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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O34714
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OXDC_BACSU
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Oxalate decarboxylase OxdC (EC 4.1.1.2)
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MKKQNDIPQPIRGDKGATVKIPRNIERDRQNPDMLVPPETDHGTVSNMKFSFSDTHNRLEKGGYAREVTVRELPISENLASVNMRLKPGAIRELHWHKEAEWAYMIYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVIAANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEGGKVYIADSTNFKVSKTIASALVTVEPGAMRELHWHPNTHEWQYYISGKARMTVFASDGHARTFNYQAGDVGYVPFAMGHYVENIGDEPLVFLEIFKDDHYADVSLNQWLAMLPETFVQAHLDLGKDFTDVLSKEKHPVVKKKCSK
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Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
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O34746
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FABH1_BACSU
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Beta-ketoacyl-[acyl-carrier-protein] synthase III 1 (Beta-ketoacyl-ACP synthase III 1) (KAS III 1) (EC 2.3.1.180) (EC 2.3.1.300) (3-oxoacyl-[acyl-carrier-protein] synthase 3 1) (3-oxoacyl-[acyl-carrier-protein] synthase III 1) (Branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase 1) (bFabH1)
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MKAGILGVGRYIPEKVLTNHDLEKMVETSDEWIRTRTGIEERRIAADDVFSSHMAVAAAKNALEQAEVAAEDLDMILVATVTPDQSFPTVSCMIQEQLGAKKACAMDISAACAGFMYGVVTGKQFIESGTYKHVLVVGVEKLSSITDWEDRNTAVLFGDGAGAAVVGPVSDDRGILSFELGADGTGGQHLYLNEKRHTIMNGREVFKFAVRQMGESCVNVIEKAGLSKEDVDFLIPHQANIRIMEAARERLELPVEKMSKTVHKYGNTSAASIPISLVEELEAGKIKDGDVVVMVGFGGGLTWGAIAIRWGR
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Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain.
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O34748
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RECQ_BACSU
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Probable ATP-dependent DNA helicase RecQ (EC 3.6.4.12)
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MLHRAQSLLAHYFGYEKFRSGQDEAIRLVTEARQNTACIMPTGGGKSICYQIPALMFEGTTIVISPLISLMKDQVDALEEAGINAAYINSTQSNQEIYERLNGLKEGAYKLFYITPERLTSIEFIRILQGIDVPLVAIDEAHCISQWGHDFRPSYRNIEILFRELHDKPVIMALTATATPEVHDDICKQLHIQKENTVYTGFSRENLTFKVVKGENKDRFIDEYVQNNRHEAGIVYTATRKEADRIYERLKRNQVRAGRYHGGLADDVRKEQQERFLNDELQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDGLASECVLLFSPQDIMVQRFLIEQSEHEEKQKQDLKKLRQMVDYCHTEDCLQRFILMYFGEKEPDACGQCGNCTDTRAAHDVTREAQMVLSCIIRMKERFGKTMVAQVLAGSKNKKVLENGFSDLSTYGILKHQSVGEISDFIEFLISDDFIRMSDGTFPTLFVSSKGRNVLKGELSVARKEALKAAAITENDELFERLRMVRKEIAAEQGVPPFVVFSDQTLKEMSGKQPVNDDELLSIKGVGEQKRAKYGRLFLQEIQAYARMTD
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Probable DNA helicase. Required for DNA repair and intramolecular recombination probably has overlapping function with RecS (AC P50729). It probably acts to help generate ss-DNA from ds-DNA breaks.
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O34777
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OHRR_BACSU
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Organic hydroperoxide resistance transcriptional regulator
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MENKFDHMKLENQLCFLLYASSREMTKQYKPLLDKLNITYPQYLALLLLWEHETLTVKKMGEQLYLDSGTLTPMLKRMEQQGLITRKRSEEDERSVLISLTEDGALLKEKAVDIPGTILGLSKQSGEDLKQLKSALYTLLETLHQKN
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Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.
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O34798
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PDAC_BACSU
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Peptidoglycan-N-acetylmuramic acid deacetylase PdaC (Peptidoglycan MurNAc deacetylase) (EC 3.5.1.-) (Polysaccharide deacetylase PdaC)
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MLAKRIKWFHVLIAVVCVVGLIGFFHNHSLKKETVMNKVRTDSQYGNVEIATLVNDGKTFNYAVNYPVFKNEKMDSALKRFAEKEVRQFQKETKDVDQEHTTKRNELNVDYKIVHYAKQTVAIVFNEYKYIGGAHGQTVKKTFNYDFSKQAFLSIDDIFKEDADYLHKLSLIAYHELKKNKDIAADDALLKEGTAPKKENFSRFAIKEDYIELYFDTYQVAAGYLGEQSIAIKKSLLKDILKEQYIDKAKNKNKIKEQKPKHEVISLPKEETVDPNQKVIALTFDDGPNPATTNQILDSLKKYKGHATFFVLGSRVQYYPETLIRMLKEGNEVGNHSWSHPLLTRLSVKEALKQINDTQDIIEKISGYRPTLVRPPYGGINDELRSQMKMDVALWDVDPEDWKDRNKKTIVDRVMNQAGDGRTILIHDIYRTSADAADEIIKKLTDQGYQLVTVSQLEEVKKQREAK
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Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in peptidoglycan, a modification that confers resistance to lysosyme. Is not able to deacetylate N-acetylglucosamine (GlcNAc) residues in peptidoglycan, but can deacylate chitin oligomers such as GlcNAc4 and GlcNAc5. Is essentially not active toward chitosan (partially deacetylated GlcNAc polymer) and has very low activity toward chitin (GlcNAc polymer). Does not deacetylate GlcNAc.
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O34817
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NAGR_BACSU
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HTH-type transcriptional repressor NagR (N-acetylglucosamine utilization regulator)
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MNINKQSPIPIYYQIMEQLKTQIKNGELQPDMPLPSEREYAEQFGISRMTVRQALSNLVNEGLLYRLKGRGTFVSKPKMEQALQGLTSFTEDMKSRGMTPGSRLIDYQLIDSTEELAAILGCGHPSSIHKITRVRLANDIPMAIESSHIPFELAGELNESHFQSSIYDHIERYNSIPISRAKQELEPSAATTEEANILGIQKGAPVLLIKRTTYLQNGTAFEHAKSVYRGDRYTFVHYMDRLS
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Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization. Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions. Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3'. Also acts as a weak repressor of mapB expression.
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O34840
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CHAA_BACSU
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Ca(2+)/H(+) antiporter ChaA
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MNRIFFILVAAGVPLSVIGSLMHWPSAVLFAVYCVTIIALASYMGRATESLSIIAGPRIGGLLNATFGNAVELIISLFALKEGLTGIVLASLTGSVLGNLLLVAGLSFFVGGLKYKRQEFNIHDARHNSGLLIFAIIVAFVIPEVFSVGMGNASKLNLSIGISIIMILLYVAALYFKLVTHRGVYQPNNAAQTEEEEEPEWSGKVATIVLFAATIVVAYISENLVHTFHSVAEQFGWSELFIGVIIVAIVGNAAEHASAIIMAFKNKMDIAVEIAVGSTLQIAMFVAPVLVICSIFFPTSMPLVFTLPELVAMVSAVLLMIAISNDGDSNWFEGATLLAAYVIMAIGFFLL
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Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons. Does not transport sodium or potassium.
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O34860
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RSBRB_BACSU
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RsbT co-antagonist protein RsbRB (Stressosome protein RsbRB)
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MKLNEKLYAFFSEHVEQMAEEWIETMEESDPNSLYALHNATVTEELKEQDREFYRHLNYMYVLPEKQFLEEFQEWVIELTNDQKHLDTPVQYVIREFMRNRRLYTKYFEKFAEENESAFEPGEKQKWADLIVKVFDFTIYTFVDHAEMNAKQQLNAQREMILELSSPVITLSKSTALLPLVGDIDTERAKFILENTLQACAKRRVEHLLIDLSGVVVVDTMVAHQIFKLIEALNLIGVRSTLSGIRPEIAQTAVQLGIDFSNITIKTNLAQALNYHQ
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One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.
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O34919
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YOSS_BACSU
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SPbeta prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase YosS (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase)
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MQIKIKYLDETQTRINKMEQGDWIDLRAAEDVAIKKDEFKLVPLGVAMELPEGYEAHVVPRSSTYKNFGVIQTNSMGVIDESYKGDNDFWFFPAYALRDTKIKKGDRICQFRIMKKMPAVDLIEVDRLGNGDRGGHGSTGTK
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Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP, so that uracil cannot be incorporated into DNA. The Ser-62 side chain changes its position upon ligand-binding to make contacts with the nucleotide phosphates.
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O34926
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CYPX_BACSU
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Pulcherriminic acid synthase (EC 1.14.15.13) (CYP134A1) (Cyclo-L-leucyl-L-leucyl dipeptide oxidase) (Cytochrome P450 CypX)
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MSQSIKLFSVLSDQFQNNPYAYFSQLREEDPVHYEESIDSYFISRYHDVRYILQHPDIFTTKSLVERAEPVMRGPVLAQMHGKEHSAKRRIVVRSFIGDALDHLSPLIKQNAENLLAPYLERGKSDLVNDFGKTFAVCVTMDMLGLDKRDHEKISEWHSGVADFITSISQSPEARAHSLWCSEQLSQYLMPVIKERRVNPGSDLISILCTSEYEGMALSDKDILALILNVLLAATEPADKTLALMIYHLLNNPEQMNDVLADRSLVPRAIAETLRYKPPVQLIPRQLSQDTVVGGMEIKKDTIVFCMIGAANRDPEAFEQPDVFNIHREDLGIKSAFSGAARHLAFGSGIHNCVGAAFAKNEIEIVANIVLDKMRNIRLEEDFCYAESGLYTRGPVSLLVAFDGA
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Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with larger hydrophobic side chains bind in a similar regime to cLL.
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O34928
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PDAA_BACSU
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Peptidoglycan-N-acetylmuramic acid deacetylase PdaA (Peptidoglycan MurNAc deacetylase) (EC 3.5.1.-)
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MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYLGNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHIIGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRLGYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLKKQGYTFKSIDDLMFEKEMRLPSL
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Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate.
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O34939
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YDIO_BACSU
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Type II methyltransferase M1.BsuMI (M1.BsuMI) (EC 2.1.1.37) (BsuMI modification methylase subunit YdiO) (Cytosine-specific methyltransferase M1.BsuMI)
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MTNFILNENKQLSLAIEDENIENFYIDGTDLVRKIIRRSGSGVTSRVPVLSTQDLENKNLHELYDESWLRMKNRPNTELTTESINIADLFSGCGGLSLGVWEACRALGINPRFSFACDLNEAALSVYEKNFSPDFSLNESIEKHINGELGAPLTVEEQRIKDKVKKIDFILAGPPCQGHSDLNNHTRRKDPRNALLMRVSRVIELFQPSSVLVENVPGIIHDKSGSFKEFKNHLKTQGYYFDEIVLNAEKLGVSQARRRYFIFASKTPVSSLNQINEFYSTNSRPISWAISDLVENVGDDIFNTASEHSLENKRRIEYLFENNLFELPNSERPDCHRLKPHSYKSVYGRMYWDRPAPTITRGFGSTGQGRFVHSLLKRTITPHEAARIQFFPDFFNFGDLRRRQYQDVIGNAVPSKLSYLLALHQLR
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A methylase, recognizes the double-stranded sequence 5'-YTCGAR-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BsuMI endonuclease.
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O34952
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LTAS2_BACSU
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Lipoteichoic acid synthase 2 [Cleaved into: Glycerol phosphate lipoteichoic acid synthase 2 (LTA synthase 1) (EC 2.7.8.-) (Polyglycerol phosphate synthase 2); Processed glycerol phosphate lipoteichoic acid synthase 2]
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MKTFIKERGLAFFLIAVVLLWIKTYVGYVLNFNLGIDNTIQKILLFVNPLSSSLFFLGFGLLFKKKLQQTAIIVIHFLMSFLLYANIVYYRFFNDFITIPVIMQAKTNGGQLGDSAFSLMRPTDAFYFIDTIILIILAIKVNKPAETSSKKSFRIIFASSILVFLINLAVAESDRPELLTRSFDRNYLVKYLGTYNFTIYDAVQNIKSNSQRALADSSDVTEVENYMKANYDVPNNVYFGKAEGKNVIYVSLESLQSFIIDYKIDGKEVTPFLNKLAHDNETFYFDNFFHQTGQGKTSDAEFMMENSLYPLAQGSVFVNKAQNTLQSVPAILKSKNYTSATFHGNTQTFWNRNEMYKAEGIDKFFDSAYYDMNEENTKNYGMKDKPFFKESMPLLESLPQPFYTKFITLSNHFPFGMDEGDTDFPAGDFGDSVVDNYFQSAHYLDQSIEQFFNDLKKDGLYDKSIIVMYGDHYGISENHNKAMAKVLGKDEITDYDNAQLQRVPLFIHAAGVKGEKVHKYAGDVDVAPTILHLLGVDTKDYLMSGSDILSKEHREVIPFRNGDFISPKYTKISGKYYDTKTGKELDESEVDKSEDSLVKKELEMSDKIINGDLLRFYEPKGFKKVNPSDYDYTKHDEDSSETSKDNEDK
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Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate.
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O34962
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MAO4_BACSU
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Bifunctional malic/malolactic enzyme (EC 1.1.1.40) (EC 4.1.1.101) (Malolactic enzyme) (MLE) (NADP-dependent malic enzyme) (NADP-ME)
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MSLREEALHLHKVNQGKLESKSKVEVRNAKDLSLAYSPGVAEPCKDIHEDINKVYDYTMKGNMVAVVTDGTAVLGLGNIGPEAALPVMEGKAVLFKSFAGVDAFPIALNTNDVDKIVETVKLLEPTFGGVNLEDIAAPNCFIIEERLKKETNIPVFHDDQHGTAIVTVAGLVNALKLSGKSMSSIKVVANGAGAAGIAIIKLLHHYGVRDIVMCDSKGAIYEGRPNGMNDVKNEVAKFTNQDRKDGSLKDVIVDADVFIGVSVAGALTKEMVQSMAKDPIIFAMANPNPEIMPEDAREAGASVVGTGRSDFPNQVNNVLAFPGIFRGALDVRATHINEEMKIAAVEAIASLVSEDELSADYVIPAPFDKRVAPAVAKAVAKAAMETGVARITVDPEEVAEKTRKLTIIGE
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Bifunctional enzyme with both malic and malolactic enzyme activities. In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate. Can use NAD and NADP, but with a very strong preference for NADP. In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate. During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions. Can also catalyze the decarboxylation of oxaloacetate.
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O35002
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CTPB_BACSU
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Carboxy-terminal processing protease CtpB (C-terminal processing protease) (EC 3.4.21.102)
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MNQKIMAVIAAGSMLFGGAGVYAGINLLEMDKPQTAAVPATAQADSERDKAMDKIEKAYELISNEYVEKVDREKLLEGAIQGMLSTLNDPYSVYMDKQTAKQFSDSLDSSFEGIGAEVGMEDGKIIIVSPFKKSPAEKAGLKPNDEIISINGESMAGKDLNHAVLKIRGKKGSSVSMKIQRPGTKKQLSFRIKRAEIPLETVFASEKKVQGHSVGYIAISTFSEHTAEDFAKALRELEKKEIEGLVIDVRGNPGGYLQSVEEILKHFVTKDQPYIQIAERNGDKKRYFSTLTHKKAYPVNVITDKGSASASEILAGALKEAGHYDVVGDTSFGKGTVQQAVPMGDGSNIKLTLYKWLTPNGNWIHKKGIEPTIAIKQPDYFSAGPLQLKEPLKVDMNNEDVKHAQVLLKGLSFDPGREDGYFSKDMKKAVMAFQDQNKLNKTGVIDTRTAETLNQQIEKKKSDEKNDLQLQTALKSLFVN
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Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.
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O35013
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YTKD_BACSU
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Putative 8-oxo-dGTP diphosphatase YtkD (8-oxo-dGTPase) (EC 3.6.1.55) (7,8-dihydro-8-oxoguanine-triphosphatase) (dGTP pyrophosphohydrolase)
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MYEFKDYYQNTVQLSFDDQPFSDSPKHVWVICRFGGKWLLTEHEDRGYEFPGGKVEPMECAEEAALREVKEETGARVKSLKYLGQYKVLGKEKVIVKNIYFADIEKLEKQADYFETKGPVLFHELPENLSRNKKFSFIMKDSVLPISLKKLKESGWIE
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Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Functions, in conjunction with MutT, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores. According to PubMed:15576788, phosphohydrolase that catalyzes the hydrolysis of all common nucleoside triphosphates as well as of the mutagenic analog 8-oxo-dGTP. The high catalytic efficiency on dGTP is in contrast to results from PubMed:14761999. According to PubMed:14761999, catalyzes the hydrolysis of 8-oxo-dGTP with a specific activity 413 times higher than that exhibited against dGTP. Preferentially catalyzes the hydrolysis of 8-oxo-dGTP and 8-oxo-GTP. According to PubMed:15576788, hydrolyzes nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate. {ECO:0000250, ECO:0000269|PubMed:14761999, ECO:0000269|PubMed:15576788}.
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O35047
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HOP2_MOUSE
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Homologous-pairing protein 2 homolog (PSMC3-interacting protein) (Proteasome 26S ATPase subunit 3-interacting protein) (Tat-binding protein 1-interacting protein) (TBP-1-interacting protein)
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MSKSRAEAAAGAPGIILRYLQEQNRPYSAQDVFGNLQKEHGLGKAAVVKALDQLAQEGKIKEKTYGKQKIYFADQNQFDTVSDADLHGLDASIVALTAKVQSLQQSCRHMEAELKELTSALTTPEMQKEIQELKKECAQYTERLKNIKAATNHVTPEEKEKVYRDRQKYCKEWRKRKRMTTELCDAILEGYPKSKKQFFEEVGIETDEDHNVLLPDP
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Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3.
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O35048
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3BHS7_RAT
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3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181) (Confluent 3Y1 cell-associated 2)
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MADSAQVPALVYLVTGGCGFLGEHIVRMLLEWEPRLRELRVFDLHLSSWLEELKTGPVQVTAIQGDVTQAHEVAAAMAGSHVVIHTAGLVDVFGKASPETIHKVNVQGTQNVIDACVQTGTRLLVYTSSMEVVGPNVKGHPFYRGNEDTPYEAIHRHPYPCSKALAEQLVLEANGRKGLRFGGRLFRAIPASVEHGRVYVGNVAWMHILVARELEQRAALMGGQVYFCYDKSPYKSYEDFNMEFLSPCGLRLIGTHPLLPYWLLVLLTALNALLQWLLRPLVLYTPLLNPYTLAVANTTFTVSTNKAQRHFGYKPLFSWEESRARTIHWVQAMEGSAW
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The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis. Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells.
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O35049
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NSMA2_RAT
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Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Confluent 3Y1 cell-associated protein 1) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II)
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MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLVASFIPTTYEKRQRADDPCYLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKSPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGSDGARAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRAQEADDPAPGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGSNSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAIRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDINGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
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Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location (By similarity). Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. May be involved in IL-1-beta-induced JNK activation in hepatocytes. May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions.
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O35052
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CDS1_RAT
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Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS 1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1)
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MLELRHRGGCPGPGGAGTPPPREGEAAGGDHETESTSDKETDIDDRYGDLDARGDSDVPEVPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQVKCFQEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLIRYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMIWFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVIFGFIAAYVLSKYQYFVCPVEYRSDVNSFVTECEPSELFQLQNYSLPPFLQAVLSRETVSLYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRGPNPSKVLQQLLVLQPEQQLNIYRTLKIHLTEKGILQPTWKV
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Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits almost no acyl chain preference for PA, showing no discrimination for the sn-1/sn-2 acyl chain composition of PAs (By similarity). Plays an important role in regulatinng the growth of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity). Positively regulates the differentiation and development of adipocytes (By similarity).
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O35054
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CLD4_MOUSE
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Claudin-4 (Clostridium perfringens enterotoxin receptor) (CPE-R) (CPE-receptor)
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MASMGLQVLGISLAVLGWLGIILSCALPMWRVTAFIGSNIVTAQTSWEGLWMNCVVQSTGQMQCKMYDSMLALPQDLQAARALMVISIIVGALGMLLSVVGGKCTNCMEDETVKAKIMITAGAVFIVASMLIMVPVSWTAHNVIRDFYNPMVASGQKREMGASLYVGWAASGLLLLGGGLLCCSCPPRSNDKPYSAKYSAARSVPASNYV
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Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
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O35074
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PTGIS_MOUSE
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Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase)
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MSWAALLGLLAVLLLLLLLLSRRRARRPGEPPLDLGSIPWLGHALEFGRDAASFLTRMKEKHGDIFTVLVGGRYVTVLLDPHSYDTVVWELRTRLDFHPYAIFLMERIFDLQLPNFNPSEEKARMKPTLMHRDLQALTEAMYTNLRTVLLGDSTEAGSGWQETGLLEFSYNALLSAGYLTLYGVEASPRTHESQAQDRVHSADVFHTFRQLDLLLPKLARGSLSAGDKDHACSVKNRLWKLLSPARLASRADRSSWLESYLRHLEEMGVSEEMQARALVLQLWATQGNMGPTAFWLLLFLLKNPEALAAVRAELKHTVWQAEQPVSQMTTLPQKILDSMPVLDSVLNETLRLTAAPFITREVMADLALPMADGREFSLRRGDRLLLFPFLSPQKDPEIYTEPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNQCLGKSYAINSIKQFVVLLLTHFDLELGSEDTEVPEFDLSRYGFGLMQPEEDVPIRYRARL
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Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE).
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O35077
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GPDA_RAT
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Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (GPD-C) (GPDH-C) (EC 1.1.1.8)
|
MAGKKVCIVGSGNWGSAIAKIVGSNASQLAHFDPRVTMWVFEEDIGGRKLTEIINTQHENVKYLPGHKLPPNVVAVPDVVQAATGADILVFVVPHQFIGKICDQLKGHLKANTIGISLIKGIDEGPNGLKLISEVIGESLGIPMSVLMGANIASEVAEEKFCETTIGCKDPAQGQLLKELMQTPNFRITVVQEVDTVEICGALKNIVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGSVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKEMLNGQKLQGPQTARELHSILQHKGLVDKFPLFTAVYKVCYEGQPVGEFICCLQNHPEHM
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Has glycerol-3-phosphate dehydrogenase activity.
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O35082
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KLOT_MOUSE
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Klotho (EC 3.2.1.31) [Cleaved into: Klotho peptide]
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MLARAPPRRPPRLVLLRLLLLHLLLLALRARCLSAEPGQGAQTWARFARAPAPEAAGLLHDTFPDGFLWAVGSAAYQTEGGWRQHGKGASIWDTFTHHSGAAPSDSPIVVAPSGAPSPPLSSTGDVASDSYNNVYRDTEGLRELGVTHYRFSISWARVLPNGTAGTPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDTYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGVRGSSRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGRVSIALSSHWINPRRMTDYNIRECQKSLDFVLGWFAKPIFIDGDYPESMKNNLSSLLPDFTESEKRLIRGTADFFALSFGPTLSFQLLDPNMKFRQLESPNLRQLLSWIDLEYNHPPIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIRLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKELLPKSSALFYQKLIEDNGFPPLPENQPLEGTFPCDFAWGVVDNYVQVDTTLSQFTDPNVYLWDVHHSKRLIKVDGVVAKKRKPYCVDFSAIRPQITLLREMRVTHFRFSLDWALILPLGNQTQVNHTVLHFYRCMISELVHANITPVVALWQPAAPHQGLPHALAKHGAWENPHTALAFADYANLCFKELGHWVNLWITMNEPNTRNMTYRAGHHLLRAHALAWHLYDDKFRAAQKGKISIALQADWIEPACPFSQNDKEVAERVLEFDIGWLAEPIFGSGDYPRVMRDWLNQKNNFLLPYFTEDEKKLVRGSFDFLAVSHYTTILVDWEKEDPMKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLRFKYGDLPMYVTANGIDDDPHAEQDSLRIYYIKNYVNEALKAYVLDDINLCGYFAYSLSDRSAPKSGFYRYAANQFEPKPSMKHYRKIIDSNGFLGSGTLGRFCPEEYTVCTECGFFQTRKSLLVFISFLVFTFIISLALIFHYSKKGQRSYK
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May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 241 and 874, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D. Essential factor for the specific interaction between FGF23 and FGFR1. The Klotho peptide generated by cleavage of the membrane-bound isoform may be an anti-aging circulating hormone which would extend life span by inhibiting insulin/IGF1 signaling.
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O35083
|
PLCA_MOUSE
|
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 1) (1-AGP acyltransferase 1) (1-AGPAT 1) (Lysophosphatidic acid acyltransferase alpha) (LPAAT-alpha)
|
MELWPGAWTALLLLLLLLLSTLWFCSSSAKYFFKMAFYNGWILFLAILAIPVCAVRGRNVENMKILRLLLLHAKYLYGIRVEVRGAHHFPPTQPYVVVSNHQSSLDLLGMMEVLPDRCVPIAKRELLWAGSAGLACWLAGIIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIIPIVMSSYQDFYSKKERRFTSPGRCQVRVLPPVSTEGLTPDDVPALADSVRHSMLTIFREISTDGLGGGDCLKKPGGAGEARL
|
Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
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O35084
|
CP27B_MOUSE
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25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1)
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MTQAVKLASRVFHRIHLPLQLDASLGSRGSESVLRSLSDIPGPSTLSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPTLVEQLLRQESHCPERCSFSSWAEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDNVVRDLVRRLRRQRGRGSGLPGLVLDVAGEFYKFGLESIGAVLLGSRLGCLEAEVPPDTETFIHAVGSVFVSTLLTMAMPNWLHHLIPGPWARLCRDWDQMFAFAQRHVELREGEAAMRNQGKPEEDMPSGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWTLYELSRHPDVQTALHSEITAGTRGSCAHPHGTALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDIRVGNYVIPQDTLVSLCHYATSRDPTQFPDPNSFNPARWLGEGPTPHPFASLPFGFGKRSCIGRRLAELELQMALSQILTHFEVLPEPGALPIKPMTRTVLVPERSINLQFVDR
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A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1-alpha position to form the hormonally active form of vitamin D3, 1alpha,25-dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR). Has 1-alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway. Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2 (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
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O35085
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ARX_MOUSE
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Homeobox protein ARX (Aristaless-related homeobox)
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MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRADQEKAMQGSPKSSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELSGPGGVAHPEERLSAASGPGSAPAAGGGTGAEDDEEELLEDEEDEEEEEELLEDDDEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAGSDSEEGLLKRKQRRYRTTFTSYQLEELERAFQKTHYPDVFTREELAMRLDLTEARVQVWFQNRRAKWRKREKAGAQTHPPGLPFPGPLSATHPLSPYLDASPFPPHHPALDSAWTAAAAAAAAAFPSLPPPPGSASLPPSGAPLGLSTFLGAAVFRHPAFISPAFGRLFSTMAPLTSASTAAALLRQPTPAVEGAVASGALADPATAAADRRASSIAALRLKAKEHAAQLTQLNILPGTSTGKEVC
|
Transcription factor (By similarity). Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C (By similarity). Positively modulates transcription of KDM5C. Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcription regulator ZNF711 synergy may be related to enrichment of histone H3K4me3 in regulatory elements (By similarity). Required for normal brain development. Plays a role in neuronal proliferation, interneuronal migration and differentiation in the embryonic forebrain. May also be involved in axonal guidance in the floor plate.
|
O35089
|
CNIH2_MOUSE
|
Protein cornichon homolog 2 (CNIH-2) (Cornichon family AMPA receptor auxiliary protein 2) (Cornichon-like protein)
|
MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF
|
Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors.
|
O35095
|
NCDN_RAT
|
Neurochondrin (Neurite outgrowth-related protein from the rat brain) (Norbin)
|
MSCCDLAAAGQLGKAGIMASDCEPALNQAESRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELASHPQVLNKIPILCTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQRAEDASKFELCQLLPLFLPPTTVPPECHRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPVGSSGSKFLALLVNLACVEVRLALEETGTEVKEDVVTACYALMELGIQECTRCEQSLLKEPQKVQLVSIMKEAIGAVIHYLLRVGPEKQKEPFVFASVRILGAWLAEETSSLRKEVCQLLPFLVRYAKTLYEEAEEASDISQQVANLAISPTTPGPAWPGDALRLLLPGWCHLTVEDGPREILIKEGAPSLLCKYFLQQWELTSPGHDTSVLPDSVEIGLQTCCHIFLNLVVTAPGLIKRDACFTSLMNTLMTSLPSLVQQQGRLLLAANVATLGLLMARLLSTSPALQGTPASRGFFAAAILFLSQSHVARATPGSDQAVLALSPDYEGIWADLQELWFLGMQAFTGCVPLLPWLAPAALRSRWPQELLQLLGSVSPNSVKPEMVAAYQGVLVELARANRLCREAMRLQAGEETASHYRMAALEQCLSEP
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Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth.
|
O35099
|
M3K5_MOUSE
|
Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
|
MGTEAGEGITFSVPPFASVGFCTIPEGGSCRRGGGAATAAEGEPSLQPLLVPPPPPPPGSFWNVESAAAPGTSCPTTAPGSSATRGRGNSGSGGGRRTTVAYVINEASQGQLVVAESEALQSLREACEAVGATLETLHFGKLDFGETAVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTVCTGNYTFIPYMVTPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFVQLLKVAQASSSQYFRESILSDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEEQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHLRVIQASEKLFRLKTPAWYLKSIVETILIYKHFVKLTTEQPSAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFGASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKRFFEMVNTITEEKGRGAEDGDCEGDSLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLIDEFLKVSSKKKKTQPKLSALSTGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKADPFSFKARAKSCGEKDGKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKVVRNLMESLAQGAEEPKLKWEHITTLISSLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADPEDLDVEDEHEELSSNQTVRRPQAITEDAVATSGVSTLSSTVSHDSQNAHRSLNVQLGRMKIETNRLLEELVRKERELQALLHQAIEEKDQEIRHLKLKSQPIDIPGFPVCHLNSPGTTTEDSELPGWLRENGADEDTISRFLAEDYTLVDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKC
|
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1).
|
O35111
|
KCNK3_MOUSE
|
Potassium channel subfamily K member 3 (Acid-sensitive potassium channel protein TASK-1) (Cardiac two pore background K(+) channel) (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1) (cTBAK-1)
|
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAVGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGVGVGVGGSGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLAAFRGLMKRRSSV
|
pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.
|
O35112
|
CD166_RAT
|
CD166 antigen (Activated leukocyte cell adhesion molecule) (HB2) (KG-CAM) (Protein MEMD) (SB-10 antigen) (CD antigen CD166)
|
MASKGSPSCRLVFCLLISAAVLRPGLGWYTVNSAYGDTIVMPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLSLSENYTLSINNAKISDEKRFVCMLVTEDNVFEAPTLVKVFKQPSKPEIVNRAAFLETEQLKKLGDCISRDSYPDGNITWYRNGKVLQPVDGEVSILFKKEIDPGTQLYTMTSSLEYKTTKSDIQMPFTCSVTYYGPSGQKTIYSEQAIFDIYYPTEQVTIQVLPPKNAIKEGDNITLQCLGNGNPPPEEFMFYLPGQAEGIRSSNTYTLTDVRRNATGDYKCSLIDQRNMAASTTITVHYLDLSLNPSGEVTKQIGDTLPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADDISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA
|
Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance axons grow preferentially on surfaces that contain ALCAM (By similarity). Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity).
|
O35114
|
SCRB2_MOUSE
|
Lysosome membrane protein 2 (85 kDa lysosomal membrane sialoglycoprotein) (LGP85) (Lysosome membrane protein II) (LIMP II) (Scavenger receptor class B member 2)
|
MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFNSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANIQFGENGTTISAVTNKAYVFERNQSVGDPNVDLIRTINIPLLTVVDLAQLTLLRELIEAMLKAYQQKLFVIHTVHELLWGYKDEILSLVHIFKPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFSKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDEVLYLFPSDLCRSVHITFSSFENVEGLPAFRYKVPAEILANTSENAGFCIPEGNCMDSGVLNISICKNGAPIIMSFPHFYQADEKFVSAIKGMHPNKEEHESFVDINPLTGIILRGAKRFQINTYVRKLDDFVETGDIRTMVFPVMYLNESVLIDKETANQLKSVINTTLVVTNIPYIIMALGVFFGLVFTWLACRGQGSMDEGTADERAPLIRT
|
Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting.
|
O35115
|
FHL2_RAT
|
Four and a half LIM domains protein 2 (FHL-2) (LIM domain protein DRAL) (Skeletal muscle LIM-protein 3) (SLIM-3)
|
MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYRDQPWHRECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
|
May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation (By similarity). Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes.
|
O35116
|
CTND2_RAT
|
Catenin delta-2
|
FPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGEANGKDAESSGCWGKKKKKKKSQDQWDGVG
|
Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses. Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation. May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. Functions as a transcriptional activator when bound to ZBTB33 (By similarity).
|
O35118
|
GFRA3_MOUSE
|
GDNF family receptor alpha-3 (GDNF receptor alpha-3) (GDNFR-alpha-3) (GFR-alpha-3)
|
MGLSWSPRPPLLMILLLVLSLWLPLGAGNSLATENRFVNSCTQARKKCEANPACKAAYQHLGSCTSSLSRPLPLEESAMSADCLEAAEQLRNSSLIDCRCHRRMKHQATCLDIYWTVHPARSLGDYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLHDKCDRLRKAYGEACSGIRCQRHLCLAQLRSFFEKAAESHAQGLLLCPCAPEDAGCGERRRNTIAPSCALPSVTPNCLDLRSFCRADPLCRSRLMDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFISKVNTTVALSCTCRGSGNLQDECEQLERSFSQNPCLVEAIAAKMRFHRQLFSQDWADSTFSVVQQQNSNPALRLQPRLPILSFSILPLILLQTLW
|
Receptor for the glial cell line-derived neurotrophic factor, artemin. Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase (By similarity).
|
O35119
|
TRPC4_RAT
|
Short transient receptor potential channel 4 (Trp4) (TrpC4) (Capacitative calcium entry channel 1) (CCE1)
|
MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFKININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSEYEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTDFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLVKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAAMIREAKTEEGLTEENVKELKQDISSFRFEVLGLLRGSKLSTIQSANAASSASSADSDEKSHSEGNGKDKRKNLSLFDLTTLIHPRSAVIASERHNLSNGSALVVQEPPREKQRKVNFVADIKNFGLFHRRSKQNAAEQNANQIFSVSEEITRQQAAGALERNIQLESKGLASRGDRSIPGLNEQCVLVDHRERNTDTLGLQVGKRVCSSFKSEKVVVEDTVPIIPKEKHAQEEDSSIDYDLSPTDTVAHEDYVTTRL
|
Thought to form non-selective a receptor-activated calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion.
|
O35126
|
ATN1_MOUSE
|
Atrophin-1 (Dentatorubral-pallidoluysian atrophy protein homolog)
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MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
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Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation.
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O35129
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PHB2_MOUSE
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Prohibitin-2 (B-cell receptor-associated protein BAP37) (Repressor of estrogen receptor activity)
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MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK
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Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus. In the mitochondria, together with PHB, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner. Also regulates cytochrome-c oxidase assembly (COX) and mitochondrial respiration. Binding to sphingoid 1-phosphate (SPP) modulates its regulator activity. Has a key role of mitophagy receptor involved in targeting mitochondria for autophagic degradation. Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6. In the nucleus, serves as transcriptional co-regulator (Probable). Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. In the plasma membrane, is involved in IGFBP6-induced cell migration (By similarity). Cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.
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O35130
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NEP1_MOUSE
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Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) (18S rRNA (pseudouridine(1248)-N1)-methyltransferase) (18S rRNA Psi1248 methyltransferase) (Nucleolar protein EMG1 homolog) (Protein C2f) (Ribosome biogenesis protein NEP1)
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MSAASGGFQPRERRFSVQEQDWETTPPKKLRLGAGSKCGGRRLIVVLEGASLETVKVGKTYELLNCDRHKSMLLKNGRDPGEVRPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKIGTSFSVEDISDIRELVPSSDPVVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKVTTAFEEVWGVI
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S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position (By similarity). Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity).
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O35132
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CP27B_RAT
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25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1)
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MTQAVKLASRVFHRVQLPSQLGSDSVLRSLSDIPGPSTPSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPALVEQLLRQESHCPERCSFSSWSEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDSVVSDLVRRLRRQRGRGSGLPDLVLDVAGEFYKFGLEGIGAVLLGSRLGCLEAEVPPDTETFIEAVGSVFVSTLLTMAMPSWLHRLIPGPWARLCRDWDQMFAFAQKHVEQREGEAAVRNQGKPEEDLPTGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWALYELSRHPEVQSALHSEITGAVNPGSYAHLQATALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDICVGNYVIPQDTLVSLCHYATSRDPAQFREPNSFNPARWLGEGPAPHPFASLPFGFGKRSCIGRRLAELELQMALAQILTHFEVLPEPGALPVKPMTRTVLVPERSIHLQFVDR
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Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.
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O35134
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RPA1_MOUSE
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DNA-directed RNA polymerase I subunit RPA1 (RNA polymerase I subunit A1) (EC 2.7.7.6) (DNA-directed RNA polymerase I largest subunit) (DNA-directed RNA polymerase I subunit A) (RNA polymerase I 194 kDa subunit) (RPA194)
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MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDYLGNPSANGLYDLALGPADSKEVCATCVQDFNNCSGHLGHIDLPLTVYNPFLFDKLYLLLRGSCLSCHMLTCPRAAIYLLISQLRVLEVGALQAVYELERILSRFLEETGDPSAFEIQEELEEYTSKILQNNLLGSQGTHVKNVCESRSKLVAQFWKTHMAAKQCPHCKTGRSVVRKEHNSKLIITYPATVHKKSDQEGTELPEGVPEAPGIDKAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPVNRLGDQMFTNGQTVNLQAVMKDAVLIRKLLALMAQEQKLPCEMTELTIDKENDSSVAIDRSFLGLLPGPSLTDKLYNIWIRLQSHVNIVFDSEMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSSVDAAQREAVAKQLLTPATGAPKPQGTKVVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYAPLNLSGKAKIGSKAWVKEKPRPIPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVVRQRIIEESTQCGPQAVKAALSLPETASCDEIQGKWQDAHLSKDQRDFNMIDMKFKEEVNHYSNEINKACMPLGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLAGNYEVIMKSKHLHEVLSRADPQKVLGHIKAIKKWHHKHSGALLRKGAFLSFSQKIQAAVKALNLKGSIQNGRSPETQQMLQMWYDLDEESRWKYQKRAAPCPDPSLSVWRPDIYFASVSETFEKKIDDFSQEWAAQAERSYKKSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFDTKKALKKVKSLKKRLTRVCLGEVLQKVDIQESFCMGEKRNKFQVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKKNKASAFRNVNSRRATQKDLNDTEDSGRSQREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEEVQEEGNIKGDGVHQGHEPDEEEHLGLEEEESSQKPPRRHSRPQGAEAIKRRIQAVRESYSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHKAIVYTTKGITRCLLNETTNSKNEKELVLNTEGINLPELFKYSEILDLRRLYSNDIHAMANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
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DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
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O35136
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NCAM2_MOUSE
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Neural cell adhesion molecule 2 (N-CAM-2) (NCAM-2) (Neural cell adhesion molecule RB-8) (R4B12)
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MSLLLSFYLLGLLVRSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIMMPQKSFNATAERGEEMTLTCKASGSPDPTISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTLVCEAEGEPVPEITWKRAIDGVMFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDIEYAPKFVSNQTMYYSWEGNPINISCDVTANPPASIHWRREKLLLPAKNTTHLKTHSVGRKMILEIAPTSDNDFGRYNCTATNRIGTRFQEYILELADVPSSPHGVKIIELSQTTAKISFNKPESHGGVPIHHYQVDVKEVASETWKIVRSHGVQTMVVLSSLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA
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May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
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O35137
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ALX4_MOUSE
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Homeobox protein aristaless-like 4 (ALX-4)
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MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRGFPGGDKFGTTFLSAGAKGQGFGDAKSRARYGAGQQDLAAPLESSSGARGSFNKFQPQPPTPQPPPAPPAPPAHLYLQRGACKTPPDGSLKLQEGSGGHNAALQVPCYAKESNLGEPELPPDSEPVGMDNSYLSVKETGAKGPQDRASAEIPSPLEKTDSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWIGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVSDFLSVSGAGSHVGQTHMGSLFGAAGISPGLNGYEMNGEPDRKTSSIAALRMKAKEHSAAISWAT
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Transcription factor involved in skull and limb development.
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O35142
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COPB2_RAT
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Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102)
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MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKRFQPSRATAQQEPDGKPASSPVIMASQTTHKEEKSFQELEDDLDTMELEDIDTTDINLDEDILDD
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The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
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O35143
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ATIF1_MOUSE
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ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1)
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MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH
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Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
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O35144
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TERF2_MOUSE
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Telomeric repeat-binding factor 2 (TTAGGG repeat-binding factor 2) (Telomeric DNA-binding protein)
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MAAGAGTAGPASGPGVVRDPMASQPRKRPSREGGEGGEGERRSNTMAGGGGSSDSSGRAASRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRKLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKLRTDLLNIIREKNLAHPVIQNFSYEVFQQKMLRFLESHLDDTEPYLLTMAKKALKSESAASSTMREEKHPEPVEKPLREPPSRQPQNPPATIGIRTLKAAFKALSTAQDSEAAFAKLDQKDLVLANLASPSSPAHKHKRPRKDEHESAAPAEGEGGSDRQPRNSPMTISRLLLEEDSQSTEPSPGLNSSHKAMSASKPRALNQPHPGEKKPKASKDKWNSPNGLEEKEVWLEEDQLFEVQAPGEDRSSSLTRKQKWTIEESEWVKDGVRKYGEGNWAAISKSYPFVNRTAVMIKDRWRTMKKLGMN
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Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.
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O35147
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BAD_RAT
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Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
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MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ
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Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
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O35149
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ZNT4_MOUSE
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Probable proton-coupled zinc antiporter SLC30A4 (Lethal milk protein) (Solute carrier family 30 member 4) (Zinc transporter 4) (ZnT-4)
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MAGPGAWKRLKSLLRKDDTPLFLNDTSAFDFSDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQDLPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAVQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKSTAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTIQLQSYRQEVIRTCANCHSSST
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Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment. Controls zinc deposition in milk.
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O35152
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BET1L_RAT
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BET1-like protein (Golgi SNARE with a size of 15 kDa) (GOS-15) (GS15) (Vesicle transport protein GOS15)
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MADWTRAQSSGAVEEIVDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTVARSGRDTRKLLCGMAVVLIVAFFILSYLFSRTRT
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Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex.
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O35158
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CDON_RAT
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Cell adhesion molecule-related/down-regulated by oncogenes
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MHPDLGPLWKLLYVLVILCSSVSSDLATYFISEPLSAVQKLGRPVVLHCSAKPVTARISWLHNGKRLDRNTEQIKIHRGTLTILSLNPSLSGCYQCVANNSVGAVVSGPATVSADALADFDSSTMHVITAEKKNTGFIGCRVPESNPKAEVRYKIRGKWLMYSTGNYIILPSGNLQILNVSSKDKGSYKCAAYNPVTSELKVEPAGRKLLVSRPSSDGFHILHPALSQALAVLPHSPVTLECVVSGVPASQVYWLKDGQDCLSGSNWRRLYSHLATASIDPADSGNYSCVVGNNSSGDVKHVTYTVNVLEHASISKGLHDQKVSLGATVRFTCEVHGNPAPNRTWFHNAQPIRPSSRHLTEGSVLKITGVIMEDSGLYQCMADNGIGFMQSTGRLQIEQDSGQRPVIVTAPANVEVTDGDFVTLSCNATGEPVPVIHWYGRHGLITSHPSQVLRSKSRKSHLFRPGDLDPEPVYLIMSQAGSSSLSIQAVTREHAGKYTCEAVNKHGSTQSEAFLTVVPFETNTKAEPVTPSEASQNDERDPRDGSESGLLNLFPVKVHSGGVELPAEKNASVPDAPNILSPPQTHMPDTYTLVWRTGRDGGMPINAYFVKYRKLDDGSGAVGSWHTVRVPGSESELHLTELEPSSLYEVLMVARSAVGEGQPAMLTFRTSKEKMASSKNTQASFPPVGIPKRPVTSEASNSNFGVVLTDSSRHSGVPEAPDRPTISMASETSVYVTWIPRANGGSPITAFKVEYKRMKSSDWLVAAEDIPPSKLSVEVRSLEPGSIYKFRVIVINHYGESFRSSASRPYQVAGFPNRFSNRPITGPHIAYTEAVSDTQIMLKWTYIPSSNNNTPIQGFYIYYRPTDSDNDSDYKRDVVEGSKQWHTIGHLQPETSYDIKMQCFNEGGESEFSNVMICETKVKRVPGASEYPMKELSTPPSSSGNGGNVGPATSPARSSDMLYLIVGCVLGVMVLILLVFIALCLWKSRQQSAIQKYDPPGYLYQGSEINGQMVEYTTLSGTARINGSVHGGFLSKGSLSNGCSHLHHKGPNGVNGILNGTINGGLYSAHTSSLTRTCVEFEHPHHLVNGGAVYTAVPQMDPLECINCRNCRNNNRCFTKTNSPLPVVPVVASYPQDGLEMKPLGVMKFPVCPVSTVPDGGQIPEECLKDSVAPAPTQRTCRQDNTSDINSDSTEDTAEFNRGDSSGHSEAEDKVFSWSPLILSPVLEDCSEKTAWSPPGPPLDGLSVVLQQAQET
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Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells (By similarity).
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O35160
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PITX3_MOUSE
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Pituitary homeobox 3 (Homeobox protein PITX3) (Paired-like homeodomain transcription factor 3)
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MEFGLLGEAEARSPALSLSDAGTPHPPLPEHGCKGQEHSDSEKASASLPGGSPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERSQQAELCKGGFAAPLGGLVPPYEEVYPGYSYGNWPPKALAPPLAAKTFPFAFNSVNVGPLASQPVFSPPSSIAASMVPSAAAAPGTVPGPGALQGLGGAPPGLAPAAVSSGAVSCPYASAAAAAAAAASSPYVYRDPCNSSLASLRLKAKQHASFSYPAVPGPPPAANLSPCQYAVERPV
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Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle.
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O35161
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CELR1_MOUSE
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Cadherin EGF LAG seven-pass G-type receptor 1
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MAPSSPRVLPALVLLAAAALPALELGAAAWELRVPGGARAFALGPGWSYRLDTTRTPRELLDVSREGPAAGRRLGLGAGTLGCARLAGRLLPLQVRLVARGAPTAPSLVLRARAYGARCGVRLLRRSARGAELRSPAVRSVPGLGDALCFPAAGGGAASLTSVLEAITNFPACSCPPVAGTGCRRGPICLRPGGSAELRLVCALGRAAGAVWVELVIEATSGTPSESPSVSPSLLNLSQPRAGVVRRSRRGTGSSTSPQFPLPSYQVSVPENEPAGTAVIELRAHDPDEGDAGRLSYQMEALFDERSNGYFLIDAATGAVTTARSLDRETKDTHVLKVSAVDHGSPRRSAATYLTVTVSDTNDHSPVFEQSEYRERIRENLEVGYEVLTIRATDGDAPSNANMRYRLLEGAGGVFEIDARSGVVRTRAVVDREEAAEYQLLVEANDQGRNPGPLSASATVHIVVEDENDNYPQFSEKRYVVQVPEDVAVNTAVLRVQATDRDQGQNAAIHYSIVSGNLKGQFYLHSLSGSLDVINPLDFEAIREYTLRIKAQDGGRPPLINSSGLVSVQVLDVNDNAPIFVSSPFQAAVLENVPLGHSVLHIQAVDADAGENARLQYRLVDTASTIVGGSSVDSENPASAPDFPFQIHNSSGWITVCAELDREEVEHYSFGVEAVDHGSPAMSSSASVSITVLDVNDNDPMFTQPVYELRLNEDAAVGSSVLTLRARDRDANSVITYQLTGGNTRNRFALSSQSGGGLITLALPLDYKQERQYVLAVTASDGTRSHTAQVFINVTDANTHRPVFQSSHYTVSVSEDRPVGTSIATISATDEDTGENARITYVLEDPVPQFRIDPDTGTIYTMTELDYEDQAAYTLAITAQDNGIPQKSDTTSLEILILDANDNAPRFLRDFYQGSVFEDAPPSTSVLQVSATDRDSGPNGRLLYTFQGGDDGDGDFYIEPTSGVIRTQRRLDRENVAVYNLWALAVDRGSPNPLSASVGIQVSVLDINDNPPVFEKDELELFVEENSPVGSVVARIRANDPDEGPNAQIMYQIVEGNVPEVFQLDLLSGDLRALVELDFEVRRDYMLVVQATSAPLVSRATVHIRLLDQNDNPPELPDFQILFNNYVTNKSNSFPSGVIGRIPAHDPDLSDSLNYTFLQGNELSLLLLDPATGELQLSRDLDNNRPLEALMEVSVSDGIHSVTALCTLRVTIITDDMLTNSITVRLENMSQEKFLSPLLSLFVEGVATVLSTTKDDIFVFNIQNDTDVSSNILNVTFSALLPGGTRGRFFPSEDLQEQIYLNRTLLTTISAQRVLPFDDNICLREPCENYMKCVSVLRFDSSAPFISSTTVLFRPIHPITGLRCRCPPGFTGDYCETEIDLCYSNPCGANGRCRSREGGYTCECFEDFTGEHCQVNVRSGRCASGVCKNGGTCVNLLIGGFHCVCPPGEYEHPYCEVSTRSFPPQSFVTFRGLRQRFHFTVSLAFATQDRNALLLYNGRFNEKHDFIALEIVEEQLQLTFSAGETTTTVTPQVPGGVSDGRWHSVLVQYYNKPNIGHLGLPHGPSGEKVAVVTVDDCDAAVAVHFGSYVGNYSCAAQGTQSGSKKSLDLTGPLLLGGVPNLPEDFPVHSRQFVGCMRNLSIDGRIVDMAAFIANNGTRAGCASQRNFCDGTSCQNGGTCVNRWNTYLCECPLRFGGKNCEQAMPHPQRFTGESVVLWSDLDITISVPWYLGLMFRTRKEDGVLMEATAGTSSRLHLQILNSYIRFEVSYGPSDVASMQLSKSRITDGGWHHLLIELRSAKEGKDIKYLAVMTLDYGMDQSTVQIGNQLPGLKMRTIVIGGVTEDKVSVRHGFRGCMQGVRMGETSTNIATLNMNDALKVRVKDGCDVEDPCASSPCPPHSHCRDTWDSYSCICDRGYFGKKCVDACLLNPCKHVAACVRSPNTPRGYSCECGPGHYGQYCENKVDLPCPKGWWGNPVCGPCHCAVSQGFDPDCNKTNGQCQCKENYYKPPAQDACLPCDCFPHGSHSRACDMDTGQCACKPGVIGRQCNRCDNPFAEVTSLGCEVIYNGCPRAFEAGIWWPQTKFGQPAAVPCPKGSVGNAVRHCSGEKGWLPPELFNCTSGSFVDLKALNEKLNRNETRMDGNRSLRLAKALRNATQGNSTLFGNDVRTAYQLLARILQHESRQQGFDLAATREANFHEDVVHTGSALLAPATEASWEQIQRSEAGAAQLLRHFEAYFSNVARNVKRTYLRPFVIVTANMILAVDIFDKLNFTGAQVPRFEDIQEELPRELESSVSFPADTFKPPEKKEGPVVRLTNRRTTPLTAQPEPRAERETSSSRRRRHPDEPGQFAVALVVIYRTLGQLLPEHYDPDHRSLRLPNRPVINTPVVSAMVYSEGTPLPSSLQRPILVEFSLLETEERSKPVCVFWNHSLDTGGTGGWSAKGCELLSRNRTHVTCQCSHSASCAVLMDISRREHGEVLPLKIITYAALSLSLVALLVAFVLLSLVRTLRSNLHSIHKNLITALFFSQLIFMVGINQTENPFLCTVVAILLHYVSMGTFAWTLVENLHVYRMLTEVRNIDTGPMRFYHVVGWGIPAIVTGLAVGLDPQGYGNPDFCWLSLQDTLIWSFAGPVGTVIIINTVIFVLSAKVSCQRKHHYYERKGVVSMLRTAFLLLLLVTATWLLGLLAVNSDTLSFHYLFAAFSCLQGIFVLLFHCVAHREVRKHLRAVLAGKKLQLDDSATTRATLLTRSLNCNNTYSEGPDMLRTALGESTASLDSTTRDEGVQKLSVSSGPARGNHGEPDASFIPRNSKKAHGPDSDSDSELSLDEHSSSYASSHTSDSEDDGGEAEDKWNPAGGPAHSTPKADALANHVPAGWPDESLAGSDSEELDTEPHLKVETKVSVELHRQAQGNHCGDRPSDPESGVLAKPVAVLSSQPQEQRKGILKNKVTYPPPLPEQPLKSRLREKLADCEQSPTSSRTSSLGSGDGVHATDCVITIKTPRREPGREHLNGVAMNVRTGSAQANGSDSEKP
|
Receptor that may have an important role in cell/cell signaling during nervous system formation.
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O35165
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GOSR2_RAT
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Golgi SNAP receptor complex member 2 (27 kDa Golgi SNARE protein) (Membrin)
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MEPLYQQTHKQVHEIQSHMGRLETADKQSVHLVENEIQASIDQIFSHLERLEILSSKEPPNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQAKEQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLQNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT
|
Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
|
O35166
|
GOSR2_MOUSE
|
Golgi SNAP receptor complex member 2 (27 kDa Golgi SNARE protein) (Membrin)
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MEPLYQQTNKQVQEIQSHMGRLERADKQSVHLVENEIQASIEQIFSHLERLEILSSKEPLNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQVREQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLHNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT
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Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
|
O35167
|
COLQ_RAT
|
Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
|
MAVLNPMTLGIYLQLFFCSIVSQPTFINSVLPISAALPGLDQKKRGNHKACCLLMPPPPPLFPPPFFRGSRSPLLSPDMKNLLELEASPSPCMQGSLGSPGPPGPQGPPGLPGKAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQLVMGLKGERGFPGPPGRCLCGPPANVNNPSYGDPMYGRGSPRVPAIFVVNNQEELEKLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVGLHHKAAWHLCGDGVLQPGEECDDGNPDVSDGCIDCHRAYCGDGYRHRGVEDCDGSDFGYLKCETYLPGSYGELRCTQYCSIDSTPCRYFT
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Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
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O35173
|
KCNS1_MOUSE
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Potassium voltage-gated channel subfamily S member 1 (Delayed-rectifier K(+) channel alpha subunit 1) (Voltage-gated potassium channel subunit Kv9.1)
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MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEENEGFHTIPACWWWGTVSMTTVGYGDVVPETVGGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRDTSQEGRSTDLETQAPREPAKSHSY
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Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2 modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
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O35174
|
KCNS2_MOUSE
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Potassium voltage-gated channel subfamily S member 2 (Delayed-rectifier K(+) channel alpha subunit 2) (Voltage-gated potassium channel subunit Kv9.2)
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MTRQSLWDVSDTDVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSVLSILVVLGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGATLKYSYKEVGLLLLYLSVGISIFSVVAYTIEKEENEGLATIPACWWWATVSMTTVGYGDVVPGTTAGKLTASACILAGILVVVLPITLIFNKFSHFYRRQKQLESAMRSCDFGDGMKEVPSVNLRDYYAHKVKSLMASLTNMSRSSPSELSLDDSLH
|
Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2 modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
|
O35177
|
CASL_MOUSE
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Enhancer of filamentation 1 (mEF1) (CRK-associated substrate-related protein) (CAS-L) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (p105)
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MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPVQETPGHEQPTPGPMHQTFGQQKLYQVPNSQAASRDTIYQVPPSYQNQGIYQVPTGHGTPEQDVYQVPPSVQRNIGGTNGPLLSKKVITPVRTGHGYVYEYPSRYQKDVYDVPPSHSTQGVYDIPPSSVKGPVFSVPVGEIKPQGVYDIPPTQGVYAIPPSACRDEAGLREKEYDFPPPMKQDGKPDTRPEGVYDIPPTSTKTAGKDLHIKFPCDAPGGVEPMARRHQSFSLHHAPSQLGQSGDTQSDAYDVPRGVQFLEVPTETSEKANPEERDGVYDVPLHNPADAKGSRDVVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPSQDKRLRLDPDTAIEKLYRLQQTLEMGVCSLMSLVTTDWRCYGYMERHINEIRTAVDKVELFLREYLHFAKGALANASCLPELVLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTISTYAETLFRADPANSHLKNGPNSIMNSSEYTHPGSQMQPLHPGDYKAQVHSKPLPPSLSKDQPPDCGSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQSKAQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNNSVGAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDIRNKVRNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF
|
Scaffolding protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion (By similarity). As a focal adhesion protein, plays a role in embryonic fibroblast migration. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRKl and SHPTP2 to the tyrosine phosphorylated form (By similarity). Promotes adhesion and migration of lymphocytes as a result required for the correct migration of lymphocytes to the spleen and other secondary lymphoid organs. Plays a role in the organization of T-cell F-actin cortical cytoskeleton and the centralization of T-cell receptor microclusters at the immunological synapse. Negatively regulates cilia outgrowth in polarized cysts (By similarity). Modulates cilia disassembly via activation of AURKA-mediated phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Positively regulates RANKL-induced osteoclastogenesis. Required for the maintenance of hippocampal dendritic spines in the dentate gyrus and CA1 regions, thereby involved in spatial learning and memory.
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O35179
|
SH3G2_RAT
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Endophilin-A1 (Endophilin-1) (SH3 domain protein 2A) (SH3 domain-containing GRB2-like protein 2) (SH3p4)
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MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH
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Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity).
|
O35180
|
SH3G3_RAT
|
Endophilin-A3 (Endophilin-3) (SH3 domain protein 2C) (SH3 domain-containing GRB2-like protein 3) (SH3p13)
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MSVAGLKKQFHKASQLFSEKISGAEGTKLDEEFLDMEKKIDITSKAVAEILSKATEYLQPNPAYRAKLGMLNTMSKLRGQVKATGYPQTEGLLGDCMLKYGRELGEDSAFGNSLVEVGEALKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLRKLEGRRLDYDYKKKRVGKIPEEEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFVEAALDYHRQSTEILQELQNKLELRIALASQVPRRDYMPKPVNTSSTNANGVEPSSSSKLTGTDIPSDQPCCRGLYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLRGESGFFPINYVEVIVPLPR
|
Implicated in endocytosis. May recruit other proteins to membranes with high curvature.
|
O35181
|
NRG3_MOUSE
|
Pro-neuregulin-3, membrane-bound isoform (Pro-NRG3) [Cleaved into: Neuregulin-3 (NRG-3)]
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MSEGAAGASPPGAASAAAASAEEGTAAAAAAAAAGGGPDGGGEGAAEPPRELRCSDCIVWNRQQTWLCVVPLFIGFIGLGLSLMLLKWIVVGSVKEYVPTDLVDSKGMGQDPFFLSKPSSFPKAMETTTTTTSTTSPATPSAGGAASSRTPNRISTRLTTITRAPTRFPGHRVPIRASPRSTTARNTAAPPTVLSTTAPFFSSSTPGSRPPMPGAPSTQAMPSWPTAAYATSSYLHDSTPSWTLSPFQDAAAASSSSPSSTSSTTTTPETSTSPKFHTTTYSTERSEHFKPCRDKDLAYCLNDGECFVIETLTGSHKHCRCKEGYQGVRCDQFLPKTDSILSDPTDHLGIEFMESEDVYQRQVLSISCIIFGIVIVGMFCAAFYFKSKKQAKQIQEHLKESQNGKNYSLKASSTKSESLMKSHVHLQNYSKADRHPVTALEKIMESSFSAPQSFPEVTSPDRGSQPIKHHSPGQRSGMLHRNTFRRAPPSPRSRLGGIVGPAYQQLEESRIPDQDTIPCQGIEVRKTISHLPIQLWCVERPLDLKYVSNGLRTQQNASINMQLPSRETNPYFNSLDQKDLVGYLSPRANSVPIIPSMGLEETCMQMPGISDVKSIKWCKNSYSADIVNASMPVSDCLLEEQQEVKILLETVQEQIRILTDARRSEDFELASMETEDSASENTAFLPLSPTAKSEREAQFVLRNEIQRDSVLTK
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Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors.
|
O35182
|
SMAD6_MOUSE
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Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (Mad homolog 7) (SMAD family member 6) (SMAD 6) (Smad6)
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MFRSKRSGLVRRLWRSRVVPDREEGSGGGGGVDEDGSLGSRAEPAPRAREGGGCSRSEVRSVAPRRPRDAVGPRGAAIAGRRRRTGGLPRPVSESGAGAGGSPLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFTAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLLQHADAAHGPYDPHSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR
|
Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (By similarity). Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes. Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions (By similarity).
|
O35185
|
BHE40_MOUSE
|
Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (E47 interaction protein 1) (EIP1) (Stimulated by retinoic acid gene 13 protein)
|
MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD
|
Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2 (By similarity). Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes (By similarity). Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May function as a transcriptional factor for neuronal differentiation. Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (By similarity). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system.
|
O35186
|
CATK_RAT
|
Cathepsin K (EC 3.4.22.38)
|
MWVFKFLLLPVVSFALSPEETLDTQWELWKKTHGKQYNSKVDEISRRLIWEKNLKKISVHNLEASLGAHTYELAMNHLGDMTSEEVVQKMTGLRVPPSRSFSNDTLYTPEWEGRVPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVSENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPVSVSIDASLTSFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGNKYWIIKNSWGESWGNKGYVLLARNKNNACGITNLASFPKM
|
Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen.
|
O35188
|
X3CL1_MOUSE
|
Fractalkine (FK) (ABCD-3) (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]
|
MAPSPLAWLLRLAAFFHLCTLLPGQHLGMTKCEIMCDKMTSRIPVALLIRYQLNQESCGKRAIVLETTQHRRFCADPKEKWVQDAMKHLDHQAAALTKNGGKFEKRVDNVTPGITLATRGLSPSALTKPESATLEDLALELTTISQEARGTMGTSQEPPAAVTGSSLSTSEAQDAGLTAKPQSIGSFEAADISTTVWPSPAVYQSGSSSWAEEKATESPSTTAPSPQVSTTSPSTPEENVGSEGQPPWVQGQDLSPEKSLGSEEINPVHTDNFQERGPGNTVHPSVAPISSEETPSPELVASGSQAPKIEEPIHATADPQKLSVLITPVPDTQAATRRQAVGLLAFLGLLFCLGVAMFAYQSLQGCPRKMAGEMVEGLRYVPRSCGSNSYVLVPV
|
Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the endothelium. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (By similarity). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (By similarity). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (By similarity). [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils.
|
O35206
|
COFA1_MOUSE
|
Collagen alpha-1(XV) chain [Cleaved into: Restin (Endostatin-XV)]
|
MTHRRTAQGRRPRWLLSIISALLSAVLQTRAATGSASQVHLDLTVLIGVPLPSSVSFTTGYGGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAFQKVIYLGLRLSSVEDGRQRVILYYTEPGSHVSREAAVFSVPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPLTFEPSAGIFVGNAGAMGLERFTGSIQQLTIYSDPRTPEELCEAQESSASGEASGFQEMDEVAEIMEAVTYTQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEQGSGEILNDTLEVHAMDGDPGTDDGSGDGALLNVTDGQGLSATATGEASVPVTTVLEAENGSMPTGSPTLAMFTQSIREVDTPDPENLTTTASGDGEVPTSTDGDTEADSSPTGGPTLKPREEATLGSHGEEWLTPAVSKMPLKAFEEEEASGTAIDSLDVIFTPTVVLEQVSRRPTDIQATFTPTVVLEETSGAPTDTQDALTPTVAPEQMFTAEPTDGGDLVASTEEAEEEGSGSMPPSGPPLPTPTVTPKRQVTLVGVEAEGSGPVGGLDEGSGSGDIVGNEDLLRGPPGPPGPPGSPGIPGKPGTDVFMGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGEVGTPGVMGPPGPPGPPGPPGPGCTTELGFEIEGSGDVRLLSKPTISGPTSPSGPKGEKGEQGAKGERGADGTSTMGPPGPRGPPGHVEVLSSSLINITNGSMNFSDIPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGAILTGDVPLEMMKGRKGEPGIHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGVTLPGPPGLPGPPGPPGPPGAVVNIKGAVFPIPARPHCKTPVGTAHPGDPELVTFHGVKGEKGSWGLPGSKGEKGDQGAQGPPGPPVDPAYLRHFLNSLKGENEDASFRGESSNNLFVSGPPGLPGYPGLVGQKGEAVVGPQGPPGIPGLPGPPGFGRPGVPGPPGPPGPPGPPAILGAAVALPGPPGPPGQPGLPGSRNLVTALSDMGDMLQKAHLVIEGTFIYLRDSGEFFIRVRDGWKKLQLGELIPIPADSPPPPALSSNPYQPQPPLNPILSANYERPVLHLVALNTPVAGDIRADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSIFSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRLIVLCIENSFMTDTRK
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Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. Restin potently inhibits angiogenesis.
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O35207
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CDKA1_MOUSE
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Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1) (Deleted in oral cancer 1) (DOC-1) (Putative oral cancer suppressor)
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MSYKPNLTAHMPAAALNAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARSLVRECLAETERNARS
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Inhibitor of cyclin-dependent kinase CDK2. Also acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity).
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O35216
|
CENPA_MOUSE
|
Histone H3-like centromeric protein A (Centromere protein A) (CENP-A)
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MGPRRKPQTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLTRRIRGFEGGLP
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Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis.
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O35217
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MINP1_RAT
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Multiple inositol polyphosphate phosphatase 1 (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase) (Ins(1,3,4,5)P(4) 3-phosphatase)
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MLRGARSHLSASVALAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDVNPWLLGDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLRQLQGLLQTRESVDGGSRVAAALDQWPLWYDDWMDGQLVEKGRQDMRQLALRLAALFPDLFCRENYGRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECDPPRVNDKLMRFFDHCEKFLTEVERNATALYHVEAFKTGPEMQTVLKKVAATLQVPVNNLNADLIQVAFFTCSFDLAIQGVHSPWCDVFDVDDAKVLEYLNDLKQYWKRSYGYAINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSSVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVHREFRSGHIVPYASNLIFVLYHCEDAQTPQEKFQIQMLLNEKVLPLAHSQKTVALYEDLKNHYQDILQSCQTSKECNLPKVNITSDEL
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Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). Through the regulation of intracellular inositol polyphosphates, may control intracellular cation homeostasis, including that of calcium and iron, hence affecting free cation availability required for neural cell signaling (By similarity).
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O35219
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KCNH2_MOUSE
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Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (MERG) (Voltage-gated potassium channel subunit Kv11.1)
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MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESSVRTGSMHSAGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPGSASPVASIRGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPPPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEDGSQAPDCGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSHIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSAELESGFNRQRKRKLSFRRRTDKDTEQPGEVSALGQGPARVGPGPSCRGQPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGDPPGGEPLTEDGEKSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPAPSLLNIPLSSPGRRSRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSASPLLPVGPVPTLTLDSLSQVSQFVAFEELPAGAPELPQDGPTRRLSLPGQLGALTSQPLHRHGSDPGS
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Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity).
|
O35226
|
PSMD4_MOUSE
|
26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
|
MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATPGTEDSDDALLKMTINQQEFGRPGLPDLSSMTEEEQIAYAMQMSLQGTEFSQESADMDASSAMDTSDPVKEEDDYDVMQDPEFLQSVLENLPGVDPNNAAIRSVMGALASQATKDGKNDKKEEEKK
|
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains.
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O35227
|
ADAM7_MOUSE
|
Disintegrin and metalloproteinase domain-containing protein 7 (ADAM 7)
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MLTTGIFWMTVLISHIQERGIVGVEGQELVHPKKLPLLHKRDLERIHDSDIPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGEHLVYKYNVKAPYATNHSCVGLNFTKKSALIDVENIEEHNAEDHHKEKFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGFPCTCPLGKCVMGDGSIPAIKFSKCSQTQYQQFLQDQKPACILNNPFPEEFNDYPFCGNKKVDEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKDEFQANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCYRMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGRPSSRLGEDKAYNLKNVKQNVTIKCRTMFLHHNSRDMGLVNSGTKCGDGMVCSNGECIEMEKAYNSTICSSPCDENDVDDNEPECQCEEGSIITEWGEALNLTSVSIMVIVLVMVIIGVGLVILLIRYQKCIKMKQVQSSPREIRGVENKGYFPEEHQTRSEPILTDIHPLHTTAESLERVPSSFSSPHYITLKSVSKDSRGIADPKQTDNVNLNLDTQSGCERLG
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Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development. Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitance. Plays a role in normal expression levels of HSPA5, ITM2B and ADAM2 in sperm both prior to and post-capacitation. This is a non catalytic metalloprotease-like protein (Probable).
|
O35231
|
KIFC3_MOUSE
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Kinesin-like protein KIFC3
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MVPSRRTWNLGATPSLRGLWRVGRVQEPKPGMARPAPASPAARPFPHTGQGRLRTGRGKDILPSGEEDSTSRTAARPSLAQCRALSVDWPGPRSPHRLYLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDPDDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSVELGPGSRRTELGSWSSQEHLEWEPACQTPQPTARAHSAPGSGTSSRPGSIRRKLQPSA
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Minus-end microtubule-dependent motor protein. Involved in apically targeted transport. Required for zonula adherens maintenance.
|
O35235
|
TNF11_MOUSE
|
Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]
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MRRASRDYGKYLRSSEEMGSGPGVPHEGPLHPAPSAPAPAPPPAASRSMFLALLGLGLGQVVCSIALFLYFRAQMDPNRISEDSTHCFYRILRLHENADLQDSTLESEDTLPDSCRRMKQAFQGAVQKELQHIVGPQRFSGAPAMMEGSWLDVAQRGKPEAQPFAHLTINAASIPSGSHKVTLSSWYHDRGWAKISNMTLSNGKLRVNQDGFYYLYANICFRHHETSGSVPTDYLQLMVYVVKTSIKIPSSHNLMKGGSTKNWSGNSEFHFYSINVGGFFKLRAGEEISIQVSNPSLLDPDQDATYFGAFKVQDID
|
Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (By similarity). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation.
|
O35240
|
ASIC3_RAT
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Acid-sensing ion channel 3 (ASIC3) (Amiloride-sensitive cation channel 3) (Dorsal root ASIC) (DRASIC)
|
MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDPLGSPRPRPSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSESYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSAQKRSGNTLLQEELNGHRTHVPHLSLGPRPPTTPCAVTKTLSASHRTCYLVTRL
|
Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.
|
O35244
|
PRDX6_RAT
|
Peroxiredoxin-6 (EC 1.11.1.27) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Glutathione-dependent peroxiredoxin) (Lysophosphatidylcholine acyltransferase 5) (LPC acyltransferase 5) (LPCAT-5) (Lyso-PC acyltransferase 5) (EC 2.3.1.23) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein)
|
MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP
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Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).
|
O35245
|
PKD2_MOUSE
|
Polycystin-2 (Polycystic kidney disease 2 protein homolog) (Transient receptor potential cation channel subfamily P member 2)
|
MVNSRRVQPQPPGDAGRSPAPRASGPGRLVAGGAGLAVPGGLGEQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRSASSSAVSSVGARGRGLGSYRGAAHLSGRRRRLEDQGAQCPSPAGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLKSVLRELVTYLFFLVVLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQTSNHTQADNRSFIFYENLLLGVPRLRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWMYTSEKELNGSSHWGIIASYSGAGYYLDLSRTREETAAQLAGLRRNFWLDRGTRAAFIDFSVYNANINLFCVVRLLAEFPATGGVVPSWQFQPVKLIRYVTAFDFFLAACEIIFCFFIIYYVVEEILEIRIHRLSYFRSFWNCLDVVIVVLSVVAMVINIYRMSNAEGLLQFLEDQNSFPNFEHVAYWQIQFNNISAVMVFLVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFTIMFSIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPLYFTTFVFFMFFILLNMFLAIINDSYSEVKSDLAQQKAEMELSDLIRKGCQKALVKLKLKRNTVDAISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEREHQQMRDDLEKEREDLDLEHSSLPRPMSSRSFPRSLDDSEEEDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDARLGRDSEIHREQMERLVREELERWESDDAASQTGHGVSTQVGLGGQPHPRNPRPPSSQSAEGLEGGGGNGSANVHA
|
Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel. Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Together with TRPV4, forms mechano- and thermosensitive channels in cilium. PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality.
|
O35250
|
EXOC7_MOUSE
|
Exocyst complex component 7 (Exocyst complex component Exo70)
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MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTRNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKESLESEFRSLMTRHSKVVSPVLLLDLISADDELEVQEDVVLEHLPESVLRDVVRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFRKSSSSSGVPYSPAIPNKRKDTPTKKPIKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGRDDMLDVETDAYIHCVSAFVKLAQSEYRLLMEIIPEHHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIRHDFSTVLTVFPILRHLKQTKPEFDQVLQGTAASTKNKLPGLITSMETIGAKALEDFADNIKNDPDKEYNMPKDGTVHELTSNAILFLQQLLDFQETAGAMLASQVLGDTYNIPLDPRETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYILKSLEKSELIQLVAVTQKTAERSYREHIEQQIQTYQRSWLKVTDYIAEKNLPVFQPGVKLRDKERQMIKERFKGFNDGLEELCKIQKVWAIPDTEQRDKIRQAQKDIVKETYGAFLHRYGSVPFTKNPEKYIKYRVEQVGDMIDRLFDTSA
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Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion. It is required for neuron survival and plays an essential role in cortical development (By similarity).
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O35251
|
VEGFD_RAT
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Vascular endothelial growth factor D (VEGF-D) (c-Fos-induced growth factor) (FIGF)
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MYGEWAAVNILMMSYVYLVQGFSIEHRAVKDVSLERSSRSVLERSEQQIRAASTLEELLQVAHSEDWKLWRCRLKLKSLANVDSRSTSHRSTRFAATFYDTETLKVIDEEWQRTQCSPRETCVEVASELGKTTNTFFKPPCVNVFRCGGCCNEESVMCMNTSTSYISKQLFEISVPLTSVPELVPVKIANHTGCKCLPTGPRHPYSIIRRSIQIPEEDQCPHSKKLCPVDMLWDNTKCKCVLQDENPLPGTEDHSYLQEPALCGPHMMFDEDRCECVCKAPCPGDLIQHPENCSCFECKESLESCCQKHKMFHPDTCRSMVFSLSP
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Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-3 (Flt4) receptor (By similarity).
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O35253
|
SMAD7_MOUSE
|
Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
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MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGELRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPTSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTAGCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
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Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
|
O35254
|
GORS1_RAT
|
Golgi reassembly-stacking protein 1 (Golgi peripheral membrane protein p65) (Golgi reassembly-stacking protein of 65 kDa) (GRASP65)
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MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSNNTSVCPSLSSSSLLTPTAVSALGPEDIGSSSSSHERGGEATWSGSEFEISFPDSPGSQAQVDHLPRLTLPDGLTSAASPEEGLSAELLEAQTEEPAHTASLDCMAQTEGPAGQVQAAPDPEPGLCEGPW
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Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis. Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis. Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
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O35260
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NACC1_RAT
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Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B)
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MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNSSRSAVVELPAAVQPQSFQQILTFCYTGRLSMNMGDQFLLIYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHPEEAPSSEPQSPVAQILGWPACSTPLPLVSRVKTEQELDSVQCTPMAKRLWDSSQKEAGGSGGNNGSRKMAKFSTPDLAPNRMPQPVSVATATAAVAVVAVGGCVSGPSMSERTSPGTSSAYTSDSPSSYHNEEDEEEDAGEEGTDEQYRQICNMYTMYSMLNVGQTVEKVEALPEQVVLESHSRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWLPKTKPLHLVEGDNYSSFISDTGKIEPDMMSMEHSFETASHDGEAGPSAEVLQ
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Functions as a transcriptional repressor. Isoform 1 is a stronger transcriptional repressor than isoform 2. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines.
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O35261
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E2F3_MOUSE
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Transcription factor E2F3 (E2F-3)
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MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAPGTYIQILTTNPSTTSCATSLQSGALTAGPLLPSVPGTEPAASSLYTTPQGPSSRVGLLQQPPAPGRGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHRPMKTNNQDHNGNIPKPTSKDLASNNSGHSDCSVSTANLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS
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Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters.
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O35263
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PA1B3_RAT
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Platelet-activating factor acetylhydrolase IB subunit alpha1 (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) (Platelet-activating factor acetylhydrolase alpha 1 subunit) (PAF-AH alpha 1)
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MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAP
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Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain (By similarity).
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O35264
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PA1B2_RAT
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Platelet-activating factor acetylhydrolase IB subunit alpha2 (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa subunit) (PAF-AH subunit beta) (PAFAH subunit beta) (Platelet-activating factor acetylhydrolase alpha 2 subunit) (PAF-AH alpha 2)
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MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
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Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity).
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O35274
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NEB2_RAT
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Neurabin-2 (Neurabin-II) (Neural tissue-specific F-actin-binding protein II) (PP1bp134) (Protein phosphatase 1 regulatory subunit 9B) (Spinophilin) (p130)
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MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTTGPPGEAGGASGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERASLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDAATEKDRGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTTATTASPAPEEPKAEAVPEEEASSSVATLERGVDNGRAPDMAPEEVDESKKEDFSEADLVDVSAYSGLGEDSGGSALEEDDEEDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVEMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST
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Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:15743906, ECO:0000269|PubMed:15793568}.
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O35276
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NRP2_RAT
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Neuropilin-2 (Vascular endothelial cell growth factor 165 receptor 2)
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MDMFPLTWIFLALYFSGHKVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWVVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPPENFQCNAPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTPNVDSNKEYLQVDLRFLTMLTAIATQGAISRETQKGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATELVLNKLHTPLLTRFIRIRPQTWHLGIALRLELFGCRVTDAPCSNMLGMLSGLIADTQISASSTREYLWSPSAARLVSSRSGWFPRNPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAMEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRRFEPVPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPMDEDATECGENCSFEDDKDLQLPSGFNCNFDFPEETCGWMYDRAKWLQSTWISSANPNDRTFPDDKNFLKLQSDGGREGQFGRLISPPVHLPRSPVCMEFQYQAMGGHGVALQVVREARQESKLLWVIREDQGSEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEISIDDIRISTDVPLENCMEPISAFAVDIPEIHGGEGYEDEIDDDYEGDWNNSSSTSGAGSPSSGKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA
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High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
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O35280
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CHK1_MOUSE
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Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
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MAVPFVEDWDLVQTLGEGAYGEVQLAVNRITEEAVAVKIVDMKRAIDCPENIKKEICINKMLSHENVVKFYGHRREGHIQYLFLEYCSGGELFDRIEPDIGMPEQDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRHNNRERLLNKMCGTLPYVAPELLKRKEFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVETPSARITIPDIKKDRWYNKPLNRGAKRPRATSGGMSESSSGFSKHIHSNLDFSPVNNGSSEETVKFSSSQPEPRTGLSLWDTGPSNVDKLVQGISFSQPTCPEHMLVNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETFEKLGYQWKKSCMNQVTVSTTDRRNNKLIFKINLVEMDEKILVDFRLSKGDGLEFKRHFLKIKGKLSDVVSSQKVWFPVT
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Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA (By similarity). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (By similarity). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (By similarity).
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O35284
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BATF_MOUSE
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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.
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O35286
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DHX15_MOUSE
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ATP-dependent RNA helicase DHX15 (EC 3.6.4.13) (DEAH box protein 15)
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MSKRHRLDLGEDYPSGKKRAGTDGKDRERDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHTGHTGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
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RNA helicase involved in mRNA processing and antiviral innate immunity. Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (By similarity). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (By similarity). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome. Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3) (By similarity). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses. The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu. Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells.
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O35291
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RNAS2_MOUSE
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Non-secretory ribonuclease (EC 4.6.1.18) (Eosinophil cationic-type ribonuclease 4) (MR-4) (Ribonuclease 2) (RNase 2)
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MGPKLLESRLCLLLLLGLVLMLASCQAQILSQKFYTQHIYNSTYPRCDAVMRVVNRYRPRCKDINTFLHTSFADVVAVCGHPNITCNNLTRKNCHASSFQVFITFCNLTMPTRICTQCRYQTTGSVKYYRVACENRTPQDTPMYPVVPVHLDGTF
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This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.
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O35293
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CP2F2_RAT
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Cytochrome P450 2F2 (EC 1.14.14.-) (CYPIIF2) (Cytochrome P450-NAH-2) (Naphthalene dehydrogenase) (Naphthalene hydroxylase)
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MDGVSTAILLLLLAVISLSLTFTSWGKGQLPPGPKPLPILGNLLQLRSQDLLTSLTKLSKDYGSVFTVYLGPRRVIVLSGYQTVKEALVDKGEEFSGRGSYPIFFNFTKGNGIAFSDGERWKILRRFSVQILRNFGMGKRSIEERILEEGSFLLDVLRKTEGKPFDPVFILSRSVSNIICSVIFGSRFDYDDERLLTIIHFINDNFQIMSSPWGEMYNIFPSLLDWVPGPHRRVFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMVQEKQDPLSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDCVVGRSRMPTLEDRASMPYTDAVIHEVQRFADVIPMNLPHRVIRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGEPLARMELFIYLTSILQNFTLHPLVEPEDIDLTPLSSGLGNLPRPFQLCMRIR
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Involved in the regio- and stereoselective transformation of naphthalene to trans-1R-hydroxy-2R-glutathionyl-1,2-dihydronaphthalene in the presence of glutathione and glutathione S-transferases. It specifically catalyzes the production of a very reactive and potentially toxic intermediate, the 2R,2S arene oxide, that is associated with necrosis of the unciliated bronchiolar epithelial cells or club cells in lung.
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O35295
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PURB_MOUSE
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Transcriptional activator protein Pur-beta (Purine-rich element-binding protein B) (Vascular actin single-stranded DNA-binding factor 2 p44 component)
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MADGDSGSERGGGGGGGGGPGGFQPAPRGGGGGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGDEDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEEVDED
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Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts. {ECO:0000250, ECO:0000269|PubMed:11751932, ECO:0000269|PubMed:9334258}.
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O35298
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AOAH_MOUSE
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Acyloxyacyl hydrolase (EC 3.1.1.77) [Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit]
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MKFPWKVFKTTLLLLLLSHSLASVPSEDQPGDSYSHGQSCLGCVVLVSVIEQLAEVHNSSVQVAMERLCSYLPEKLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFCKRGAVQPQCHLYPLPQEAWESALEKARQVLRRSSTMKYPRSGRNICSLPFLTKICQKIELSIKKAVPFKDIDSDKHSVFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDIHQDSNCNGIWGIDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDSTSGIEEKSIYHRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPEMTTPEQMYANVMQTLTHLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQLNPCNGWMSSNKTLRTLTSERAEQLSNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEVASLLQANRVWEKIQLQWPHVLGKENPFNSQIEEVFGDQGGH
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Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.
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O35303
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DNM1L_RAT
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Dynamin-1-like protein (EC 3.6.5.5) (Dynamin-like protein)
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MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENDPATWKNSRHLSKGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
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Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (By similarity). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (By similarity). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis (By similarity). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (By similarity). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution (By similarity). Rhythmic control of its activity following phosphorylation at Ser-656 is essential for the circadian control of mitochondrial ATP production (By similarity).
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O35304
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VACHT_MOUSE
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Vesicular acetylcholine transporter (VAChT) (Solute carrier family 18 member 3)
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MEPTAPTGQARAAATKLSEAVGAALQEPQRQRRLVLVIVCVALLLDNMLYMVIVPIVPDYIAHMRGGSESPTLISEVWEPTLPPPTLANASAYLANTSASPTAAGSARSILRPRYPTESEDVKIGVLFASKAILQLLVNPLSGPFIDRMSYDVPLLIGLGVMFASTVMFAFAEDYATFFAARSLQGLGSAFADTSGIAMIADKYPEEPERSRALGVALAFISFGSLVAPPFGGILYEFAGKRVPFLVLAAVSLFDALLLLAVAKPFSAAARARANLPVGTPIHRLMLDPYIAVVAGALTTCNIPLAFLEPTIATWMKHTMAASEWEMGMVWLPAFVPHVLGVYLTVRLAARYPHLQWLYGALGLAVIGVSSCVVPACRSFAPLVVSLCGLCFGIALVDTALLPTLAFLVDVRHVSVYGSVYAIADISYSVAYALGPIVAGHIVHSLGFEQLSLGMGLANLLYAPVLLLLRNVGLLTRSRSERDVLLDEPPQGLYDAVRLREVQGKDGGEPCSPPGPFDGCEDDYNYYSRS
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Electrogenic antiporter that exchanges one cholinergic neurotransmitter, acetylcholine or choline, with two intravesicular protons across the membrane of synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to store neurotransmitters inside the vesicles prior to their release via exocytosis (By similarity). Determines cholinergic vesicular quantal size at presynaptic nerve terminals in developing neuro-muscular junctions with an impact on motor neuron differentiation and innervation pattern (By similarity). Part of forebrain cholinergic system, regulates hippocampal synapse transmissions that underlie spatial memory formation. Can transport serotonin.
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O35305
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TNR11_MOUSE
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Tumor necrosis factor receptor superfamily member 11A (Osteoclast differentiation factor receptor) (ODFR) (Receptor activator of NF-KB) (CD antigen CD265)
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MAPRARRRRQLPAPLLALCVLLVPLQVTLQVTPPCTQERHYEHLGRCCSRCEPGKYLSSKCTPTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVDPGNHTAPRRCACTAGYHWNSDCECCRRNTECAPGFGAQHPLQLNKDTVCTPCLLGFFSDVFSSTDKCKPWTNCTLLGKLEAHQGTTESDVVCSSSMTLRRPPKEAQAYLPSLIVLLLFISVVVVAAIIFGVYYRKGGKALTANLWNWVNDACSSLSGNKESSGDRCAGSHSATSSQQEVCEGILLMTREEKMVPEDGAGVCGPVCAAGGPWAEVRDSRTFTLVSEVETQGDLSRKIPTEDEYTDRPSQPSTGSLLLIQQGSKSIPPFQEPLEVGENDSLSQCFTGTESTVDSEGCDFTEPPSRTDSMPVSPEKHLTKEIEGDSCLPWVVSSNSTDGYTGSGNTPGEDHEPFPGSLKCGPLPQCAYSMGFPSEAAASMAEAGVRPQDRADERGASGSGSSPSDQPPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGPGSAEPESEPVGRPVQEETLAHRDSFAGTAPRFPDVCATGAGLQEQGAPRQKDGTSRPVQEQGGAQTSLHTQGSGQCAE
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Receptor for TNFSF11/RANKL/TRANCE/OPGL essential for RANKL-mediated osteoclastogenesis. Its interaction with EEIG1 promotes osteoclastogenesis via facilitating the transcription of NFATC1 and activation of PLCG2. Involved in the regulation of interactions between T-cells and dendritic cells.
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O35309
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NMI_MOUSE
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N-myc-interactor (Nmi) (N-myc and STAT interactor)
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MDADKDNIKQACDERSAEMDDMRGEQSMGLVHEIMSENKELDEEIKKLEAELQSDAREFQIKENVPEKKLKLTSVESPKDGCHFSNSSCSFQVSSQILYELQEGQALITFEKEEVAQNVISMGNHVVQMEGTPVKVSAHPVPLNTGVRFQVHVDISKMKINVTGIPDELSEEQTRDKLELSFCKSRNGGGEVESVDYDRKSRSAVITFVETGVVDKILKKKTYPLYMNQKCHSVAVSPCIERCLEKYQVFSAVSKKTVLLTGLEGIPVDEETGEDLLNIHFQRKNNGGGEVEVVKCSLDQSFAAYFKEEARETI
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Acts as a signaling pathway regulator involved in innate immune system response. In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis (By similarity). Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription (By similarity). In response to interferon IFN-alpha, associates in a complex with transcriptional regulator IFI35 to regulate immune response the complex formation prevents proteasome-mediated degradation of IFI35 (By similarity). In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries (By similarity). Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion (By similarity). Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines (By similarity).
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O35310
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HS3S1_MOUSE
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Heparan sulfate glucosamine 3-O-sulfotransferase 1 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1) (Heparan sulfate 3-O-sulfotransferase 1)
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MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH
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Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site.
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