLNDQGYLLKKGPKIYQLQTM
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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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D3ZVM4
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LIN41_RAT
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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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MASFPETDFQICLLCKEMCGSPAPLSSSSSASSSSSQTSTSSAGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAPGGAGPAEALKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGGGPGGAGGHSNHRHHAHHPAQRAAAPAPQPPPGPAASPGSLLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAASAAQQLGLGPPFAGAPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTLGRHGGHSFAYLQDALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTIRGLLQPQEDDRVMFTPPDQALYLALKSFGFVSSGAFAPLTKAAGDGIKRALQGKVASFTVMGYDHNGEPRLSGGDLMSVVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLYNQHIENSPFKVVVKSGRSYVGIGLPVLSFGSEGDGEGKLCRPWGVSVDKEGYIIVADRSNNRIQVFKPCGSFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGSLWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFEANGSFLCKFGAQGSGFGQMDRPSGIAVTPEGLIVVVDFGNNRILIF
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E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (By similarity). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity).
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D3ZVU1
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SPRTN_RAT
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DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)
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MDEDLVVALRLQEEWDVQAARRAAAREPLSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHKQPYYGYVKRATNRAPSAHDYWWADHQKTCGGTYIKIKEPENYAKKGRGKTKAGKQPTSAVENKDKLCRGEAQPLIPFSGKGYVLGDTSTCPSAGKLNTSHMVNDTKGLSGQDHSASGLKLDSNVEVKCEQNGLPNKKPHLVTPLPTASHQSVLSSYFPRVSVANQKAFRNVNGSPVKSGTIDGTKHSASAGAQRKVPPSRASLRNSSKVTAPASATVTSAAGTSAAISREESGSEDQFLNKRPRLEDRTALNNIKEQTQSGGDLEDSSRPTAISTPRSSGGQRRLVNCPVCQGVVLESQINEHLDRCLEGSKTNLRPRRV
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DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity).
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D3ZVU9
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NAT8L_RAT
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N-acetylaspartate synthetase (NAA synthetase) (N-acetyltransferase 8-like protein) (EC 2.3.1.17)
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MHCGPPDMVCETKIVATEDHEALPGAKKDALLAAAGAMWPPLPAAPGPAAAPPPAAGPQPHGGTGGAGPPEGRGVCIREFRAAEQEAARRIFYDGILERIPNTAFRGLRQHPRTQLLYALLAALCFAVTRSLLLTCLVPAGLLALRYYYSRKVILAYLECALHTDMADIEQYYMKPPGSCFWVAVLDGNVVGIVAARAHEEDNTVELLRMSVDSRFRGKGIAKALGRRVLEFAMLHNYSAVVLGTTAVKVAAHKLYESLGFRHMGASDHYVLPGMTLSLAERLFFQVRYHRYRLQLREE
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Catalyzes the synthesis of N-acetylaspartate acid (NAA) from L-aspartate and acetyl-CoA. Promotes dopamine uptake by regulating TNF-alpha expression (By similarity). Attenuates methamphetamine-induced inhibition of dopamine uptake (By similarity).
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D3ZVV1
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KHDC3_RAT
|
KH domain-containing protein 3 (Protein Filia)
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MATLKTFRTLVQLKHKLGKAYEIVGEPRLPKWFHVEYLEDPKKMYVEPTLVEIMFGKDGEHIPHVECTLHVLIHVNVWGPEKQAEILIFGPPNFQKDVAQMLSNVAHFCRMKLMEKEALEAGVERRLMAASKATTQPTPVKVRDAATQVAPVQVRDAAIQPAPVKVRDAATQVAPVQVHEVATQPVPVQVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATEPVPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVREAATQQTPVEVADDTQLVQLKAGEAFAQHTSGKVHQDVNGQSPIEVCEGATQRHSVDASEALSQKCPEDLEGGDTETSLDDSYVIIRPSRAVWEPFVML
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As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Regulates homologous recombination-mediated DNA repair via recruitment of RAD51 to sites of DNA double-strand breaks, and sustainment of PARP1 activity, which in turn modulates downstream ATM activation (By similarity). Activation of ATM or ATR in response to DNA double-strand breaks may be cell-type specific (By similarity). Its role in DNA double-strand break repair is independent of its role in restarting stalled replication forks (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for maintenance of euploidy during cleavage-stage embryogenesis (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process (By similarity). Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function (By similarity). Promotes neural stem cell neurogenesis and neuronal differentiation in the hippocampus (By similarity). May regulate normal development of learning, memory and anxiety (By similarity). Capable of binding RNA (By similarity).
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D3ZW55
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ITPA_RAT
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Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase)
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MAASLVGKKIVFVTGNAKKLEEVIQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAARQVQGPVLVEDTCLCFNALGGLPGPYIKWFLQKLKPEGLYQLLAGFEDKSAYALCTFALSTGDPSQPVLLFRGKTPGQIVMPRGSRDFGWDPCFQPDGYEQTYAEMPKAEKNTISHRFRALFKLQEYFGVTDGAGDH
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Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148}.
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D3ZWK4
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LMBL1_RAT
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Lethal(3)malignant brain tumor-like protein 1 (H-l(3)mbt) (H-l(3)mbt protein) (L(3)mbt-like) (L(3)mbt protein homolog)
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MEGHSDMEIIRAVKGSATGEINVHLVARDSAGSHPHLPTTTFIIPTNAATLGLPSTALDVSYPREPVHVGAAERVAGSEPVTATILPQLSTGPGTNSTVRLLDWTGVSAPLAGSGMRFRINEYATQNMIEIERPRSPEQRHEGGTAGREADIQHPDVHKDPQEVIPQEPSVDAGSCKCQTCGPQQSIGLDVGSSGDRCPQPFQKRSVIVENSGCTVASELIKPMKKRKHKEYQSPSEESEPEAMKQGKGKDPDREPTPGTSENEEWSRSQLVSSEKKEGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEGVDPQHPSMYFVLTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTKAQAAPKHLFVSQSHSPPPVGFQVGMKLEAVDRMNPSLVCVASVTDVVASRFLVHFDDWDDTYDYWCDASSPYIHPVGWCQKQGKPLTPPQDYPDPDSFCWEKYLEETGTSAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKLHFDGWSHNYDFWIDADHPDIHPAGWCSKTGHPLEPPLRPRESSSASPGGCPPLSHRSPPHTKTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSETTARKKNQSNLSPRKKPRHQGRIGRPPKYRKMPDEDFQALPPSVVHQSLFMSTLPTHADRPLSVCWEQHCKLLPGVAGISASAVSKWTIEEVFGFVQTLTGSEDQARLFKEEMIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNNDDVFK
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Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity).
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D3ZYR1
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FCHO2_RAT
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F-BAR domain only protein 2
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MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYNAKCVEQERLKKEGATPREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPVHPNNVHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPITSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPATLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC
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Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor (By similarity).
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D3ZYW7
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FRDA_RAT
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Frataxin, mitochondrial (Fxn) (EC 1.16.3.1) [Cleaved into: Frataxin intermediate form; Frataxin mature form; Extramitochondrial frataxin]
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MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT
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[Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+) the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (By similarity). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity).
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D3ZZC3
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KLH22_RAT
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Kelch-like protein 22
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MAEEQDFAQLCKLSTQPSHSHCVNNTYRSTQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLNRLTQQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYSMEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLGPSPLRDTVASALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTILSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGKYIYAVAGRDYHNNLSAVERYDPATNSWEYVAPLKKEVYAHAGTTLQGKMYITCGRRGEDYLKETHCYDPGSNTWHTLADGPVRRAWHGMAALLDKLFVIGGSNNDAGYRRDVHQVACYSCTSRQWSSVCPLPAGHGEPGIAVLDNRIYVLGGRSHNRGSRTGYVHIYDMEKDCWEEGPQLNNSISGLAACVLTLPRSLLHEQPRGTPNRSQADADFASEVMSVSDWEEFDNSSED
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy.
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D3ZZX1
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I5P1_RAT
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Inositol polyphosphate-5-phosphatase A (EC 3.1.3.56) (Type I inositol 1,4,5-trisphosphate 5-phosphatase) (5PTase)
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MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVLHTHKPHFMALHCQEFGGKNYEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQFDFKAKKYKKVTGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDLVNIHLFHDASNLVAWETSPSVYSGVRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSKSVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVVLQLEKKLFDYFNQDVFRDNNGTALLEFDKELSVFKDRLYELDISFPPSYPYSEDSSQGEQYMNTRCPAWCDRILMSLSAKELVLKSESEEKVATYDHIGPNVCMGDHKPVFLAFRIAPGAGKPHAHVHKCCVVQ
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Phosphatase that specifically hydrolyzes the 5-phosphate of inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate, and inositol 1,3,4,5-tetrasphosphate to inositol 1,3,4-trisphosphate. Plays a crucial role in the survival of cerebellar Purkinje cells (By similarity).
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D4A055
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CACB4_RAT
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Voltage-dependent L-type calcium channel subunit beta-4 (CAB4) (Calcium channel voltage-dependent subunit beta 4)
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MSSSYAKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTTTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTSSSTPMTPLLGRNVGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGCSHDSRHRL
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The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
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D4A1F2
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MICA2_RAT
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[F-actin]-monooxygenase MICAL2 (EC 1.14.13.225) (MICAL C-terminal-like protein) (Mical-cL) (Molecule interacting with CasL protein 2) (MICAL-2) (Protein RSB-11-77)
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MGENEDEKQAQASQVFENFVQATTCKGTLQAFNILTCLLDLDPLDHRNFYTQLKSKVNTWKAKALWHKLDKRGSHKEYKRGKACSNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDTFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVRVREPPKDQENRKIGWRAEFLPADHALSNFEFDVIIGADGHRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDSTHYFVMTAKKQSLLDKGVILNDYIDTEMLLCAENVNQDNLLSYAREAADFATNYQLPSLDFAINHNGQPDVAMFDFTSMYASENAALMRERQAHQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMVKSWDQGTPPLEVLAERESLYRLLPQTTPENINKNFEQYTLDPATRYPNLNVHCVRPHQVKHLYITKEMDRFPLERWGSVRRSASLSRRESDIRPNKLLTWCQQQTKGYQHVRVTDLTTSWRSGLALCAIIHSFRPELINFDSLNENDVVENNQLAFDVAKREFGILPVTTGKEMASTQEPDKLSMVMYLSKFYELFRGTPLRPMDSRRKNYGENADFGLGKTFFQNNYLNLTLPRKRTPRVDAQTEENDVNKRRRQGFNNLEELPAFSSRSLGSSQEYAKESGNQNKVKYMANQLLAKFEENTRNPSALKQDCPRVSGMGKPVLCSASRPPGTSHCPKLEESTPRLPPPLKRQFSSTVATGQVLRELNQVPASGECPGRPWRARAKSDLQLGGAENLATLPPTCQGALALSGVLRRLQQVEEKVLQKRAQNLANREFHTKNIKEKAAHLASMFGHGDLPQDKLLSKRVPHAHPPSPPSCLPSPDPAAAPSPPAADSVSPARKVLTVGKVSSGIGAAAEVLVNLYLNDHRPKTQATSPDLESLRKAEFPLSLGGRDTCYFCKKRVYVMERLSAEGHFFHRECFRCSVCAAILRVAAYAFDCDEGKFYCKLHFAHCKTSSKQRKRRAELNQQREEEGTWPEQEAARRDVPAESSCAVAAISTPEGSPPDEPISPKKSKSVPKPNSRPMEVEATSPRPSEWTSVRIGPGQDGQDVLAVRVLVTSEDSSSDTESDSGSIIGPCTEACEERPRLPESPPLSQPLTRHISLRETLTQPVSLLLHHKEPQAVPGLQRAYSLQSPSKYQNWRRKFQSNSTPMNQRALSPPKEPPPSSSSSSPSLPSSFSSASVPGHTTDDSSSPQVTYNLHSPQISRDDVSPTPIYLRRARAQGITKEIPLYLPHSPMLESTEHCLVSPDGEELRSPEEISASDGCQKALALGNSESTHKDSYPVSGKDPYLPNQMLALGAAGNTGDLSEESRMGQTGGAELSKERKLGLKKLVLTEEQKTMLLDWNDYTQEHKAGERLAQEKAENGRGNSLKPICSSTLSQAVKEKLLSQKKALGETRTPAAKAPREREVPPPKSPLRLIANAIFRSLLPSSEAGKKTSSKPETKTLPRGQPHAFTRSFSFRKLGSSKDGDQQSPGRHMAKKASAFFSLASPTSKAAQASDLSPPNPILRSRSLPNRPSKMFFATTSLPPSSKVEDVPTLLEKVSLQDAAQGPKKGASHISPLGLKDKSFESFLQECKERKDIGDFFNSPKEKGPPGNRVPSLEKLVQPVDSTSMGQVAHPSSTGQDAQAAVRTQAGKEGSSLVSSLVLVSGPGAPVTEDTSSPTSSSAEEDVETQLSSRLKEKIPRRRRKLEKQMAKQEELKRLHKAQAIQRQLEEVEERQRTSEIQGVRLEKVLRGETADSGTQDEAQLLQEWFKLVLEKNKLMRYESELLIMAQELELEDHQSRLEQKLRQKMLKDEGQKDENDLKEEQEIFEEMMQVIEQRNKLVDSLEEQRIKERTQDQHFENFVLSRGCQLSRT
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Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (By similarity). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By similarity).
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D4A1J4
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DHRS6_RAT
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Dehydrogenase/reductase SDR family member 6 (EC 1.1.1.-) ((R)-beta-hydroxybutyrate dehydrogenase) (3-hydroxybutyrate dehydrogenase type 2) (EC 1.1.1.30) (4-oxo-L-proline reductase) (EC 1.1.1.104) (Oxidoreductase UCPA) (Short chain dehydrogenase/reductase family 15C member 1)
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MGRLEGKVIVLTAAAQGIGRASALAFAREGAKVIATDINEAKLQELENYPGIQTRVLDVTKKRQIDQFASEIEKIDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVENRCVYSATKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARDDPKEALKAFLNRQKTGRFASAEEVALLCVYLASDESAYVTGTPVVIDGGWSL
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NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines. Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (By similarity).
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D4A1R8
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CPNE1_RAT
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Copine-1 (Copine I)
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MAHCVTLVQLSVSCDHLIDKDIGSKSDPLCVLLQDVGGAWAELCRTERVRNCSSPAFSKTLQIEYYFETVQKLRFGIYDIDNKTPELGDDDFLGGAECSLGQIVSSQTLTLPLMLKPGKPAGRGTITVSAQELKDSRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLAYRTEVVKNNLNPTWKRFSVSLQHFCGGDLNTPIQVRCSDYDSDGSHDLIGTFHTTLAQLQAVPAEFECIHPEKQQRKKSYKNSGTVCVKTCRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLTALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFNPSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAQQRTASQYFVLLLLTDGAVTDVEATCKAVVEASKLPMSVIIVGVGGADFEVMEQLDADGGPLRTRSGEAAARDIVQFVPYRRFQNAPRETLAMTVLAEVPTQMVSYFKAQGWAPLKTLPAPAKGPAQAPQV
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Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner. Exhibits calcium-dependent phospholipid binding properties. Plays a role in neuronal progenitor cell differentiation induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner. May recruit target proteins to the cell membrane in a calcium-dependent manner. May function in membrane trafficking. Involved in TNF-alpha-induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit. Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL.
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D4A1W8
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MTP_RAT
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Microsomal triglyceride transfer protein large subunit
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MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKLQDSVGYRISSDVDVVLLWRNPDGDDDQLIQVTITAVNVENAGQQRGEKSIFKGKSTPKIVGKDNLEALRRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLTSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVTSKATSVTTYKIEDSFVTAVVAEETRAFALNFLQTVAGKIVSKQKLELKTTEAGPRMVPGKQVAGVIKAIDSKYKAIPIVGQVLQSVCKGCPSLAEHWQSIRKHLEPENLSNAEAVQSFLAFIQHLRTSRREEILQILKAEKKEVLPQLVDAVTSAQTPASLEAILDFLDFKSDSSIILQERFLYACGFASHPDEELLQALLSKFKGSFASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEAKKLILGGLEKPEKKEDTTMYLLALKNALLPEGIPLLLKYAEAGEGPVSHLATTVLQRYDASFITDEVKKTLNRIYHQNRKVHEKTVRTTAAAVILKNNPSYMDVKNILLSIGELPKEMNKYMLTIVQDILHFEMPASKMIRRVLKEMIVHNYDRFSKSGSSSAYTGYVERSPHAASTYSLDILYSGSGILRRSNLNIFQYIGKAELHGSQVVIEAQGLEGLIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPVSVVKGLILLIDHSQDIQLQSGLKANMDIQGGLAIDISGSMEFSLWYRESKTRVKNRVAVVITSDITVDSSFVKAGLESRAETEAGLEFISTVQFSQYPFLVCMQMDKAEAPLRQFETKYERLSTGRGYVSRRRKESLVPGCELPLHQENSEMCNVVFPPQPESGNSGGGWF
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Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (By similarity). May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins (By similarity).
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D4A208
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SRGP2_RAT
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SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2)
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MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDIIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRRQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLRHEGVFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLIACVTMDNLQERAVHIRKVLLVLPKPTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPNPRELEGPIYSRGGSMEDYCDSTHGETISAEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVMSEPPEEKVTARTGASCPSGGHVADIYLANINKQRKRPESGSIRKAFRSDSHGLGSSLTDSSSPGVGASCRPSSQPIMSQNLPKEGPDKCSISGHGSLNSISRHSSLKNRMDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELQELERQSSAKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSASPQSTDKSCTV
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Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses. Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation. Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions. In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.
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D4A280
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PAK5_RAT
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Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7)
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MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKSCKESSINGLLEDFDNISVTRSNSLRKESPPTPDQGAASRIQGHSEENGFITFSQYSSESDTTTDYTTEKYRDRSLYGDDLDLYYRGSHAAKQNGHAMKMKHGDAYYPEMKPLKSDLARFPVDYHTHLDSLSKASEYGDLKWDYQRASSSSPLDYSFQLTPSRTAGTSRCSKESLAYSESDWGPSFDDYDRRPKSSYLHQTSPQPAMRQRSKSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVFSPPLSGSDTYPRGPTKLPQSQSKVGYSSSSHQYPGYHKASLYHHPSLQTSSQYISTASYLSSLSISSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLDNFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLKALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSMLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH
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Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions (By similarity).
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D4A2H2
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SPTC1_RAT
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Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
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MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSRNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAAFASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVAEGLYMNTGTICPLPELVRLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKKKCQTIHKSLQGVSGLKVVGESLCPALHLQLEESTGSRERDMKLLQEIVEQCMNKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTDEELQRAAATIREAAQAVLL
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Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity).
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D4A2Z8
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DHX36_RAT
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ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.12) (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH-box protein 36) (G4-resolvase-1) (G4R1) (MLE-like protein 1) (RNA helicase associated with AU-rich element protein)
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MSYDYHQSWSRDGGPRGSGQGSGGGGGGSRGSGGGGGGRGGRGRHPAHLKGREIGLWYAKKQTQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKNDKDSEAQISWFAPEDHGYGTEVSSEKKINSEKKLDNQEKKLLNQEKKTYRITDKSYIDRDSEYLLQQNEPNLGLDQQLLEDLQKKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGNGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVVEYLLEDIIEKIRYFPEQKEHRSQFKRGFMQGHVNRQEKEEKEAIYKERWPAYIKELQTRYSASTIDVLEMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDRFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFLSRLMDPPSDEAVVLSIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKETRSDHLTVVNAFEGWEEAKRRGFRYEKDYCWEYFLSSNTLQMLHNMKGQFAEHLLGAGFVSSRSPKDPKANINSDNEKIIKAVICAGLYPKVAKIRLNLGKKRKMVKVHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDKDQEIIAVDEWIVFQSPERIAHLVKGLRKELDILLQEKIECPHPVDWNDTKSRDCAVLSAILDLIKTQEKAIPRNLPPRSQDGYYS
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Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (By similarity). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses. G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA) (By similarity). Plays a role in genomic integrity. Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (By similarity). Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (By similarity). Plays a role in post-transcriptional regulation. Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment. Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size. Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability. Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression. Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively. Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation. Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Required for the early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification (By similarity).
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D4A3K5
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H11_RAT
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Histone H1.1 (Histone H1a)
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MSETAPVPQPASVAPEKPAATKKTRKPAKAAVPRKKPAGPSVSELIVQAVSSSKERSGVSLAALKKSLAAAGYDVEKNNSRIKLGLKSLVNKGTLVQTKGTGAAGSFKLNKKAESKASTTKVTVKAKASGAAKKPKKTAGAAAKKTVKTPKKPKKPAVSKKTSSKSPKKPKVVKAKKVAKSPAKAKAVKPKAAKVKVTKPKTPAKPKKAAPKKK
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H1 histones bind to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. H1 histones are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling (By similarity).
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D4A4D7
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E2F7_RAT
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Transcription factor E2F7 (E2F-7)
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MEVNCLTLKDLISPRQTRLDFAVEDAETAQKENIFVDRSRMTPKTPMKNEPIDLSKQRIFTPERSPITPVKLVDRQPQVEPWTPTANLKMLISAASPDIRDREKKKELFRPIENKGDAFVNSLQLDVVGDSAVDDYEKRRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRTLQRLGEEQKYEEQMACLQQKELDLMEYRFGERRKDGSPDPRDQHLLDFSESDYPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDTPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSIDEELLDVSASVLPELKKETYGQIRVCAKERLARYGSFNTVQTSEKIQRKVNSEPSSPQGGKQGPAYSLEIGSLAAIYRQKVEDSSQGEAFVNKRAAPPASVLDPTLPVDSEYCVKPLAQPVFSVAQTDLQAFSAQNGLNGQVGVPVPSAASDAETLKSALLASQPLVYVPSTSLFMLYGSVQEALSPESRSEEDGSGSDVPADLSLAPTAQKRLCEERNPLEDDEPAVKRQSREFEDSPLSLVMPKKPSNSTDLAFPVTTGNGRATPLEDACVKGQLPAAEDASGRAVPNGFIASECGNPSRNPDTEKSSNDNEITKDPSLLQYLYVQSPAGLNGFNMLLPGGQTPHAVAPSSAAMPSFGVPCMFLPSPGLGPFPVLYSPAIPGPISSAPGTLPNTGPMNFGLSTLASASHLLISPAAMVNPKSSTLPSADPQLRCQPPLNPNPVMPGSHGVIHPESPGYMRHPVSMVKAEQSPAPATPKSIQRRHRETFFKTPGSLGDPAFRRERNQSRNTSSAQRRLEISSSGPD
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Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation (By similarity).
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D4A4K3
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BAKOR_RAT
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Beclin 1-associated autophagy-related key regulator (Barkor) (Autophagy-related protein 14-like protein) (Atg14L)
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MASPSGKGSWTPEAPGFGPRALAPDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLHILELTSVIFPMDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFCGENLSKQRLTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVSPHSEHLGRSGPFEVRADLEESMEFVDPGVAGESDVSGDERVSDEETDLGTDWENLPSPRFCDIPSQPVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR
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Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Modulates the hepatic lipid metabolism (By similarity).
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D4A523
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NLRP3_RAT
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NACHT, LRR and PYD domains-containing protein 3 (EC 3.6.4.-)
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MKMMSVRCKLAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKKDQPEWNDACTSNLSMVCQEDSLEEEWIGLLGYLSRISICKKKKDYCKIYRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRTKMWDRPMSSLKLELLFEPEDEHLEPVHTVVFQGAAGIGKTILARKIMLDWALGKLFKDKFDYLFFIHCREVSLRAPKSLADLIISCWPDPNPPVCKILCKPSRILFLMDGFDELQGAFDEHIEEVCTDWQKAVRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQTSKTTTAVYVFFLSSLLQSRGGIEEHLFSAYLPGLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSFSHMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSDLLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQEEDFVQSAMGHFPKIEINLSTRMDHVVSSFCIKNCHRVKTLSLGFLHNSPKEEEEEKRGSQPLDQVQCVFPDPHVACSSRLVNCCLTSSFCRGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFGVRLLCVGLKHLLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNSGLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCSLTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLCEVLKQQGCLLQSLQLGEMYLNCETKRTLEALQEEKPELTVVFEISW
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Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF.
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D4A540
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AUGN_RAT
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Augurin (Esophageal cancer-related gene 4 protein homolog)
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MGTSSARPAVLALAGLALLLLLCLGPGDVSGNKLKKMLQKREGPVPSKTNVAVSEHTAKEFLGGLKRAKRQLWDRTRPEVQQWYQQFLYMGFDEAKFEDDVNYWLNRNQNGHDYYGDYYQRHYDEDAAIGPRSREGFRHGASVNYDDY
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Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system. ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation.
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D4A612
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ELOV2_RAT
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Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2)
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MFGPRDSRVRGWFLLDSYLPTFTLTIVYLLSIWLGNKYMKNRPALSLRGILTLYNLGITLLSAYMLVELVLSSWEGGYNLQCQNLDSAGEGDIRVAKVLWWYYFSKLVEFLDTIFFVLRKKTSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHRYLWWKKYLTQAQLVQFVLTITHTLSAVVKPCGFPFGCLIFQSSYMMTLVILFLNFYIQTYRKKPMKKEMPEGAAGKEVKNGFPKAHSIAANGVTDKKVQ
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Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}.
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D4A631
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BIG1_RAT
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Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1)
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MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGSAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQHHLLQSPVSHHEPESPHLRYLPPQTVDHIAQEQEGDLDPQTHDVDKSLQDDIEPENGSDISSAENEQTEADQATAAETLSKDDVLCDGECEEKPQDIVQSIVEEMVDIIVGDMGEGTAVSASADGNAGAVEDGSDSENVQANGIPGTPISAAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQAGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTDVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTSGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCVINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAAPPSPSAMSEKQLDAISQKSVDIHDSAQPRSSDNRQQAPLVSVSPASEEVSKGRPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINKQ
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Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity).
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D4A693
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AZIN2_RAT
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Antizyme inhibitor 2 (AzI2) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p)
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MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLAELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDALGLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVDGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQACRVTYAMSRLAWEALQGQLLPAEEDQDAEGVCKPLSCGWEITDSLCVGPVFTPASIM
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Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking.
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D4A6D8
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LRRT1_RAT
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Leucine-rich repeat transmembrane neuronal protein 1
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MDFLLLGLCLHWLLRRPSGVVLCLLGACFQMLPAAPSGCPGQCRCEGRLLYCEALNLTEAPHNLSGLLGLSLRYNSLSELRAGQFTGLMQLTWLYLDHNHICSVQGDAFQKLRRVKELTLSSNQITELANTTFRPMPNLRSVDLSYNKLQALAPDLFHGLRKLTTLHMRANAIQFVPVRIFQDCRSLKFLDIGYNQLKSLARNSFAGLFKLTELHLEHNDLIKVNFAHFPRLISLNSLCLRRNKVAIVVSSLDWVWNLEKMDLSGNEIEYMEPHVFETVPYLQSLQLDSNRLTYIEPRILNSWKSLTSITLAGNLWDCGRNVCALASWLSNFQGRYDANLQCASPEYAQGEDVLDAVYAFHLCEDGAEPTSGHLLSAAVTNRSDLAPPESSATTLVDGGEGLHDSTLEPITVAIPGGEHAENAVQIHKVVTGTMALIFSFLIVVLVLYVSWKCFPASLRQLRQCFVTQRRKQKQKQTMHQMAAMSAQEYYVDYKPNHIEGALVIINEYGSCTCHQQPARECEV
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Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level.
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D4A6L0
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MGLYR_RAT
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Metabotropic glycine receptor (mGlyR) (G-protein coupled receptor 158)
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MGAMAYSLLLCLLLAHLGLGEVGASLDPSERPDSSRERTSRGKQHGQQLPRASAPDPSIPWSRSTDGTILAQKLAEEVPMDVASYLYTGDFHQLKRANCSGRYELAGLPGKSPSLASSHPSLHGALDTLTHATNFLNMMLQSNKSREQTVQDDLQWYQALVRSLLEGEPSISRAAITFSTESLSTPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRPHLHRRGSNQGPRGLGHSWRRRDGLGGDRSHVKWSPPFLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYQCVCKAGFYHPRVFSVNNFQRRGPDHHFSGSTKDVSEEAHVCLPCREGCPFCADDRPCFVQEDKYLRLAIISFQALCMLLDFVSMLVVYHFRKAKSIRASGLILLETILFGSLLLYFPVVILYFEPSTFRCILLRWVRLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVIVLVVFWFLVGWTSSMCQNLERDILLVGQGQTSDNLTFNMCLIDRWDYMTAVAEFLFLLWGIYLCYAVRTVPSAFHEPRYMAVAVHNELIITAIFHTIRFVLASRLQPDWMLMLYFAHTHLTVTVTIGLLLIPKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKEGTDHSAAKGTGLVRKNPTESSGNTGRPKEESLKNRVFSLKKSHSTYDHVRDQTDESSSLPTESQEEEVTENSTLESLSSKKLTQKVKEDSEAESTESVPLVCKSASAHNLSSEKKPGHPRTSMLQKSLSVIASAKEKTLGLAGKTQTLVMEDRAKSQKPQPKDRETNRKYSNSDNTETNPNSNHTEELRKPQKSGIMKQQRVNLPTANPDASSSTTQIKDNFDIGEVCPWEVYDLTPGPVPSEPKAQKHVSIAASEVEQNPASFSKEKSHHKPKAAEGLYQANHKSIDKTEVCPWESHGQSPLEDENRLISKTPVLPGRAREENGSQLYTTNMCAGQYEELPPKAVASKVENENLNQMGDQEKQTSSSVDIIPGSCISSNNSPQPLTSRAEVCPWEFEPLEQPNAERIVALPASSALSASKIPGPRK
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Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Glycine-binding changes the conformation of the intracellular surface, inhibiting the GTPase activator activity of the RGS7-GNB5 complex, promoting G protein alpha subunits into their active GTP-bound form and regulating cAMP levels. Also able to bind taurine, a compound closely related to glycine, but with a two-fold lower affinity. Glycine receptor-dependent regulation of cAMP controls key ion channels, kinases and neurotrophic factors involved in neuronal excitability and synaptic transmission (By similarity). Plays a pivotal role in regulating mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Also involved in spatial learning by regulating hippocampal CA1 neuronal excitability. Acts as a synaptic organizer in the hippocampus, required for proper mossy fiber-CA3 neurocircuitry establishment, structure and induces presynaptic differentiation in contacting axons via its interaction with GPC4. In addition to glycine, may also act as a receptor for osteocalcin (BGLAP) hormone: osteocalcin-binding initiates a signaling response that prevents neuronal apoptosis in the hippocampus and regulates the synthesis of neurotransmitters (By similarity).
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D4A702
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SYNP2_RAT
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Synaptopodin-2 (Myopodin)
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MGTGDFICISMTGGAPWGFRLQGGKEEKQPLQVAKIRSQSKASDSGLCVGDEVVSINGNPCADLTYPEVIKLMESITDSLHLLIKRPTSGTSEALDSETENTNHQHLPHGGPMESTTLQIQHAAKTQGKDFLLASVQTSAPRTEDQGNAWGYAECTTEDQVSQMPGSQEGHLVEEVILRKKPEAGQPGHVVELQLSLSKERQRCTSDPIVTLLGNEKFKSPDPDWGTQHGRTVHINSIPAPEKADTSLTSGTTVQTSSGRELTVIQGRDPGGTGLPQVEVILDCSDRLKAEECRLQAGRGCVASPVEGGRSEAPPSLVSFAVSSEGTEQGEDQRSGKDQGRPHKHRARHARLRRSESLSEKQVKEAKSKCKSIALLLTDAPNPNSKGVLMFKKRRRRARKYTLVSYGTGELEREEEEEDQEAGDKDEISDLAFLGTSESEVDEELLSDVDDNTQVVNFDWDSGLVDIEKRLNRGDKMEMLPDTTGKGALMFAKRRERMEQFTAQNEEEKTGGLAGGGSDALQTDGLRTMTSYQRKEESVRMQSSVSESSFQMGRSLGSVPQQNGFSGVSETAGPQRMIPMNRTAKPFLGSVNQTAAPFSPTQSVTSPIPDFPAPPPYSAVSPPPEAFSRGISSPVAGPAQPPPWPQPAPWSQPAFYDSSEQIASRDERIAVPAKRTGILQEAKRRGTTKPMFTFKETKVSPNPELLSLLQNAEGKRGTGAGGDSGPEEDYLSLGAEACNFMQSSAKQKTPPPVAPKPAVKTSSSSQPVAPVSPVWSPGVAPAQGPAFSTTNPPNPPQVTAVSSIKIAQPTCPPARPASALNLAGPFKGPQAAVVSHNYTPKPSAPTPLVNAAPAGAGGPSNELPGMSGKGAQLFAKRQSRMEKYVVDSDTVQAHTVRAQSPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAAIKSQPPGAQASKTSKKKGKKPLNTLDVMKHQPYQLNASLFTFQPPDSKDGLPQKSTVKVSSVAPAMKQALPPRQADIGSPTNAKASSVYSVPAYTSQPNFFAEATSPVSASPVPVSVPTSPKQETTSTSYFVAPRPKFSAKKSGVTVQENWRSLSLPGRAAPPIMSAPPWLCQPAYSYSSKPTLEQEKANKRPTPWEAAAKSPLGLVDEAFRPRNIEESIVANVVSAARRKVFAGSQEDWKERLSFVPQTQKTSMSFSERREYNVPSPVNSHVSSHSLYSSQLPYVCYRKESRNDLKAMSMDTRSEYCLPLGGYDYNPHPRGWRHQP
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Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks. At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines (By similarity). Involved in autophagosome formation. May play a role in chaperone-assisted selective autophagy (CASA) involved in Z lines maintenance in striated muscle under mechanical tension may link the client-processing CASA chaperone machinery to a membrane-tethering and fusion complex providing autophagosome membranes. Involved in regulation of cell migration. May be a tumor suppressor (By similarity).
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D4A734
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MOT12_RAT
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Monocarboxylate transporter 12 (MCT 12) (Solute carrier family 16 member 12)
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MTKITRVGSASPPDGGWGWMIVAGCFLVTICTRAVTRCISIFFVEFQTYFAQDYSQTAWIHSIVDCMTMLCAPLGSVVSNQLSCQAGIMLGGLLASTGLILGSFATSLKHLYLSLGVLTGLGFALCYSPAIAMVGKYFSRRKAFAYGIAMSGSGIGTFILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRPITLKEDPSGPEKSHDRDAQREDCKQASPYSPLTKEWTETRLCCSLQQGYGFLLMSDFVVLAVSVLFMAYGCSPLFVYLVPYALSVGVSHHQAAFLMSILGVIDIVGNITFGWLTDRRCLKNYRYVCYLFAVALDGLCYLCLPMLQSFPLLVPFSCTFGYFDGAYVTLIPVVTAEIVGTTSLSSALGVVYFLHAVPYLVSPPIAGWLVDTTGSYTAAFLLCGFAMIFSSILLGFAKIAKRMKRTQVPFLVKDSDPKLHLWTNGSVAYSIAKELDQKDEESLAKARTGCNLT
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Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na(+), Cl(-), or pH. Contributes to the process of creatine biosynthesis and distribution.
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D4A7E1
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BATF_RAT
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Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF)
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MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP
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AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity).
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D4A7H1
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SL9A9_RAT
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Sodium/hydrogen exchanger 9 (Na(+)/H(+) exchanger 9) (NHE-9) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 9)
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MAGQLRLTSGKDEDHFQHQGAVELLAFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIDSGTVYNCGKLLFSPSTLLVNITDQVYEYKYQREINQHNISPHQGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCVVIGLIMYGFVKAMVHAGQLKSGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDTAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLREFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSSDSKLRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKQKIPWNFQHMMMFSGLRGAIAFALAIRNTESQPKQMMFTTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDESLKEEPSSQQEANKVDKDMTKTESAQLFRMWYGFDHKYLKPILTHSGPPLTTTLPAWCGPVSRLLTSPQAYGEQLKEDDVECIVNQDELAMNYQEQSPTSSSPATKLALDQKSSGLTLGKENIYEGDLGLGGYELKLEQTRGQPQMD
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Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (By similarity). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (By similarity). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity).
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D4A7K7
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GP183_RAT
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G-protein coupled receptor 183 (Epstein-Barr virus-induced G-protein coupled receptor 2) (EBI2) (EBV-induced G-protein coupled receptor 2)
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MANNFTTPLAASHGNNCDLYAHHSTARILMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSMNLVISDILFTTALPTRIVYYALGFDWRIGDALCRITALLFYINTYAGVNFMTCLSIDRFFAVVHPLRYNKIKRIEYAKGICVFVWILVFAQTLPLLLKPMSKQEADKTTCMEYPNFEGTASLPWILLGACLLGYVLPLAIILLCYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIGVFVLCFTPYHVAIMQHMVKTLYAPGALGCGVRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMKMLKRQVSVSISSAVRSAPEENSREMTESQMMIHSKASNGR
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G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (By similarity). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (By similarity). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Collaborates with CXCR5 to mediate B-cell migration probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5 (By similarity). Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (By similarity). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4(+) dendritic cells in bridging channels (By similarity). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages (By similarity). Promotes osteoclast precursor migration to bone surfaces (By similarity). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha (By similarity). Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity).
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D4A7P2
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LRRT2_RAT
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Leucine-rich repeat transmembrane neuronal protein 2 (Leucine-rich repeat neuronal 2 protein)
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MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILSSLRSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQGPYSEYEPTHEGPFIIINGYGQCKCQQLPYKECEV
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Involved in the development and maintenance of excitatory synapses in the nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B.
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D4A7T3
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BRDT_RAT
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Bromodomain testis-specific protein
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MSLPSRQMAIVNPPPPEYINAKKTGRLTNQLQFLQRVVLKALWKHSFSWPFQQPVDAAKLKLPDYYTIIETPMDLSTIKKRLENRYYEKASECVGDFNTMFSNCYLYNKPGDDIVVMAQALEKLFMQKLSQMPQEEQIVGGKERMKKDIQQKTAVSSAKEQTPSKSAENVFKRQEIPAGFPDVCLSPLNMAQEAPPTCDSQTVVQITKGVKRRADTTTPTTSSAKASSESPPPLREAKPANAPVKENTVKSVLPDSQQQHRVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDVDALGLHNYYDIVKNPMDLGTIKGKMDKQEYKDACEFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFEMHFAKIPDEPVESMRACHLTTNSAKALSRESSSEASSGDCSSEDSEDERVQRLAKLQEQLNAVHQQLQVLSQVPLRKLKKKNEKSKRAPKRKKVNRDENPKKKAKQMKQKEKAKSNQPKKKKPLLKLEEEDNAKPMNYDEKRQLSLDINKLPGDKLGRIVHIIQSREPSLRNSNPDEIEIDFETLKASTLRELEKYVLACLRKRSLKPHAKKVVRSKEELHSEKKLELERRLLDVNNQLNCRKRQTKRPAKVAVSPRPPLPPPPPPPPELASGSRLSDSSSSSSSSGSGSSSSSSSSSGSGSSSSDSSSSDSSDSEPEISPKFTGVKQNDLPSKENTKQIQCSVPDITSAETALVQQSTGPCGAPGKPPQQMPGCQVPHHLQATESTASVQTQPLAGDCKRVLHGPPVVHASAESHTVLELQCHAPVQKDIKIKNADSWKSLGKPVKASSVLKSSDELFNQFRKAAIEKEVKARTQEQIRKHLEHSAKDPKVSQESQREFGSGFTPESSSNKVQGRSHGEEQSEQQQLPSPSETQDISKLWLLKDRNLAREKEQERRRREAMAGTIDMTLQSDIMTMFENNFD
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Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.
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D4A7V9
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E2AK4_RAT
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eIF-2-alpha kinase GCN2 (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 4) (GCN2-like protein)
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MAGGRGAAGRGPAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELRVKCPPTYPDVVPEIELKNTKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARQKEEQEQREILHEIQKRKEEIKEEKKRKEMAKQERLEITSLTNQDHASKRDPAGHRAAAFLHGGSPDFVGNGKARAHSSGRSRRERQYSVCSGEASPGSCDILYFCVGSADQLMVHKGKCVGSDEQLGKVVYNALETATGSFVLLYEWVLQWQKKMGPCLTSQEKEKIDKCKKQIQGAETEFSSLVKLSHPNIVRYFAMNSREEKDSIVVDILAEHISGISLAAHLSHSGPVPMHQLRKYTAQLLAGLDYLHRNSVVHKVLSTASVLVDAEGTVKITDYSISKRLADICKEDVFEQTRVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECEEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKMPLVEQSPEDSGGQDYIETIIPSNQLPSAAFFTETQRQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRQFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDYIPQAQNSSATGGKASGDTEELGSVEAAAPPPILSSSVEWSTSAERSNSARFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNEKDSRHEIEPSVTTEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFNAEGKQDDQAGDHVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIILFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFEDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANTDGKAYRTMMSQLFCQHSSPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTANSSLPTAETIYTIYEVIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGIAQLVKYSLKDLEEVVGLLKKLGVKLQVSINLGLVYKVQQHNGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQALGPVPTAVGVSIAIDKIFAAVLNMGEPVTVSSCDLLVVSAGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPTVSVISPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF
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Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By similarity). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (By similarity). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a role in feeding behavior to maintain amino acid homeostasis contributes to the innate aversion toward diets of imbalanced amino acid composition. Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity).
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D4AA47
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AT8B1_RAT
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Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (P4-ATPase flippase complex alpha subunit ATP8B1)
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MNTERDSETTFDEDSQPNDEVVPYSDDETEDELEDQGPAVEPEQNRVNREVEKKKETFRKDCTWQVKANDRKFHEQPHFMNTKFFCIKESKYASNAIKTYKYNALTFLPMNLFEQFKRAANFYFLILLILQAIPQISTLAWYTTLVPLLLVLGITAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKIIKWKDIQVGDVIRLKKNDFIPADILLLSSSEPNSLCYVETAELDGETNLKFKMALEITDQYLQIEDNLATFDGFIECEEPNNRLDKFTGTLFWRNQSFPLDADKILLRGCVIRNTDVCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIIIVLILVSAGLAIGHAYWEAQIGNYSWYLYDGENATPSYRGFLNFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKSRTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGTIYGDHRDASQHSHSKIELVDFSWNEFADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLSICHTVMVDRIDGQINYQAASPDEGALVNAARNFGFAFLARTQNTITVSELGTERTYSVLAILDFNSDRKRMSIIVRTPEGSIRLYCKGADTVIYERLHRMNPMKQETQDALDIFASETLRTLCLCYKEIEEKEFAEWNKKFMAASVASSNRDEALDKVYEEIERDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHTRMENQRNRGGVSAKFAPPAYEPFFPPGENRALIITGSWLNEILLEKKTKRSKILKLKFPRTEEERRMRSQSRRRLEEKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYSSLPVLLMGLLDQDVSDKLSLRFPGLYVVGQRDLLFNYKKFFVSLLHGVLTSMVLFFIPFGAYLQTVGQDGEAPSDYQSFAVTMASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWKRRQSVFRRGASSRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIIADGTAEYRRTVES
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (By similarity). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane. Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts. Involved in the microvillus formation in polarized epithelial cells the function seems to be independent from its flippase activity. Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (By similarity). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (By similarity). Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury (By similarity).
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D4AB34
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ERFE_RAT
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Erythroferrone (Complement C1q tumor necrosis factor-related protein 15) (Myonectin)
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MASTRSPGGARTLLACASLLAAMGLGVPESAEPVGTQARPQPPGTELPAPPAHSPPEPTIAHAHSVDPRDAWMLFVKQSDKGINSKKRSRTKARRLKLGLPGPPGPPGPQGPPGPFIPSEVLLKEFQLLLKGAVRQRESTEHCTRDLTTPASGGPSRDPVTQELESQDQGAVLALLAATLAQSPRAPRVEAAFHCRLRRDVQVERRALHELGVYYLPEVEGAFRRGPGLNLTSGQYTAPVAGFYALAATLHVALTKQPRKGPPQPRDRLRLLICIQSLCQHNASLETVMGLENSSELFTISVNGVLYLQTGHYTSVFLDNASGSSLTVRGGSHFSAILLGL
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Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores (By similarity). Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake. Inhibits apoptosis and inflammatory response in cardiomyocytes via promotion of sphingosine-1-phosphate (S1P) and cAMP-dependent activation of AKT signaling. Inhibits autophagy induced by nutrient deficiency in hepatocytes via promoting the phosphorylation of IRS1, AKT, and MTOR, and thereby subsequent activation of the AKT-MTOR signaling pathway. Negatively regulates the differentiation of osteoblasts, potentially via sequestering BMP2, and thereby inhibits the activation of SMAD signaling (By similarity). The reduction in BMP2 signaling in osteoblasts also results in an increase in expression of the osteoclastogenesis-promoting factors TNFSF11/RANKL and SOST, thereby indirectly promotes bone resorption (By similarity).
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D4ABL6
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MCTP1_RAT
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Multiple C2 and transmembrane domain-containing protein 1
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MEPRGAAAGEPEPAVSPSFQARLWKNLQLGVGKGKGGGGGRAGGPERRTAATPTPSLPPPKTTQDVGSTGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRLREHLLPVAKGSSTAAGTVGVTPPGGRSPDSAPSSSASSSLSSSPQPPPRGDRIRDEGTRRGSPEAHLCHQKSSSLPGTACLEQLLEPAPPPAEPARRPAEPQSLQKGEELDCSQKINPVETSNADVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGRKEVFRSKIIHKNLNPVWEEKACVLIDHLREPLYIKVFDYDFGLQDDFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGEPRDVTMLMRKSWKRSSKFQTQSLRLSDQHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTLNPQWREQFDFHLYEERGGVMDITAWDKDAGKRDDFIGRCQVDLSSLSREQTHKLELQLEEGEGHLVLLVTLTASATVSISDLSVNSMEDHKEREEILKRYSPLRIFNNIKDVGFLQVKVIRAEGLMAADVTGKSDPFCVVELNNDRLLTHTVYKNLNPEWNKVFTFNIKDIHSVLEVTVYDEDRDRSADFLGRVAIPLLSIQNGEQKAYVLKNKQLTGPTKGVIHLEIDVIFNAVKASLRTLIPKERKYIEEENRLSKQLLLRNFIRTKRCVMVLVNAAYYVNSCFDWDSPPRSLAAFVLFLLVVWNFELYMIPLLLLLLLTWNYFLIISGKDNRQRDTVVEDMLEDEEEEDDRDDKDGEKKGFINKIYAIQEVCVSVQNILDEAASLGERVKNTFNWTVPFLSWLAIIALCVFTAILYFIPLRYIVLVWGINKFTKKLRSPYAIDNNELLDFLSRVPSDVQVVQYQELKPDHSHSPYKRKKNNLG
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Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (By similarity). Overexpression in cultured neurons significantly inhibits neuronal transferrin endocytosis, secretory vesicle retrieval, cell migration, and oxidative stress from glutamate toxicity.
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D4ACE5
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INTU_RAT
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Protein inturned (Inturned planar cell polarity effector homolog) (PDZ domain-containing protein 6)
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MADPARRDPRGRAPELPGDLSSQEEEEEESDSDAGASSLGSCSSASSDTDLEPEWLDSVQRNGELFYLELSEDEEESLLPETQTVNHVNHVRFSEKEVIIEEDDSRERKKYEPKLRRFTKILKSKSLLPKRHHKKKSSNTGPVSILKHQSTQRTGVTVQQRYKDVTVYINPKKLTAIKAREQAKLLEVLVGVIHQTKWSWKRSGKQADGERLVVHGLVPGGSAMKSGQVLVGDVLVAVNDVDVTSENIERVLSCIPGPMQVKLTFENAYAVKKETAQPKKKKAQSSTNDLVKLLCGSEADATQHSTLSIPHITMYLTLQLQSEVAREEQEMLYHYPVSEASQKLKSVRGIFLTLCDMLESVTGTQVTSSSLHVNGKQIHVAYLKESDKLLLIGLPAEEVPLPQLRNMTEDVAQTLKFMYGSLDSAFCQVENTPRLDHFFSLFFERALRPGKLHLSASPSAQQYDAASAVLLDNLPGVRWLLLPQELKVELDTALSDLEAADFQELSEDYYDMRRLYTILGSSLFYKGYMVCSHLPKDDVVEIAAYCRQYCLLPLAAQQRIGQLIIWREVFPQHHLQPATDSDPEAFQEPEGRYFLLIVGLRHYMLCVLLEAGGCASKATGNPGPDCIYVDQARATLHQLEGVESRIEEQLAATPGPCLSCADWFLAAPREKADSLTTSPILGRLQGPSKTAASPTCRRTFFSDYSFKARKPSPSRIGGGREPGEGEENVGLSPHTTPDTVRKQRESEGSDDNVALLKLARKKSTLPNPFHLGTSKKELSEKELEVYNMMKLTSGPENTLFHYVALETVQGIFITPTHEEVAQLGGSVHSQLIKNFHRCCLTIRAVFQQTLKVEKKKALSDGDHLESANSVSSLSPVKEHGVLFECSPENWTDQKKTPPVMSYWVVGRLFLNPKPQELYVCFHDSVSEIAIEMAFRLFFGLTL
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Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity).
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D4ACP5
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RECQ5_RAT
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ATP-dependent DNA helicase Q5 (EC 3.6.4.12) (DNA helicase, RecQ-like type 5) (RecQ5) (RecQ protein-like 5)
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MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESAIMAVVKGDKDVFVCMPTGAGKSLCYQLPAVLAKGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLLSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKADNGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASERTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEKRGNKPSDKATLLAFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDCCQSPAAIRKKLDALEHSSSWGKTCIGPSQGDGFDPELYEGGRRGYGGFSRYDEGSGGSGDEGRDEAHKREWNLFYQRQMSLRKGKEAKPEEFTPPGEDCPLRDASSRKIPKLTVKAREHCLRLLEEALNSNHQAAGSTHGADLQAKAVELEHETFRSAKMVNLYKASVLKKVAEIHKASKDGQLYDMESSTKSCGAIAELLEPSDYDIPPTSHLYSLKPKRVGAGFSKGPCPFQTATELLGKSQTEKLAPEAALESEQEPSGWVCDPQDGDRSKPCLGYQEEAPGSRTNCGDPSPEKRTKGSSQGSAKARASKRQQLLATAARKDSQSITRFLRQRTECPPPAASVPSSEDASPCGDVPGKCTEEVGAQGHLVAVFQTECPRERLSTCSLEDQSLPKGQPSPLKETQAEKRPRPQQESQEKRAQKRLRPSTNSSALASDPSTENRVAREPCQLSAPGISLKEAADIVVRYLTPFYKEGRFISKDLFKGFARHLSHLLAQKLSPGRSVKEEAQSLIKQFFHNRARCESEADWHGLCGPQR
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DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination.
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D4ACX8
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PCD16_RAT
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Protocadherin-16 (Protein dachsous homolog 1)
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MQEELSVALSCPGMKSLGTLLPLLVLLGTTVPGIRGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLDIDEHSGVVCTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPAHDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLKLERPLDFEQRRVHELVVQARDGGAHPELGSAFVTVHVRDANDNQPSMTVIFLSADGSPRVSEAAPPGQLVARISVSDPDDGDFAHVNVSLEGGEGHFALSTQDSVIYLVCVARRLDREERDVYNLRVTATDSGSPPLRAEAAFVLHVTDVNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGTHTHWFSIDPTSGIITTAATLDYELEPQPQLIVVATDGGLPPLVSSATVSVALQDVNDNEPQFQRTFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGASGSPPFRIDAHSGEVCTTRILDRDQGPSSFDFTVTAIDGGGLKSMVYVKVFVADENDNPPQFYPREYAASLSAQSTPGTAVLRVHAHDPDQGPHGRLSYHILAGNSPPLFALDAHSGLLTVAWPLGRRANSVVQLEIGAQDGGGLQAEPIARVNISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGVVQAHNPPGRLGPVTLTLSGGDPRGLFSLDSASGLLKTLRPLDRELLGPVLELEVRAGSGTPPVFSAARIRVLLDDVNDNSPAFPAPEDTVLLPQNTAPGTPVYTLRALDPDSGANSRVTFSLLAGGDGLFTVDPTTGHVRLMGPLGPPGGPPHELEVEAQDGGSPPRTSHFRLRVVIQDLGIHGLAPRFDSPTYRVDLPSGTTTGTQILQVQAQAPDGSPVTYHLAADGASNPFGLESQSGWLWVRAALDRESQELYTLKVMAVSGSKAELGQQTGTATVRVVILNQNDHSPRLSEEPTFLAVAENQPPGTSVGRVFATDKDSGPNGRLTYSLQQLSEDSKAFRIHPQTGEVTTLQTLDREQQSSFQLLVQVQDAGSPPRSATGTVHVAVLDLNDNSPTFLQASGAAGGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGSGSELFSLHPHTGELHTAASLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSTRMVESPDLVEADSAATVPVVLTVTAAEGLRPGSLLGSVAPQEPASMGVLTYTLVGGADPEGTFALDSASGRLYLARVLDFESGPAWRALTVRAEGPGGAGARLMRVQVRVQDENEHAPAFARDPLALALPENPEPGATLYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPALLLIVEATDRPANASRRKATRVSARVFVTDENDNAPVFASPSRMRLPEDQPPGPAALHVVARDPDLGEAARVSYRLAAGGDGHFRLHATTGALSVVRPLDREQRAEHVLTVVASDHGSPPRSSTQLLTVSVVDVNDEAPAFPQQEYNVILRENSPPGTSLLTLKATDPDLGANGQVTYGGVSGESFSLDPNSGVLTTLRALDREEQEEINLTVYARDRGLPPLLTHITVRVTVEDENDHSPTFGNTHLSLEVPEGQDPQTLTTLRASDPDGGLNGQLQYRILGGDPSGAFALDLTSGEFGTTRPLDREVEPAFQLQIEARDGGQPALSATLLVTVTVLDANDHAPAFPVPSYSVEVPEDAPVGTLLLQLQAHDPDEGDNGRVMYYLGAGTAGAFLLEPTSGELSTATALDREHCASYAFSVTAVDGAAAGPLSTTVPITVTVRDVNDHAPAFPTSPLRLRLPRPGPSLNKPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPAALGPRDRVLFIVATDLGRPARSATGVVIVGIQGEPERGPRFPRANNEAVLRENAPPGTPVISPKAVHSGGSNGPITYSILSGNERGIFSIQPSTGTITVQSAEGLDFETNPRLRLVLQAESGGAFAFSVLTLTLQDANDNAPRFLQPHYVAFLPESRPLEGPLLQVEADDLDQGSGGQISYSLAASQPARGLFHVDPATGTITTTAILDREIWAETRLVLMATDRGSPALVGSATLTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQDPFSIGRYGGRVSLTGPLDFEQCDHYHLQLLAHDGPHEGHANLTVLVEDVNDNVPIFSQSLYQVMMLEHTPPGSAILSVSATDRDSGANGHISYHLASPAEGFSVDTNNGTLFTTVGAMALGHEGPGVVDVVLEARDHGAPGRSAQATVHVQLKDQNDHAPSFTLPHYRVAVSEDLPPGSTLLTLEAIDADGSRSHATVDYSIISGNRGRVFQLEPRLAEVGDGVGPGPQALGCLVLLEPLDFESLTQYNLTVTAADRGQPPRSSAVPVTVTVLDVNDNPPVFTRASYRVTVPEDMPVGAELLHVEASDADPGPHGLVHFTLSSGDPLGLFELDENSGALRLAHPLDCETQAQHQLVVQAADPAGTHFALVPVTVEVQDVNDHGPAFPLSLLSTSLAENQPPGTLVTTLHAMDGDAGTFGRLRYTLLEAVPGPEGREAFSLNSSTGELRARVPFDYEHTGSFRLLVGAADAGNLSASVTVSVLITGEDEYDPVFLAPSFHFQVPEGAQRGHSLGHVQATDEDGGADGLVLYSLATSSPYFGINQTTGALYLRVDSRAPGSGTATSGGGGRTRREAPRELRLEVVARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVLGLVRARSRKAEAAPGPMSQTAPIASSSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAGGPYPRGGSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDADGLSDTSCEPPAPDTWYKGRKAGLLLPGAGATLYREEGPPATATAFLGGCGLSPAPTGDYGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAHPGAKSVPPKPASTAATRAIFPPASHRSPISHEGSLSSAAMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSTESGLEPPDDTELRI
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Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation (By similarity).
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D4AD37
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IMPA3_RAT
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Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase (Golgi-resident PAP phosphatase) (gPAPP) (EC 3.1.3.7) (3'(2'), 5'-bisphosphate nucleotidase 2) (Inositol monophosphatase domain-containing protein 1) (Myo-inositol monophosphatase A3) (Phosphoadenosine phosphate 3'-nucleotidase)
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MAPMGIRLSPLGVAVFFLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAEVAVDGGTVDLREMLAVAVLAAERGGDEVRRVRESNVLHEKSKGKTREGAEDKMTSGDVLSNRKMFYLLKTAFPNVQINTEEHVDASDKEVIVWNRKIPEDILKEIAAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDSGSNVKARSSYNEKTPKIIVSRSHAGMVKQVALQTFGNQTLIIPAGGAGYKVLALLDVPDMTQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKSGH
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Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
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D4AD53
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KCNG1_RAT
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Potassium voltage-gated channel subfamily G member 1 (Voltage-gated potassium channel subunit Kv6.1)
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MTLLPGDNSDYDYSALSCASDTSFHPAFFPQRQAIKGVFYRRAQRLGPQDDLHQSISLGDRRRQIIINVGGIKYSLPWTTLDEFPLTRLGQLKACTNFDDILSVCDDYDVTCNEFFFDRNPGAFGTILTFLRAGKLRLLREMCALSFQEELLYWGIAEDHLDGCCKRRYLQKIEEFAEMMEREDEEEALDSEDQESEGPSTSEGRLSRCMRRLRDMVEKPHSGLPGKVFACLSVLFVTVTAVNLSVSTLPSLREEEEQGQCSQMCHNVFIVESVCVGWFSLEFLLRFIQAPSKFAFLRSPLTLIDLVAILPYYVTLLVDGAASSRRKPSTGNSYLDKVGLVLRVLRALRILYVMRLARHSLGLQTLGLTARRCTREFGLLLLFLCVAIALFAPLLYVIENEMADSPEFTSIPACYWWAVITMTTVGYGDMVPRSTPGQVVALSSILSGILLMAFPVTSIFHTFSRSYLELKQEQERVLIRRAQYLIKTKSQLSGMSQDSDILFGSASSDTRDNN
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Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1.
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Subsets and Splits
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