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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O70201
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BIRC5_MOUSE
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Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor 4) (Apoptosis inhibitor survivin) (TIAP)
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MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA
|
Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). Acts as an important regulator of the localization of this complex directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function.
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O70209
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PDLI3_MOUSE
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PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein)
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MPQNVVLPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAASYQLCLKIDRAETRLWSPQVSEDGKAHPFKINLEAEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTSNIQDALHGQLRGLIPGSLQNEPTASVPPQSDVYRMLHDNRDDPAAPRQSGSFRVLQDLVNDGPDDRPAGTRSVRAPVTKVHGGAGSAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFVEGELYCETHARARTRPPEGYDTVTLYPKA
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May play a role in the organization of actin filament arrays within muscle cells.
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O70212
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5HT3A_CAVPO
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5-hydroxytryptamine receptor 3A (5-HT3-A) (5-HT3A) (5-hydroxytryptamine receptor 3) (5-HT-3) (5-HT3R) (Serotonin receptor 3A) (Serotonin-gated ion channel receptor)
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MVLWLQLALLALLLPTSLAQGEVRGKGTAQAHNSTRPALQRLSDHLLADYRKSVRPVRDWRKPTTVSIDAIVYAILSVDEKNQVLTTYIWYRQFWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYVRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDKSVFMNQGEWELLGVLTEFLEFSDRESRGSFAEMKFYVVIRRRPLFYAVTLLLPSIFLMIVDIVGFYLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLISVYFVVCMALLVISLAETILIVRLVHKQDLQQPVPLWLRHLVLERIAGLLCLGEQLTSHRGPATLQATKTDDFSGSTLLPAMGNHCGPLGGPQDLEKTSRGRGSPPPPPREASLAMCGLLQELASIRHFLEKREETREVARDWLRVGSVLDKLLFRVYLLAVLAYSITLVTLWSVWHYA
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This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel.
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O70215
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NKG2D_RAT
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NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NK lectin-like receptor) (NKLLR) (NKG2-D-activating NK receptor) (NKR-P2) (CD antigen CD314)
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MSKCHNYDLKPAKWDTSQEHQKQRSALPTSRPGENGIIRRRSSIEELKISPLFVVRVLVAAMTIRFTVITLTWLAVFITLLCNKEVSVSSREGYCGPCPNDWICHRNNCYQFFNENKAWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQSPANGSWQWEDGSSLSPNELTLVKTPSGTCAVYGSSFKAYTEDCSNPNTYICMKRAV
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Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins.
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O70220
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FOXQ1_MOUSE
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Forkhead box protein Q1 (HFH-1l) (HNF-3/forkhead-like protein 1) (HFH-1) (Hepatocyte nuclear factor 3 forkhead homolog 1)
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MKLEVFVPRAAHGDKMGSDLEGAGSSDVPSPLSAAGDDSLGSDGDCAANSPAAGSGAGDLEGGGGERNSSGGPSAQDGPEATDDSRTQASAAGPCAGGVGGGEGARSKPYTRRPKPPYSYIALIAMAIRDSAGGRLTLAEINEYLMGKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPWGKDNYWMLNPNSEYTFADGVFRRRRKRLSHRTTVSASGLRPEEAPPGPAGTPQPAPAARSSPIARSPARQEERSSPASKFSSSFAIDSILSKPFRSRRDGDSALGVQLPWGAAPCPPLRAYPALLPAAPGGALLPLCAYGASEPTLLASRGTEVQPAAPLLLAPLSTAAPAKPFRGPETAGAAHLYCPLRLPTALQAAAACGPGPHLSYPVETLLA
|
Plays a role in hair follicle differentiation.
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O70228
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ATP9A_MOUSE
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Probable phospholipid-transporting ATPase IIA (EC 7.6.2.1) (ATPase class II type 9A)
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MTDSIPLQPVRHKKRVDSRPRAGCCEWLRCCGGGEPRPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFSQFRYFFNFYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTIIREAVEEIRCYVRDKEMNSQVYSRLTSRGTVKVKSSNIQVGDLILVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFLGTFTREDSDPPISESLSIENTLWAGTVIASGTVVGVVLYTGRELRSVMNTSDPRSKIGLFDLEVNCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSWVIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMVFKRLHLGTVAYGLDSMDEVQSHIFSIYTQQSQDPPAQKGPTVTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTDQAEAEKQFEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQVLNLTILQVFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLVVAKKSLTEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVRPTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLTCAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSAALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKSEVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTSLILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVITLVSCLPLYVLKYLRRRFSPPSYSKLTS
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Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation. Also involved in endosome to trans-Golgi network retrograde transport (By similarity). In complex with MON2 and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a transporter of Wnt morphogens in developing tissues. Participates in the formation of endosomal carriers that direct WLS trafficking back to Golgi, away from lysosomal degradation. Appears to be implicated in intercellular communication by negatively regulating the release of exosomes. The flippase activity towards membrane lipids and its role in membrane asymmetry remains to be proved. Required for the maintenance of neurite morphology and synaptic transmission.
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O70230
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ZN143_MOUSE
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Zinc finger protein 143 (Zfp-143) (Selenocysteine tRNA gene transcription-activating factor) (mStaf)
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MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDGRLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSSLQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSDGVTSTGMIGENEQEKKMQIVLQGHATRVTPKSQQSGEKAFRCKYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHSGCGKAFATGYGLKSHFRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRTHTGERPFKCPIEGCGRSFTTSNIRKVHIRTHTGERPYYCTEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEAFFEPPPGQGDDVLKGSQITYVTGVDGEDIVSTQVATVTQSGLSQQVTLISQDGTQHVNISQADMQAIGNTITMVTQDGTPITVPTHDAVISSAGTHSVAMVTAEGTEGQQVAIVAQDLAAFHTASSEMGHQQHSHHLVTTETRPLTLVATSNGTQIAVQLGEQPSLEEAIRIASRIQQGETPGLDD
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Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:9535833}.
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O70237
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GFI1B_MOUSE
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Zinc finger protein Gfi-1b (Growth factor independent protein 1B)
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MPRSFLVKSKKAHTYHQPRAQGDELVWPPAVIPVAKEHSQSASPLLSTPLPSQTLDWNTIKQEREMLLNQSLPKMASAPEGPLVTPQPQDGESPLSESPPFYKPSFSWDTLASSYSHSYTQTPSTMQSAFLERSVRLYGSPLVPSTESPLDFRLRYSPGMDTYHCVKCNKVFSTPHGLEVHVRRSHSGTRPFACDVCGKTFGHAVSLEQHTHVHSQERSFECRMCGKAFKRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFSCELCTKGFQRKVDLRRHRESQHNLK
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Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Transcriptional repressor or activator depending on both promoter and cell type context represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1 GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation.
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O70239
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AXIN1_RAT
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Axin-1 (Axis inhibition protein 1) (rAxin)
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MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDSVPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHAPKLGLKLDSAGLHHHRHVHHHVHHNSARPKEQMEAEAARRVQSSFSWGPETHGHAKPRSYSESTGTNPSAGDLAFGGKASAPSKRNTKKAESGKNASAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGMRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRTKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAILPVFEEKIIGKVEKVD
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Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects down-regulates beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (By similarity). Also facilitates the phosphorylation of APC by GSK3B (By similarity). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (By similarity). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity).
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O70240
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AXIN2_RAT
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Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin)
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MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGIPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHQQCHALLPTGGKLPPEAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHSKPPEPLPGEQFCGSRGGTLPKRNTKGTEPGLALPAREGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSTQSIRKSYPLESARAPPGERVSRHHLLGASGHPRSAARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHPATGQAGPTSFSNPSLASEDHKEPKRLASVHALQASELIVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
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Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
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O70244
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CUBN_RAT
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Cubilin (460 kDa receptor) (Glycoprotein 280) (gp280) (Intrinsic factor-cobalamin receptor) (Intrinsic factor-vitamin B12 receptor)
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MSSQFLWGFVTLLMIAELDGKTGKPEQRGQKRIADLHQPRMTTEEGNLVFLTSSTQNIEFRTGSLGKIKLNDEDLGECLHQIQRNKDDIIDLRKNTTGLPQNILSQVHQLNSKLVDLERDFQNLQQNVERKVCSSNPCLNGGTCVNLHDSFVCICPSQWKGLFCSEDVNECVVYSGTPFGCQSGSTCVNTVGSFRCDCTPDTYGPQCASKYNDCEQGSKQLCKHGICEDLQRVHHGQPNFHCICDAGWTTPPNGISCTEDKDECSLQPSPCSEHAQCFNTQGSFYCGACPKGWQGNGYECQDINECEINNGGCSQAPLVPCLNTPGSFSCGNCPAGFSGDGRVCTPVDICSIHNGGCHPEATCSSSPVLGSFLPVCTCPPGYTGNGYGSNGCVRLSNICSRHPCVNGQCIETVSSYFCKCDSGWSGQNCTENINDCSSNPCLNGGTCIDGINGFTCDCTSSWTGYYCQTPQAACGGILSGTQGTFAYHSPNDTYIHNVNCFWIVRTDEEKVLHVTFTFFDLESASNCPREYLQIHDGDSSADFPLGRYCGSRPPQGIHSSANALYFHLYSEYIRSGRGFTARWEAKLPECGGILTDNYGSITSPGYPGNYPPGRDCVWQVLVNPNSLITFTFGTLSLESHNDCSKDYLEIRDGPFHQDPVLGKFCTSLSTPPLKTTGPAARIHFHSDSETSDKGFHITYLTTQSDLDCGGNYTDTDGELLLPPLSGPFSHSRQCVYLITQAQGEQIVINFTHVELESQMGCSHTYIEVGDHDSLLRKICGNETLFPIRSVSNKVWIRLRIDALVQKASFRADYQVACGGMLRGEGFFRSPFYPNAYPGRRTCRWTISQPQRQVVLLNFTDFQIGSSASCDTDYIEIGPSSVLGSPGNEKFCSSNIPSFITSVYNILYVTFVKSSSMENRGFTAKFSSDKLECGEVLTASTGIIESPGHPNVYPRGVNCTWHVVVQRGQLIRLEFSSFYLEFHYNCTNDYLEIYDTAAQTFLGRYCGKSIPPSLTSNSNSIKLIFVSDSALAHEGFSINYEAIDASSVCLYDYTDNFGMLSSPNFPNNYPSNWECIYRITVGLNQQIALHFTDFTLEDYFGSQCVDFVEIRDGGYETSPLVGIYCGSVLPPTIISHSNKLWLKFKSDAALTAKGFSAYWDGSSTGCGGNLTTPTGVLTSPNYPMPYYHSSECYWRLEASHGSPFELEFQDFHLEHHPSCSLDYLAVFDGPTTNSRLIDKLCGDTTPAPIRSNKDVVLLKLRTDAGQQGRGFEINFRQRCDNVVIVNKTSGILESINYPNPYDKNQRCNWTIQATTGNTVNYTFLGFDVESYMNCSTDYVELYDGPQWMGRYCGNNMPPPGATTGSQLHVLFHTDGINSGEKGFKMQWFTHGCGGEMSGTAGSFSSPGYPNSYPHNKECIWNIRVAPGSSIQLTIHDFDVEYHTSCNYDSLEIYAGLDFNSPRIAQLCSQSPSANPMQVSSTGNELAIRFKTDSTLNGRGFNASWRAVPGGCGGIIQLSRGEIHSPNYPNNYRANTECSWIIQVERHHRVLLNITDFDLEAPDSCLRLMDGSSSTNARVASVCGRQQPPNSIIASGNSLFVRFRSGSSSQNRGFRAEFREECGGRIMTDSSDTIFSPLYPHNYLHNQNCSWIIEAQPPFNHITLSFTHFQLQNSTDCTRDFVEILDGNDYDAPVQGRYCGFSLPHPIISFGNALTVRFVTDSTRSFEGFRAIYSASTSSCGGSFYTLDGIFNSPDYPADYHPNAECVWNIASSPGNRLQLSFLSFNLENSLNCNKDFVEIREGNATGHLIGRYCGNSLPGNYSSAEGHSLWVRFVSDGSGTGMGFQARFKNIFGNNNIVGTHGKIASPFWPGKYPYNSNYKWVVNVDAYHIIHGRILEMDIEPTTNCFYDSLKIYDGFDTHSRLIGTYCGTQTESFSSSRNSLTFQFSSDSSVSGRGFLLEWFAVDVSDSTPPTIAPGACGGFMVTGDTPVHIFSPGWPREYANGADCIWIIYAPDSTVELNILSLDIEPQQSCNYDKLIVKDGDSDLSPELAVLCGVSPPGPIRSTGEYMYIRFTSDTSVAGTGFNASFHKSCGGYLHADRGVITSPKYPDTYLPNLNCSWHVLVQTGLTIAVHFEQPFQIQNRDSFCSQGDYLVLRNGPDNHSPPLGPSGRNGRFCGMYAPSTLFTSGNEMFVQFISDSSNGGQGFKIRYEAKSLACGGTVYIHDADSDGYLTSPNYPANYPQHAECIWILEAPPGRSIQLQFEDQFNIEDTPNCSVSYLELRDGANSNARLVSKLCGHTLPHSWVSSRERIYLKFHTDGGSSYMGFKAKYSIASCGGTVSGDSGVIESIGYPTLPYANNVFCQWFIRGLPGHYLTLSFEDFNLQSSPGCTKDFVEIWENHTSGRVLGRYCGNSTPSSVDTSSNVASVKFVTDGSVTASGFRLQFKSSRQVCGGDLHGPTGTFTSPNYPNPNPHARICEWTITVQEGRRIVLTFTNLRLSTQPSCNSEHLIVFNGIRSNSPLLQKLCSRVNVTNEFKSSGNTMKVVFFTDGSRPYGGFTASYTSTEDAVCGGFLPSVSGGNFSSPGYNGIRDYARNLDCEWTLSNPNRENSSISIYFLELSIESHQDCTFDVLEFRVGDADGPLIEKFCSLSAPTAPLVIPYPQVWIHFVSNERVEYTGFYIEYSFTDCGGIRTGDNGVISSPNYPNLYSAWTHCSWLLKAPEGHTITLTFSDFLLEAHPTCTSDSVTVRNGDSPGSPVIGRYCGQSVPRPIQSGSNQLIVTFNTNNQGQTRGFYATWTTNALGCGGTFHSANGTIKSPHWPQTFPENSRCSWTVITHESKHWEISFDSNFRIPSSDSQCQNSFVKVWEGRLMINKTLLATSCGDVAPSPIVTSGNIFTAVFQSEEMAAQGFSASFISRCGRTFNTSPGDIISPNFPKQYDNNMNCTYLIDADPQSLVILTFVSFHLEDRSAITGTCDHDGLHIIKGRNLSSTPLVTICGSETLRPLTVDGPVLLNFYSDAYTTDFGFKISYRAITCGGIYNESSGILRSPSYSYSNYPNNLYCVYSLHVRSSRVIIIRFNDFDVAPSNLCAHDFLEVFDGPSIGNRSLGKFCGSTRPQTVKSTNSSLTLLFKTDSSQTARGWKIFFRETIGPQQGCGGYLTEDNQSFVSPDSDSNGRYDKGLSCIWYIVAPENKLVKLTFNVFTLEGPSSAGSCVYDYVQIADGASINSYLGGKFCGSRMPAPFISSGNFLTFQFVSDVTVEMRGFNATYTFVDMPCGGTYNATSTPQNASSPHLSNIGRPYSTCTWVIAAPPQQQVQITVWDLQLPSQDCSQSYLELQDSVQTGGNRVTQFCGANYTTLPVFYSSMSTAVVVFKSGVLNRNSQVQFSYQIADCNREYNQTFGNLKSPGWPQNYDNNLDCTIILRAPQNHSISLFFYWFQLEDSRQCMNDFLEVRNGGSSTSPLLDKYCSNLLPNPVFSQSNELYLHFHSDHSVTNNGYEIIWTSSAAGCGGTLLGDEGIFTNPGFPDSYPNNTHCEWTIVAPSGRPVSVGFPFLSIDSSGGCDQNYLIVFNGPDANSPPFGPLCGINTGIAPFYASSNRVFIRFHAEYTTRLSGFEIMWSS
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Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.
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O70247
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SC5A6_RAT
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Sodium-dependent multivitamin transporter (Na(+)-dependent multivitamin transporter) (Solute carrier family 5 member 6)
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MTVASTAAPSYTTSDTNRVISTFSVVDYVVFGLLLVLSLVIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGGPAEIYRFGTQYWFLGCSYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKAVRICGTVTFIFQMVVYMGVALYAPSLALNAVTGFDLWLSVLALGIVCNIYTALGGLKAVIWTDVFQTLIMFLGQLVVIIVGAAKVGGLGHVWAVASQHGLISGIELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSHSEKAAVLSCYAVFPCQQVALCMSCLIGLVMFAYYKKYSMSPQQEQAAPDQLVLYFVMDLLKDMPGLPGLFVACLFSGSLSTISSAFNSLATVTMEDLIQPWFPQLTETRAIMLSRSLAFAYGLVCLGMAYVSSHLGSVLQAALSIFGMVGGPLLGLFCLGMFFPCANPLGAIVGLLTGLTMAFWIGIGSIVSRMSSAAASPPLNGSSSFLPSNLTVATVTTLMPSTLSKPTGLQQFYSLSYLWYSAHNSTTVIAVGLIVSLLTGGMRGRSLNPGTIYPVLPKLLALLPLSCQKRLCWRSHNQDIPVVTNLFPEKMGNGALQDSRDKERMAEDGLVHQPCSPTYIVQETSL
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Sodium-dependent multivitamin transporter that mediates the electrogenic transport of pantothenate, biotin, lipoate and iodide. Functions as a Na(+)-coupled substrate symporter where the stoichiometry of Na(+):substrate is 2:1, creating an electrochemical Na(+) gradient used as driving force for substrate uptake. Required for biotin and pantothenate uptake in the intestine across the brush border membrane (By similarity). Plays a role in the maintenance of intestinal mucosa integrity, by providing the gut mucosa with biotin (By similarity). Contributes to the luminal uptake of biotin and pantothenate into the brain across the blood-brain barrier (By similarity).
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O70249
|
OGG1_RAT
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N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
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MLFSSSLSSSMRHRTLTSSPALWASIPCPRSELRLDLVLASGQSFRWREQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDKGQVGRPTLEELETLHKYFQLDVSLTQLYSHWASVDSHFQSVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLVQLDDVTYHGFPNLHALAGPEVETHLRKLGLGYRARYVCASAKAILEEQGGPAWLQQLRVASYEEAHKALCTLPGVGTKVADCICLMALDKPQAVPVDIHVWQIAHRDYGWQPKTSQTKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQQNLSREPPAKRKKGSKKTEG
|
DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
|
O70250
|
PGAM2_MOUSE
|
Phosphoglycerate mutase 2 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 2) (Muscle-specific phosphoglycerate mutase) (Phosphoglycerate mutase isozyme M) (PGAM-M)
|
MTTHRLVMVRHGESLWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYTSISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGQRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELDQNLKPTKPMRFLGDEETVRKAMEAVAAQGKAK
|
Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
|
O70252
|
HMOX2_MOUSE
|
Heme oxygenase 2 (HO-2) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 2 soluble form]
|
MSSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPSLQLILAASVALVAGLLAWYYM
|
[Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. [Heme oxygenase 2 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
|
O70255
|
MPZL2_MOUSE
|
Myelin protein zero-like protein 2 (Epithelial V-like antigen 1)
|
MYGKSPALVLPLLLSLQLTALCPTEAVEIYTSGALEAVNGTDVRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSILLWKLQFDDNGTYTCQVKNPPDVDGLVGTIRLSVVHTVPFSEIYFLAVAIGSACALMIIVVIVVVLFQHFRKKRWADRADKAEGTKSKEEEKLNQGNKVSVFVEDTD
|
Mediates homophilic cell-cell adhesion.
|
O70257
|
STX7_RAT
|
Syntaxin-7
|
MSYTPGIGGDPAQLAQRISSNIQKITQCSAEIQRTLNQLGTPQDTPELRQQLQQEQQYTNQLAKETDKYIKEFGFLPTTPSEQRQRKIQKDRLVAEFTTALTNFQKVQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNFVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDVIDSIEANVESAEVHVQQANQQLSRAANYQRKSRKTLCIIILILVVGIVIIFFIVWGLKG
|
May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity).
|
O70258
|
SGCE_MOUSE
|
Epsilon-sarcoglycan (Epsilon-SG)
|
MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTHFHIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVTLAVPSAVALVLFLILAYIMCCRREGVEKRDMQTPDIQLVHHSSIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEVIPPTHTDNYDSTNMPLMQAQQNLPHQTQIPQPQTTGKWYP
|
Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
|
O70260
|
PIAS3_RAT
|
E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (KChAP) (Potassium channel-associated protein) (Protein inhibitor of activated STAT protein 3)
|
MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPSPLASIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSPVQEGNQSENKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYSPSVITSLDEQDTLGHFFQFRGTPPHFLGPLAPTLGSSHRSATPAPAPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD
|
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1. Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity).
|
O70263
|
LNX1_MOUSE
|
E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb protein X 1) (Ligand of Numb-binding protein 1) (Numb-binding protein 1) (RING-type E3 ubiquitin transferase LNX)
|
MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTSCKGASHYGLTKDRKRRSQDGCPDGCASLMATTLSPEVSAAATISLMTDEPGLDNPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVVANHVDQGRDNSENTTVPEVFPRLFHLIPDGEITSIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDGRLLPGDIILKVNGMDISNVPHNYAVRLLRQPCQVLRLTVLREQKFRSRSNAHVPDSYGPRDDSFHVILNKSSPEEQLGIKLVRRVDEPGVFIFNVLNGGVADRHGQLEENDRVLAINGHDLRFGSPESAAHLIQASERRVHLVVSRQVRQSSPDIFQEAGWISNGQQSPGPGERNTASKPAATCHEKVVSVWKDPSESLGMTVGGGASHREWDLPIYVISVEPGGVISRDGRIKTGDILLNVNGIELTEVSRTEAVAILKSAPSSVVLKALEVKEQEAQEDCSPAALDSNHNVTPPGDWSPSWVMWLELPQYLCNCKDVILRRNTAGSLGFCIVGGYEEYSGNKPFFIKSIVEGTPAYNDGRIRCGDILLAVNGRSTSGMIHACLARMLKELKGRITLTIASWPGTFL
|
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
|
O70274
|
TP4A2_MOUSE
|
Protein tyrosine phosphatase type IVA 2 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a2) (Protein-tyrosine phosphatase of regenerating liver 2) (PRL-2)
|
MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ
|
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB (By similarity).
|
O70276
|
RPE65_RAT
|
Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase)
|
MSIQIEHPAGGYKKLFETVEELSTPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYYRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEITDNALVNIYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIESDGTVYNIGNCFGKNFTVAYNIIKIPPLKADKEDPINKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNESMGVWLHVADKKRRKYFNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKRNAMKAPQPEVRRYVLPLTIDKADTGRNLVTLPHTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKCGGKPYTYAYGLGLNHFVPDKLCKLNVKTKEIWMWQEPDSYPSEPIFVSQPDALEEDDGVVLSVVVSPGAGQKPAYLLVLNAKDLSEIARAEVETNIPVTFHGLFKKP
|
Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT.
|
O70277
|
TRIM3_RAT
|
Tripartite motif-containing protein 3 (EC 2.3.2.27) (Brain-expressed RING finger protein) (RING finger protein 22)
|
MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSAAAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELCAEITGPDGMRLAVPVVDHKNGTYELVYTARTEGDLLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIVDELVFRVGSRGREKGEFTNLHPLSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
|
E3 ubiquitin ligase that plays essential roles in neuronal functions such as regulation of neuronal plasticity, learning, and memory. In addition to its neuronal functions, participates in other biological processes such as innate immunity or cell cycle regulation. Component of the cytoskeleton-associated recycling or transport complex in neurons, polyubiquitinates gamma-actin, thus regulating neuronal plasticity, learning, and memory (By similarity). Ubiquitinates postsynaptic scaffold GKAP, a neuronal substrate involved in synaptic remodeling and thereby modulates dendritic spine morphology. Positively regulates motility of microtubule-dependent motor protein KIF21B (By similarity). Induces growth arrest via its RING-dependent E3 ligase activity and ubiquinates CDKN1A. Positively regulates TLR3-mediated signaling by mediating 'Lys-63'-linked polyubiquitination of TLR3. In turn, promotes the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes (By similarity).
|
O70281
|
TPST1_MOUSE
|
Protein-tyrosine sulfotransferase 1 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 1) (TPST-1)
|
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPARLENPKATVRAGLDIKANKTFTYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEVIVKHGEPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKILENTRRVYKGEFQLPDFLKEKPQTEQVE
|
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
|
O70283
|
WNT2B_MOUSE
|
Protein Wnt-2b (Protein Wnt-13)
|
MLKLQGEDEAAQLAPRRARVPVPRPTAPDVSPSSARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRAMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVTATQDGANFTAARQGYRHATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT
|
Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a redundant role in embryonic lung development.
|
O70291
|
GRK4_MOUSE
|
G protein-coupled receptor kinase 4 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK4)
|
MELENFVANNLLLKARLGFNKQTGRSKKWRELLKFPPVSMCTELRWSIEKDFSSLCDKQPIGRLLFRQFCDTKPDLKRCIEFLDAVAEYEVTIEEEQREFGLAIFSRFFKEKSEVPLPEIPPDIVKECKWNLKQNSPSQNVFEECAGIVCKYLSETPFEEYQESTYFNRFLQWKWLERRPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKLHSRFVVSLAYTYETKDALCLVLTIMNGGDLKYHIYNLGDPGFEEPRAVFYAAELCCGLEDLQRKRIVYRDLKPENILLDDHGHIRISDLGLAMEVPEGEMVRGRVGTVGYMAPEIINHEKYTFSPDWWGLGCLIYEMIAGHSPFRKYKEKVNREELERRVKNETEEYSERFSEDAKSICSMLLIKDPSKRLGCQRDGVSAVKQHPIFKDINFSRLEANMLDPPFIPDPQAIYCRNILDIGQFSVVKGVNLDTNDEIFYAEFATGSVTIPWQNEMIESGCFKDLNENEDDLSSLEKYKMCSSILRPKRNFFRRLFRRTGCLNIALSEEREPTEH
|
Specifically phosphorylates the activated forms of G protein-coupled receptors.
|
O70293
|
GRK6_MOUSE
|
G protein-coupled receptor kinase 6 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK6)
|
MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELTRCTAFLDGVSEYEVTPDEKRKACGRRLMQNFLSHTGPDLIPEVPRQLVSNCAQRLEQGPCKDLFQELTRLTHEYLSTAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVRNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVAEEYTDRFSSQARSLCSQLLSKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPDPQAIYCKDVLDIEQFSTVKGVDLEPTDQDFYQKFATGSVSIPWQNEMVETECFQELNVFGLDGSVPPDLDWKGQPTAPPKKGLLQRLFSRQDCCGNCSDSEEELPTRL
|
Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12032308, ECO:0000269|PubMed:12718862, ECO:0000269|PubMed:14634128}.
|
O70299
|
MB211_MOUSE
|
Putative nucleotidyltransferase MAB21L1 (EC 2.7.7.-) (Protein mab-21-like 1)
|
MIAAQAKLVYHLNKYYNEKCQARKAAIAKTIREVCKVVSDVLKEVEVQEPRFISSLNEMDNRYEGLEVISPTEFEVVLYLNQMGVFNFVDDGSLPGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRSRFQTLVAQAVDKCSYRDVVKMVADTSEVKLRIRDRYVVQITPAFKCTGIWPRSAAHWPLPHIPWPGPNRVAEVKAEGFNLLSKECHSLAGKQSSAESDAWVLQFAEAENRLQMGGCRKKCLSILKTLRDRHLELPGQPLNNYHMKTLVSYECEKHPRESDWDESCLGDRLNGILLQLISCLQCRRCPHYFLPNLDLFQGKPHSALENAAKQTWRLAREILTNPKSLEKL
|
Putative nucleotidyltransferase required for several aspects of embryonic development including normal development of the eye, notochord, neural tube and other organ tissues, and for embryonic turning. It is unclear whether it displays nucleotidyltransferase activity in vivo (By similarity). Binds single-stranded RNA (ssRNA) (By similarity).
|
O70302
|
CIDEA_MOUSE
|
Lipid transferase CIDEA (Cell death activator CIDE-A) (Cell death-inducing DFFA-like effector A)
|
METARDYAGALIRPLTFMGLQTKKVLLTPLIHPARPFRVSNHDRSSRRGVMASSLQELISKTLDVLVITTGLVTLVLEEDGTVVDTEEFFQTLRDNTHFMILEKGQKWTPGSKYVPVCKQPKKSGIARVTFDLYRLNPKDFLGCLNVKATMYEMYSVSYDIRCTSFKAVLRNLLRFMSYAAQMTGQFLVYAGTYMLRVLGDTEEQPSPKPSTKGWFM
|
Lipid transferase that promotes unilocular lipid droplet formation by mediating lipid droplet fusion. Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage. Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by promoting directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. May also act as a CEBPB coactivator in epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter. When overexpressed, induces apoptosis the physiological significance of its role in apoptosis is unclear.
|
O70303
|
CIDEB_MOUSE
|
Lipid transferase CIDEB (Cell death activator CIDE-B) (Cell death-inducing DFFA-like effector B)
|
MEYLSAFNPNGLLRSVSTVSSELSRRVWNSAPPPQRPFRVCDHKRTVRKGLTAASLQELLDKVLETLLLRGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLEQGQSWSPKSGMLSYGLGREKPKHSKDIARITFDVYKQNPRDLFGSLNVKATFYGLYSMSCDFQGVGPKRVLRELLRWTSSLLQGLGHMLLGISSTLRHVVEGADRWQWHGQRHLHS
|
Lipid transferase specifically expressed in hepatocytes, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion. Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage. Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (By similarity). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (By similarity). Promotes lipid exchange and lipid droplet fusion in both small and large lipid droplet-containing hepatocytes. In addition to its role in lipid droplet fusion, also involved in cytoplasmic vesicle biogenesis and transport. Required for very-low-density lipoprotein (VLDL) lipidation and maturation. Probably involved in the biogenesis of VLDL transport vesicles by forming a COPII vesicle coat and facilitating the formation of endoplasmic reticulum-derived large vesicles. Also involved in sterol-regulated export of the SCAP-SREBP complex, composed of SCAP, SREBF1/SREBP1 and SREBF2/SREBP2, by promoting loading of SCAP-SREBP into COPII vesicles. May also activate apoptosis.
|
O70305
|
ATX2_MOUSE
|
Ataxin-2 (Spinocerebellar ataxia type 2 protein homolog)
|
MRSSTAAVQRPAAGDPEPRRPAGWAARRSLPRTARRGGRGGAVAYPSAGPPPRGPGAPPRGPRSPPCASDCFGSNGHGASRPGSRRLLGVCGPPRPFVVVLLALAPAATPARACPPGVRASPPRSGVSSSARPAPGCPRPACEPVYGPLTMSLKPQPQPPAPATGRKPGGGLLSSPGAAPASAAVTSASVVPAPAAPVASSSAAAGGGRPGLGRGRNSSKGLPQPTISFDGIYANVRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESVLFKCSDFVVVQFKDTDSSYARRDAFTDSALSAKVNGEHKEKDLEPWDAGELTASEELELENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNCSDREGHGPNTRDNKYIPPGQRNREVLSWGSGRQSSPRMGQPGPGSMPSRAASHTSDFNPNAGSDQRVVNGGVPWPSPCPSHSSRPPSRYQSGPNSLPPRAATHTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSMSSGLEFVSHNPPSEAAAPPVARTSPAGGTWSSVVSGVPRLSPKTHRPRSPRQSSIGNSPSGPVLASPQAGIIPAEAVSMPVPAASPTPASPASNRALTPSIEAKDSRLQDQRQNSPAGSKENVKASETSPSFSKADNKGMSPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLSKNREGEKSRDLIKDKTEASAKDSFIDSSSSSSNCTSGSSKTNSPSISPSMLSNAEHKRGPEVTSQGVQTSSPACKQEKDDREEKKDTTEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPAPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAGKVPNMPQQRQDQHHQSTMMHPASAAGPPIVATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPAHAQPGLVSSSAAQFGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNAALHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQSSFPAAQQTVFTIHPSHVQPAYTTPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGPKAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL
|
Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane.
|
O70306
|
TBX15_MOUSE
|
T-box transcription factor TBX15 (T-box protein 15) (MmTBx8) (T-box transcription factor TBX14) (T-box protein 14)
|
MSERRRSAVALSSRAHAFSVEALIGSNKKRKLRDWEEKGLDLSMEALSPAGPLGDTDDPATHGLEPHPDSEQSTGSDSEVLTERTSCSFSTHTDLASGAAGPVPAAMSSMEEIQVELQCADLWKRFHDIGTEMIITKAGRRMFPAMRVKITGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSLASGDTWMRQVVSFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDFSSDLSPTKPVPVGDGVKTFNFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRTGLEAIMETYAFWRPPVRTLTFEDFTTMQKQQGGSTGTSPTTSSTGTPSPSASSHLLSPSCSPPTFHLAPNTFNVGCRESQLCNLNLSDYPPCARSNMAALQSYPGLSDSGYNRLQSGTASATQPSETFMPQRTPSLISGIPTPPSLPSNSKMEAYGGQLGSFPTSQFQYVMQAGNAASSSSSPHMFGGSHMQQSSYNAFSLHNPYNLYGYNFPTSPRLAASPEKLSASQSTLLCSSPSNGAFGERQYLPTGMEHSMHMISPSTNNQQATNTCDGRQYGAVPGSASQMSVHMV
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Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes.
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O70309
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ITB5_MOUSE
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Integrin beta-5
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MPRVPATLYACLLGLCALVPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEYFGNPRSITSRCDLKANLIRNGCEGEIESPASSTHVLRNLPLSSKGSSATGSDVIQMTPQEIAVSLRPGEQTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLENIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILHGDSKNIIQLIINAYSSIRAKVELSVWDQPEDLNLFFTATCQDGISYPGQRKCEGLKIGDTASFEVSVEARSCPGRQAAQSFTLRPVGFRDSLQVEVAYNCTCGCSTGLEPNSARCSGNGTYTCGLCECDPGYLGTRCECQEGENQSGYQNLCREAEGKPLCSGRGECSCNQCSCFESEFGRIYGPFCECDSFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDVSTCKAKDGQICSDRGRCVCGQCQCTEPGAFGETCEKCPTCPDACSSKRDCVECLLLHQGKPDNQTCHHQCKDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFSYTELPNGRSNLTVLREPECGSAPNAMTILLAVVGSILLIGMALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFAFNKFNKSYNGSV
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Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.
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O70310
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NMT1_MOUSE
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Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (NMT 1) (Type I N-myristoyltransferase) (Peptide N-myristoyltransferase 1)
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MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDNSHNRSGLSPANDTGAKKKKKKQKKKKEKGSDMESTQDQPVKMTSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMEKKDIPVVHQLLSRYLKQFHLTPVMNQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
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Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (By similarity). Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle (By similarity). Required for normal embryogenesis.
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O70318
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E41L2_MOUSE
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Band 4.1-like protein 2 (Erythrocyte membrane protein band 4.1-like 2) (Generally expressed protein 4.1) (4.1G)
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MTTEVGSASEVKKGSDQAGADASKEKAKEVENEQTPVSEPEEEKGSQPGPPVERQSTPRLRKRGKDPSENRGISRFIPPWLKKQRSYNLVVAKDGGDKKEPTQADVEDQILGKEESLPEEESRAKGDAEEMAQRKHLEVQVEVREAKPALKSSVETQPAEEVRKDKEETIQDTQEEKLEGGAAKRETKEVQTSELKAEVASQKATKKTKTVLAKVTLLDGTEYSCDLEKRAKGQVLFDRVCEHLNLLEKDYFGLLFQDHPEQKNWLDPAKEIKRQLKNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAEHGDYDPEEYDSIDLGDFQFAPAHTKELEEKVSELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKTKFLTLGSKFRYSGRTQAQTREASTLIDRPAPQFERASSKRVSRSLDGAPIGVVDQSPPGEGSVPGPGVISYTTIQDGRRDSKSPTKATPLPAEGKKNTLRVDGDNIYVRHSNLMLEDLDKAQEAILKHQASISELKRNFMASTPEPRPSEWEKRRVTPLPFQPQASSHETLNVVEEKKRAEVGKDESVITEEMNGKEMSPGHGPGETRKVEPVAHKDSTSLSSESSSSSSESEEDVGEYQPHHRVTEGTIREEQEECDEELEEEPGQGAKVVEREAAVPDAVPDRQAGASVLPVETEAQEHVVAQKLPGEKGAHGGTAEQDPREEAEEDPHRVNGEVPHLDLDGLPEIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGVLLTAQTITSESASTTTTTHITKTVKGGISETRIEKRIVITGDAALDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGEE
|
Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.
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O70320
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PLB1_CAVPO
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Phospholipase B1, membrane-associated (Phospholipase B) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A2) (EC 3.1.1.4) (Phospholipase B/lipase) (PLB/LIP) (Triacylglycerol lipase) (EC 3.1.1.3)
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MGLQPGVLLVGLLLLGQGITQIHTSSGKSTLEGQLWPETKKNFPFSCSPKKLGLNMPSESVHTLTPADIKLIAAIGDMETPPDSGAVNLDTSERTEKEPWRGCMGMMTVLSDIISHFNPSVLLPTCPPWRSAAVRGGVEELRTQAEELVSSLKKNPQLDFQQDWKLINVFFSNASLCYLCPSAHENGPLMSNMDKLAGILHYLHQEVPRAFVNLVDLFEVVAMPRWHQGTMLSRPSPEACGCSGETSKLDTVVMQWSYQETWDSLLASSSFNDQESFAVVFQPFFYEVSSPVEEPPSQDPTTLALSLWNNMMKPVGQKDEPFSTIERRPMKCPSQESPYLFTYRNSNYQSRLLKRQRQHKEREGTEIRCPDKDPSDSTPTSVHRLKPADIKVIGALGDSLTAGNGAGSRPGNILDVLTEYRGLSWSIGADHNISSVTTLPNILREFNPSLKGFSTGTGKANSVGAFFNQAVAGARAGDLIPQARTLVDLMKNHTSINFEEDWKIITVFIGGNDLCDFCSDPVTNSPENFTDNIRQALDILHAEVPRAFVNMVKVLQIVNLRELYKDSRVSCPRLILRNLCRCVLLPDDNSTELESLIDINKKYQERTHQLIESGRYDTREDFTVVLQPFFEKVDIPKTSEGLPDNTSFAPDCFHFSSKTHARAASALWKNMLEPVGQKTTQNNFENSIDIICPNQAFPYLSTYKNGIEGHGTWLTCRERTPSASPPTSVHALRPADVRVVAALGDSLTAGSGIGSKPGDLADVITQYRGLSYSSGGDGSLMNVTTLPNILREFNSNLTGYAVGTGDASNTNAFLNQAVPGAKAEELMSQVKTLVQKMKDDPRINFHEDWKVITVLIGTNDLCNHCTDLDLYSSANFFNHLLNALDILHREVPRALVNLVDFMNPSIMRQVFLGNPDKCPVQQASILCNCVLSLRENSYELARMDALTRAYQSSMRELVESGRYDTREDFSVVLQPFFLNIRLPILEDGRPDTSFFAPDCINPGQKFHSQLSRALWVNMLEPVGSKTDTLDLTADISLPCPTQEEPFLRTPQNSDYTYPTKPAIENWGSDFLCTEWKPSNSVPTSVHKLQPADIKVVAALGDSLTTAVGARASNSSDLLMSWRGLSWSIGGDGALETHTTLPNILKKFNPSIFGFSTGTLEETAGFNVAVEEARARDMPAQARDLVERMKASTEINLEMDWKLITLFIGSNDLCHYCDNPENHSAEEYVQHIRQALDILYEELPRAFINVVDIIMELAGLHQGQGGHCTALLPAQSTCSCLRHFPSSPVIQELKKVTWNLQSDMSRLSYQEKYTQREDFAVVVQPFFQNTLIPLDKLGSTDPTFFSEDCLHFSERGHAEMAIALWNNMLEPVGHKTTFNNFTYNRTKLKCPSTESPYLYTLQNSLSLPVQTEKASGVAPGIVSAAAAGGLLVGLIVGILAVSLWSSFRRRQKKSPPESVPVANF
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Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (By similarity). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (By similarity).
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O70324
|
MOT8_MOUSE
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Monocarboxylate transporter 8 (MCT 8) (Solute carrier family 16 member 2) (X-linked PEST-containing transporter)
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MALPSPASEEAEGPCQEANQEYQEPVCSPVPEPEPEPEPEPEPDPEPVPVPPPEPQPEPEPQPLPDPAPLPELGFEAEPVQEPEPTPTVETRGTARGFQPPEGGFGWIVVFAATWCNGSIFGIHNSVGILYSMLLEEEKEKNRQVEFQAAWVGALAMGMIFFCSPIVSIFTDRLGCRITATTGAAVAFIGLHTSSFTSSLSLRYFTYGILFGCGCSFAFQPSLVILGHYFQRRLGLANGVVSAGSSIFSMSFPFLIKMLGDKIKLAQTFQVLSTFMFVLTLLSLTYRPLLPSSQDTPSKRGAHTLRQRFLVQFRKYFNMRVFRQRTYRIWAFGIAAAALGYFVPYVHLMKYVEDKFKEIKETWVLLVCIGATSGLGRLVSGHISDSIPGLKKIYLQVLSFLLLGLMSMMIPLCRDFGGLIVVCLFLGLCDGFFITIMAPIAFELVGPMQASQAIGYLLGMMALPMIAGPPIAGLLRNCFGDYHVAFYFAGVPPIIGAVILFFVPLMHQRMFKKEQRDSSKDKMLSHDPDPNGELLPGSPTPEEPI
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Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient. Major substrates are the iodothyronines T3 and T4 and to a lesser extent rT3 and 3,3-diiodothyronine (3,3'-T2). Acts as an important mediator of thyroid hormone transport, especially T3, through the blood-brain barrier.
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O70325
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GPX4_MOUSE
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Phospholipid hydroperoxide glutathione peroxidase (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4)
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MSWGRLSRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVCLDKYRGFVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAGYNVKFDMYSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
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Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation. Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species. The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis. The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures. May be required to protect cells from the toxicity of ingested lipid hydroperoxides. Required for normal sperm development and male fertility. Essential for maturation and survival of photoreceptor cells. Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion. Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity).
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O70326
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GREM1_MOUSE
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Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein)
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MNRTAYTVGALLLLLGTLLPTAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
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Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as BMP a antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner. Antagonist of BMP2 inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (By similarity). Acts as inhibitor of monocyte chemotaxis (By similarity).
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O70333
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CRIPT_MOUSE
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Cysteine-rich PDZ-binding protein (Cysteine-rich interactor of PDZ three) (Cysteine-rich interactor of PDZ3)
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MVCEKCEKKLGRVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFSTCRICKSSVHQPGSHYCQGCAYKKGICAMCGKKVLDTKNYKQTSV
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As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses (By similarity).
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O70337
|
BIK_MOUSE
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Bcl-2-interacting killer (Apoptosis inducer NBK) (Bik-like killer protein)
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MSEARLMARDVIKTVPHDQVPQPPVASETPSMKEPVRDVDLMECVEGRNQVALRLACIGDEMDLCLRSPRLVQLPGIAIHRLAVTYSRTGVRGIFRSLIRSLTNLRENIWSWRVLTPGAWVSPDQDPGQLFPMVLLVFLLLGGAWYLQLQ
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Accelerates programmed cell death. Binding to the apoptosis repressors Bcl-X(L), BHRF1 or Bcl-2 suppresses this death-promoting activity.
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O70342
|
NPY5R_MOUSE
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Neuropeptide Y receptor type 5 (NPY5-R) (NPY-Y5 receptor) (NPYY5-R) (Y5 receptor)
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MEVKLEEHFNKTFVTENNTAASQNTASPAWEDYRGTENNTSAARNTAFPVWEDYRGSVDDLQYFLIGLYTFVSLLGFMGNLLILMAVMKKRNQKTTVNFLIGNLAFSDILVVLFCSPFTLTSVLLDQWMFGKAMCHIMPFLQCVSVLVSTLILISIAIVRYHMIKHPISNNLTANHGYFLIATVWTLGFAICSPLPVFHSLVELKETFGSALLSSKYLCVESWPSDSYRIAFTISLLLVQYILPLVCLTVSHTSVCRSISCGLSHKENRLEENEMINLTLHPSKKSRDQAKPPSTQKWSYSFIRKHRRRYSKKTACVLPAPAGPSQEKHLTVPENPGSVRSQLSPSSKVIPGVPICFEVKPEESSDAQEMRVKRSLTRIKKRSRSVFYRLTILILVFAVSWMPLHVFHVVTDFNDNLISNRHFKLVYCICHLLGMMSCCLNPILYGFLNNGIKADLRALIHCLHMS
|
Receptor for neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders (By similarity).
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O70343
|
PRGC1_MOUSE
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Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1-alpha) (PPAR-gamma coactivator 1-alpha) (PPARGC-1-alpha)
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MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGAVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHAANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSGLSRGHEERKTKRPSLRLFGDHDYCQSLNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSGQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPCQAVFDDKSDKTSELRDGDFSNEQFSKLPVFINSGLAMDGLFDDSEDESDKLSYPWDGTQPYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEAYEHERLKRDEYRKEHEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDTNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR
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Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner (By similarity). Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK.
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O70344
|
KCNQ1_CAVPO
|
Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1)
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MAAASSPPRTERKRGGWGRLLGSRRGSASLAKKCPFSLELAEGGPAGGTLYAPVAPPGALSPGSPAPPASPAAPPAGLELGPRPPVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLACLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYVRKPARSHTLLSPSPKPKKSAMVRKKKFKPDKDNGVSPGEKMLTVPHITCDPPEERRPDHFSVDGYDSSVRKSPTLLEVSPTHFMRTNSFAEDLDLEGETLLTPITHVSQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVVITDMLHQLLSLHQGGPHSGGGPQMVQPCSEDGSIHPELFLPSNSLPTYEQLTVPQRGPDEAS
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Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity).
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O70348
|
DXO_MOUSE
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Decapping and exoribonuclease protein (DXO) (EC 3.6.1.-) (5'-3' exoribonuclease DXO) (EC 3.1.13.-) (Dom-3 homolog Z) (NAD-capped RNA hydrolase DXO) (DeNADding enzyme DXO) (EC 3.6.1.-)
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MEPRGTKRKAEKTEVEKPLNKLPRAVPSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPINGPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQLEGGPGWLAGATVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPLLRELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLFSGEVDCLNPQAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPHVVAGFRNPEGFVCSLKTFPTMEMFENVRNDREGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHRDAPYAFLPSWYVETMTQDLPPLSKTPSPKD
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Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to environmental stress (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA. Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates. Exhibits decapping activity towards FAD-capped RNAs. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
|
O70351
|
HCD2_RAT
|
3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-estradiol 17-dehydrogenase) (EC 1.1.1.62) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))) (EC 1.1.1.239) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (3alpha(or 20beta)-hydroxysteroid dehydrogenase) (EC 1.1.1.53) (7-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.159) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)
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MAAAVRSVKGLVAVITGGASGLGLSTAKRLVGQGATAVLLDVPNSEGETEAKKLGGNCIFAPANVTSEKEVQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHEKKNQVHTLEDFQRVINVNLIGTFNVIRLVAGVMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVVTIAPGLFATPLLTTLPDKVRNFLASQVPFPSRLGDPAEYAHLVQMVIENPFLNGEVIRLDGAIRMQP
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Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism. Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA. Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway. Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel. Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Essential for structural and functional integrity of mitochondria. In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
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O70355
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BTNL2_MOUSE
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Butyrophilin-like protein 2
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MVDCPRYSLSGVAASFLFVLLTIKHPDDFRVVGPNLPILAKVGEDALLTCQLLPKRTTAHMEVRWYRSDPDMPVIMYRDGAEVTGLPMEGYGGRAEWMEDSTEEGSVALKIRQVQPSDDGQYWCRFQEGDYWRETSVLLQVAALGSSPNIHVEGLGEGEVQLVCTSRGWFPEPEVHWEGIWGEKLMSFSENHVPGEDGLFYVEDTLMVRNDSVETISCFIYSHGLRETQEATIALSERLQTELASVSVIGHSQPSPVQVGENIELTCHLSPQTDAQNLEVRWLRSRYYPAVHVYANGTHVAGEQMVEYKGRTSLVTDAIHEGKLTLQIHNARTSDEGQYRCLFGKDGVYQEARVDVQVMAVGSTPRITREVLKDGGMQLRCTSDGWFPRPHVQWRDRDGKTMPSFSEAFQQGSQELFQVETLLLVTNGSMVNVTCSISLPLGQEKTARFPLSGW
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Negative regulator of T-cell proliferation.
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O70361
|
PER3_MOUSE
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Period circadian protein homolog 3 (mPER3) (Circadian clock protein PERIOD 3)
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MDPCGDPAVPGGDCPQTRGPGLQGASGQEGPLQGTCVDSSHSEHEDRNRMSEELIMVVQEMKKYFPAERHTKPSTLDALNYALRCVHSVQANSDFFQSLGPRGAHQADVTVYSLEDLTALASEHTSKNTDTFAAVFSFLSGRLVHISEQAALILNSKRGFLKSVHFVDLLAPQDVRAFYAHTAPTQLPFWNNWTQRASQYECAPAKPFFCRICGGGDREKRHYSPFRILPYLVHVHSSAQPEPEPCCLTLVEKIHSGYEAPRIPVDKRIFTTTHTPGCVFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEHSPVRFCTQNGEYVILDSSWSSFVNPWSRKVSFIIGRHKVRTSPLNEDVFATRIKKAASNDKDIAELQEQIHKLLLQPVHASASSGYGSLGSSGSQEQHVSITSSSESSGHCPEEGQHEQMTLQQVYASVNKIKNVGQQLYIESMARSSVKPVAETCVEPQGGDEQKDFSSSQTLKNKSTTDTGSGGNLQQEQPSSSYQQMNCIDSVIRYLTSYSLPALKRKCISCTNTSSSSEEAKPIPEVDSSQRDTEQLLDIRKQETTGPSTDIEGGAARTLSTAALSVASGISQCSCSSTSGHAPPLQSESVAVACKPWALRTKASHLAAGGFKHVGLTAAVLSAHTQKEEQNYVDRFREKILTSPYGCYLQQESRNRAQYSCVQAGSTAKHSRCAGSERQKHKRKKLPAPVDTSSPGAHLCPHVTGLLPDEQHWGPSASPSPLGAGLAFPSALVVPSQTPYLLPSFPLQDMASQGVGVSAAWGAAAGCPPLSAGPQAVAAFPSAYVDTLMTIFLHNAPLFPLWPPSFSPYPSLGAAGSSELAPLVPAMAPNPEPTTSGHSQRRVEENWEAHSEELPFISSRSSSPLQLNLLQEEMPAPSESADAVRRGAGPDAKHHCVTGPSGSRSRHCTSGELATATAQQESAAASGSSASSIYFSSTDYASEVSENRQRPQDRQRDEALPGAAEESIWRMIERTPECVLMTYQVPERGREEVLKQDLEKLQSMEQQQPLFSPAQREELAKVRSWIHSHTAPQEGHLQSCVACEDRGSVGDTAEVLEQHPAEDTS
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Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme.
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O70362
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PHLD_MOUSE
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Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D)
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MSAGRLWSSLLLLLPLFCSKSSSCGLSTHVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADLSWHNLGFLRTMGAIDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVLVDCTYLQFLEMHGEMFAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRNHTLSGSKVQKNDFHRNLTMFISRDIRKNLNYTERGVFYSTGSWARPESVTFMYQTLERNLRLMLAGSSQKNLNHVSSPSASYTLSVPYARLGWVMTSADLNQDGHGDLVVGAPGYSHPGRFQIGRVYIIYGNDLGLPPIDLDLNKEGILEGFQPSGRFGSALAVLDFNQDGLPDLAVGAPSVGSGQLTYNGSVYVYYGSQQGRLSSSPNVTISCKDTYCNLGWTLLATDADGDGRHDLVISSPFAPGGRKQKGIVATFYSHPRRNDKELLTLEEADWKVNGEEDFSWFGYSLHGVTVANRSLLLIGSPTWKNVSRMARSSHKKNQEEKSLGKVYGYFLPNRQSTITISGDKAMGKLGTSLSSGYVRVNGTLTQVLLVGAPTHDDVSKMAFLTMTLHQGGATRMYELAPEKTQPALLSTFSGDRRFSRFGSVLHLTDLDDDGLDEIIMAAPLRITDVTSGLLGGEDGRVYIYNGMYTTLGDMTGKCKSWMTPCPEEKAQYVLTSPEASSRFGSSLVSVRSKGRNQVVVAAGRSSWGARLSGALHVYSFSSD
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This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.
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O70370
|
CATS_MOUSE
|
Cathepsin S (EC 3.4.22.27)
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MRAPGHAAIRWLFWMPLVCSVAMEQLQRDPTLDYHWDLWKKTHEKEYKDKNEEEVRRLIWEKNLKFIMIHNLEYSMGMHTYQVGMNDMGDMTNEEILCRMGALRIPRQSPKTVTFRSYSNRTLPDTVDWREKGCVTEVKYQGSCGACWAFSAVGALEGQLKLKTGKLISLSAQNLVDCSNEEKYGNKGCGGGYMTEAFQYIIDNGGIEADASYPYKATDEKCHYNSKNRAATCSRYIQLPFGDEDALKEAVATKGPVSVGIDASHSSFFFYKSGVYDDPSCTGNVNHGVLVVGYGTLDGKDYWLVKNSWGLNFGDQGYIRMARNNKNHCGIASYCSYPEI
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Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
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O70372
|
TERT_MOUSE
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Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit)
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MTRAPRCPAVRSLLRSRYREVWPLATFVRRLGPEGRRLVQPGDPKIYRTLVAQCLVCMHWGSQPPPADLSFHQVSSLKELVARVVQRLCERNERNVLAFGFELLNEARGGPPMAFTSSVRSYLPNTVIETLRVSGAWMLLLSRVGDDLLVYLLAHCALYLLVPPSCAYQVCGSPLYQICATTDIWPSVSASYRPTRPVGRNFTNLRFLQQIKSSSRQEAPKPLALPSRGTKRHLSLTSTSVPSAKKARCYPVPRVEEGPHRQVLPTPSGKSWVPSPARSPEVPTAEKDLSSKGKVSDLSLSGSVCCKHKPSSTSLLSPPRQNAFQLRPFIETRHFLYSRGDGQERLNPSFLLSNLQPNLTGARRLVEIIFLGSRPRTSGPLCRTHRLSRRYWQMRPLFQQLLVNHAECQYVRLLRSHCRFRTANQQVTDALNTSPPHLMDLLRLHSSPWQVYGFLRACLCKVVSASLWGTRHNERRFFKNLKKFISLGKYGKLSLQELMWKMKVEDCHWLRSSPGKDRVPAAEHRLRERILATFLFWLMDTYVVQLLRSFFYITESTFQKNRLFFYRKSVWSKLQSIGVRQHLERVRLRELSQEEVRHHQDTWLAMPICRLRFIPKPNGLRPIVNMSYSMGTRALGRRKQAQHFTQRLKTLFSMLNYERTKHPHLMGSSVLGMNDIYRTWRAFVLRVRALDQTPRMYFVKADVTGAYDAIPQGKLVEVVANMIRHSESTYCIRQYAVVRRDSQGQVHKSFRRQVTTLSDLQPYMGQFLKHLQDSDASALRNSVVIEQSISMNESSSSLFDFFLHFLRHSVVKIGDRCYTQCQGIPQGSSLSTLLCSLCFGDMENKLFAEVQRDGLLLRFVDDFLLVTPHLDQAKTFLSTLVHGVPEYGCMINLQKTVVNFPVEPGTLGGAAPYQLPAHCLFPWCGLLLDTQTLEVFCDYSGYAQTSIKTSLTFQSVFKAGKTMRNKLLSVLRLKCHGLFLDLQVNSLQTVCINIYKIFLLQAYRFHACVIQLPFDQRVRKNLTFFLGIISSQASCCYAILKVKNPGMTLKASGSFPPEAAHWLCYQAFLLKLAAHSVIYKCLLGPLRTAQKLLCRKLPEATMTILKAAADPALSTDFQTILD
|
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:17130244, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:9582020}.
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O70373
|
XIRP1_MOUSE
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Xin actin-binding repeat-containing protein 1 (Cardiomyopathy-associated protein 1)
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MADAQMQVAPTPTIQMRTEEDLSLPHPSAPEGLPPPPPKETFSKFQQQRQASELRRLYKHIHPELRKNLEEAVAEDLAEVLGSEEPTEGDVQCMRWIFENWRLDAIGDHERPAAREPVSGGNVQATSRKFEEGSFTNSSDQEPEGLRPSGGDVQAARQMFETKPLDALRGQEEATQTTMREPAATGDVQGTRKLFETRPLDRLGSRPSIQEQSPLELRSEIQELKGDVKKTVKLFQTEPLCAIQDAEGTIHEVKAACREEIQSNAVRSARWLFETRPLDAFNQDPSQVRVIRGISLEEGALPDVSATRWIFETQPLDAIREIEVDEKDFQPSPDLIPPGPDVQHQRHLFETCSLDTLKGERETEAEVPPKEEVIPGDVRSTLWLFETKPLDAFRDQVQVGHLQRVGHQEGEGLVTECLPSNGTSVLPLSQGVPQNDGLKGDVKTFKNLFETLPLDSIGQGEPSAYGNINRGQNTDSAEQSQGSDAPVYAMQDSRGQLHALTSVSREQVVGGDVQGYKWMFETQPLDTLGRSPSTIDVVRGITRQEVVAGDVGTTRWLFETQPLEMIHQQEQQKPEEEEGKGPGGPPPELPKKGDVQTIRWLFETYPMSELAEKRESEVTDPVSKAETQSCTWMFGPQSLNPAEGSGEQHLQTSQVPAGDRQTDRHVFETESLPASNQSSGRKPVRYCSRVEIPSGQVSRQKEVFQALEAGKKEVPETTINLGSIPTGSVHKFTWLFENCPMGSLAAESIRGDNLQEEQPKGSAGHGTPERQETAAERTLRTLHATPGILHHGGILMEARGPGELCLAKYVLPSPGQGRPYIRKEELVCGELPRIVRQVLRRTDVDQQGLLVQEDTAGQLQLHPLMLPGPGDPGNIEDMDPELQQLLACGLGVSVSKTGLVMQETGQGLVALTAYSLQPQLTSRAPERSSVQLLASCIDKGDLHSLHSLRWEPPTDPSSGPATEESQRVPPTESIIHVTPLDSTMEMGQLRISGSTPCPPPSRAAGKVVLPNGKPVAQAPLQEARKKRDISHAGQKGKAASGRPEASPLGSGAPDLQEAMQNLRLATAEAQSLHQQVLSRHPQGSDPVATSMPVQDVLQASTPATGVTQGSIRPVAGSEARIPAVPRKLL
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Protects actin filaments from depolymerization.
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O70374
|
MTG8R_MOUSE
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Protein CBFA2T2 (MTG8-like protein) (MTG8-related protein 1)
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MVGVPGAAAFQLGCEKRVPAMPGSPVEVKIQSRSSPPIMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERRDENNFERDTVPPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRERHHNLSLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRFNENTELRKTGTELVSRQHSPGSTDSLSNDSQREFTSRPATGYVPVEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAEDAFLVINEQEESTENCWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLCGQSLHGHSPHSQSRPLLPGGRGSARSADCSVPSPALDKTSATTSRSSTPASVTAIDANGL
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Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency. Involved in primordial germ cell (PCG) formation. Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent mannerCan repress the expression of MMP7 in a ZBTB33-dependent manner (By similarity). Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes. Required for the maintenance of the secretory cell lineage in the small intestine. Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation.
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O70377
|
SNP23_RAT
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Synaptosomal-associated protein 23 (SNAP-23) (Vesicle-membrane fusion protein SNAP-23)
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MDDLSPEEIQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCVCPCNRTKNFESGKNYKATWGDGGDSSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
|
Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
|
O70394
|
I27RA_MOUSE
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Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1)
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MNRLRVARLTPLELLLSLMSLLLGTRPHGSPGPLQCYSVGPLGILNCSWEPLGDLETPPVLYHQSQKYHPNRVWEVKVPSKQSWVTIPREQFTMADKLLIWGTQKGRPLWSSVSVNLETQMKPDTPQIFSQVDISEEATLEATVQWAPPVWPPQKVLICQFRYKECQAETWTRLEPQLKTDGLTPVEMQNLEPGTCYQVSGRCQVENGYPWGEWSSPLSFQTPFLDPEDVWVSGTVCETSGKRAALLVWKDPRPCVQVTYTVWFGAGDITTTQEEVPCCKSPVPAWMEWAVVSPGNSTSWVPPTNLSLVCLAPESAPCDVGVSSADGSPGIKVTWKQGTRKPLEYVVDWAQDGDSLDKLNWTRLPPGNLSTLLPGEFKGGVPYRITVTAVYSGGLAAAPSVWGFREELVPLAGPAVWRLPDDPPGTPVVAWGEVPRHQLRGQATHYTFCIQSRGLSTVCRNVSSQTQTATLPNLHLGSFKLWVTVSTVAGQGPPGPNLSLHLPDNRIRWKALPWFLSLWGLLLMGCGLSLASTRCLQARCLHWRHKLLPQWIWERVPDPANSNSGQPYIKEVSLPQPPKDGPILEVEEVELQPVVESPKASAPIYSGYEKHFLPTPEELGLLV
|
Receptor for IL27. Requires IL6ST/GP130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms.
|
O70400
|
PDLI1_MOUSE
|
PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1) (Elfin) (LIM domain protein CLP-36)
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MTTQQIVLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAAIANLCIGDLITAIDGEDTSSMTHLEAQNKIKGCADNMTLTVSRSEQKIWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPAPSTRVITNQYNSPTGLYSSENISNFNNAVESKTSASGEEANSRPVVQPHPSGSLIIDKDSEVYKMLQEKQELNEPPKQSTSFLVLQEILESDGKGDPNKPSGFRSVKAPVTKVAASVGNAQKLPICDKCGTGIVGVFVKLRDHHRHPECYVCTDCGINLKQKGHFFVEDQIYCEKHARERVTPPEGYDVVTVFRE
|
Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (By similarity). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity).
|
O70404
|
VAMP8_MOUSE
|
Vesicle-associated membrane protein 8 (VAMP-8) (Endobrevin) (Edb)
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MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT
|
SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells. Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity).
|
O70405
|
ULK1_MOUSE
|
Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Serine/threonine-protein kinase Unc51.1) (Unc-51-like kinase 1)
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MEPGRGGVETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHTMRTLSEDTVRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPGGRRANPSNIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPAIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASTPIKKSPPVPVPSYPSSGSGSSSSSSSASHLASPPSLGEMPQLQKTLTSPADAAGFLQGSRDSGGSSKDSCDTDDFVMVPAQFPGDLVAEAASAKPPPDSLLCSGSSLVASAGLESHGRTPSPSPTCSSSPSPSGRPGPFSSNRYGASVPIPVPTQVHNYQRIEQNLQSPTQQQTARSSAIRRSGSTTPLGFGRASPSPPSHTDGAMLARKLSLGGGRPYTPSPQVGTIPERPSWSRVPSPQGADVRVGRSPRPGSSVPEHSPRTTGLGCRLHSAPNLSDFHVVRPKLPKPPTDPLGATFSPPQTSAPQPCPGLQSCRPLRGSPKLPDFLQRSPLPPILGSPTKAGPSFDFPKTPSSQNLLTLLARQGVVMTPPRNRTLPDLSEASPFHGQQLGSGLRPAEDTRGPFGRSFSTSRITDLLLKAAFGTQASDSGSTDSLQEKPMEIAPSAGFGGTLHPGARGGGASSPAPVVFTVGSPPSGATPPQSTRTRMFSVGSSSSLGSTGSSSARHLVPGACGEAPELSAPGHCCSLADPLAANLEGAVTFEAPDLPEETLMEQEHTETLHSLRFTLAFAQQVLEIAALKGSASEAAGGPEYQLQESVVADQISQLSREWGFAEQLVLYLKVAELLSSGLQTAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDGIHGVTAERLILSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHTLTDQADIENIAKCKLCIERRLSALLSGVYA
|
Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation (By similarity). May also phosphorylate SESN2 and SQSTM1 to regulate autophagy. Phosphorylates FLCN, promoting autophagy (By similarity). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (By similarity). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (By similarity).
|
O70418
|
RN112_RAT
|
RING finger protein 112 (EC 2.3.2.27) (Brain finger protein) (Zinc finger protein 179)
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MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWSHASFPKLELGLGQRPSPPRESPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQKKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLRGLPGLESGDSTRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSRETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHHNKSGQGHVGDILQKLSGKYPKVQELLLGKRARCYLLPAPERQWVNKGQASPGGNTEDDFSHHFRAYISDVLSTAPQHAKSRCQGYWSEGRAMARGDRRLLTGQQLAQEIKNLSGWMGKSGPSFSSPDEMAAQLHDLRKVEAAKKEFEEYVRQQDIATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKEREQTLEALEAELQAEAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERVQGGDREPLLQEE
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E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins. Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage. Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density.
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O70421
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FZD1_MOUSE
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Frizzled-1 (Fz-1) (mFz1)
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MAEEAAPSESRAAGRLSLELCAEALPGRREEVGHEDTASHRRPRADPRRWASGLLLLLWLLEAPLLLGVRAQAAGQVSGPGQQAPPPPQPQQSGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGTVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV
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Receptor for Wnt proteins. Activated by WNT7B. Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity). Contradictory results showing activation by WNT7B have been described for mouse. Functions in the canonical Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable).
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O70423
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AOC3_MOUSE
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Membrane primary amine oxidase (EC 1.4.3.21) (Copper amine oxidase) (Semicarbazide-sensitive amine oxidase) (SSAO) (Vascular adhesion protein 1) (VAP-1)
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MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGGLSQPLHCPSVLPSVQPRTHPSQSQPFADLSPEELTAVMSFLTKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLDREYQDIEEMIFHRELPQASGLLHHCCFYKHQGQNLLTMTTAPRGLQSGDRATWFGLYYNLSGAGFYPHPIGLELLIDHKALDPALWTIQKVFYQGRYYESLTQLEDQFEAGLVNVVLVPNNGTGGSWSLKSSVPPGPAPPLQFHPQGPRFSVQGSQVSSSLWAFSFGLGAFSGPRIFDIRFQGERVAYEISVQEAIALYGGNSPASMSTCYVDGSFGIGKYSTPLIRGVDCPYLATYVDWHFLLESQAPKTLRDAFCVFEQNQGLPLRRHHSDFYSHYFGGVVGTVLVVRSVSTLLNYDYIWDMVFHPNGAIEVKFHATGYISSAFFFGAGEKFGNRVGAHTLGTVHTHSAHFKVDLDVAGLKNWAWAEDMAFVPTIVPWQPEYQMQRLQVTRKLLETEEEAAFPLGGATPRYLYLASNHSNKWGHRRGYRIQILSFAGKPLPQESPIEKAFTWGRYHLAVTQRKEEEPSSSSIFNQNDPWTPTVNFTDFISNETIAGEDLVAWVTAGFLHIPHAEDIPNTVTAGNSVGFFLRPYNFFDEDPSFHSADSIYFREGQDATACEVNPLACLSQTATCAPEIPAFSHGGFAYRDN
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Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis (By similarity).
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O70433
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FHL2_MOUSE
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Four and a half LIM domains protein 2 (FHL-2) (Skeletal muscle LIM-protein 3) (SLIM-3)
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MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYREQPWHKECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
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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.
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O70435
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PSA3_MOUSE
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Proteasome subunit alpha type-3 (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K)
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MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSANDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
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Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
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O70436
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SMAD2_RAT
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Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (SMAD family member 2) (SMAD 2) (Smad2)
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MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFSLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
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Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).
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O70437
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SMAD4_RAT
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Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
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MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPSESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD
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Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site required for synergistic transcriptional activity in response to TGF-beta. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8 (By similarity).
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O70439
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STX7_MOUSE
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Syntaxin-7
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MSYTPGIGGDSAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQRKSRKTLCIIIFILVVRIVIICLIVWGLKG
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May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity).
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O70441
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SYN3_RAT
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Synapsin-3 (Synapsin III)
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MNFLRRRLSDSSFVANLPNGYMPDLQRPESSSSSPASPATERRHPQPLAASFSSPGSSLFSSFSSAMKQTPQAPTGLMEPPTPVTPVVQRPRILLVIDDAHTDWSKYFHGKKVNGDIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKIVRSFKPDFILVRQHAYSMALAEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMLTAPNFPVVIKLGHAHAGMGKIKVENQHDYQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKNGRDYIIEVMDSSMPLIGEHVEEDKQLMADLVVSKMSQLLVPGASVPSPLRPWGPQTKSAKSPGQGQLGPLLGQPQPRPPPQGGPRQAQSPQPPRSRSPSQQRLSPQGQQPVSPQSGSPQQQRSPGSPQLSRASGGSSPNQASKPTASLSSHTRPPVQGRSTSQQGEEPQKTASPHPHLNKSQSLTNSLSTSDTSHRGTPSEDEAKAETIRNLRKSFASLFSD
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May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed.
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O70443
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GNAZ_MOUSE
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Guanine nucleotide-binding protein G(z) subunit alpha (G(x) alpha chain) (Gz-alpha)
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MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGGFNLDACKEYKPLIIYNAIDSLTRIIRALAALKIDFHNPDRAYDAVQLFALTGPAESKGEITPELLGVMRRLWADPGAQACFGRSSEYHLEDNAAYYLNDLERIAAPDYIPTVEDILRSRDMTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQTSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLSVCFPEYKGQNTYEEAAVYIQRQFEDLNRNKETKEIYSHFTCATDTSNIQFVFDAVTDVIIQNNLKYIGLC
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Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
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O70444
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PIM3_RAT
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Serine/threonine-protein kinase pim-3 (EC 2.7.11.1) (Kinase induced by depolarization) (Protein kinase Kid-1)
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MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKVYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGMAVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHNCGVVHRDIKDENLLVDLRSGELKLIDFGSGAVLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLFFRRRVSPECQQLIEWCLSLRPSERPSLDQIAAHPWMLGTEGSVPENCDLRLCALDTDDGASTTSSSESL
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Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression and protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth (By similarity).
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O70445
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BARD1_MOUSE
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BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1)
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MPRRPPRVCSGNQPAPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHDNKDSKDNTSRASLFGDAERKKNSIKMWFSPRSKKVRYVVTKVSVQTQPQKAKDDKAQEASMYEFVSATPPVAVPKSAKTASRTSAKKHPKKSVAKINREENLRPETKDSRFDSKEELKEEKVVSCSQIPVMERPRVNGEIDLLASGSVVEPECSGSLTEVSLPLAEHIVSPDTVSKNEETPEKKVCVKDLRSGGSNGNRKGCHRPTTSTSDSCGSNIPSTSRGIGEPALLAENVVLVDCSSLPSGQLQVDVTLRRKSNASDDPLSLSPGTPPPLLNNSTHRQMMSSPSTVKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAVNIFGVRPVDYTDNENIRSLLLLPEENESFSTSQCSIVNTGQRKNGPLVFIGSGLSSQQQKMLSKLETVLKAKKCMEFDSTVTHVIVPDEEAQSTLKCMLGILSGCWILKFDWVKACLDSKVREQEEKYEVPGGPQRSRLNREQLLPKLFDGCYFFLGGNFKHHPRDDLLKLIAAAGGKVLSRKPKPDSDVTQTINTVAYHAKPESDQRFCTQYIVYEDLFNCHPERVRQGKVWMAPSTWLISCIMAFELLPLDS
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E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
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O70451
|
MOT2_MOUSE
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Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7)
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MPSEPSAPLPQPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFKDIQEIFNTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCIGMILASYSNSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRRRPLANGCAMAGSPVFLSTLAPFNQYLFNNYGWKGSFLILGGIFLHSCVAGCLMRPVGPSPNTKKSKSKVGSRHDSTLKKASKVSTAQKVNRFLDFSLFMHRGFLIYLSGNVILFLGIFAPIIFLAQYAKHIGVDDYNSAFLLSVMAFIDMFARPSVGLIANTSLIRPRIQYLFSSAIIFTGICHLLCPLATTYSALVVYVVFFGLGFGSISSLLFECLMDIVGATRFSSAVGLTTIVECCPVLFGPPLAGKLLDITGEYKYLYIASGTVVLVSGTYLLIGNAINYRLLDKERKREKAKKKKSASHASREMEALNRSKQDEVTVKASNAHNPPSDRDKESNI
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Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity).
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O70456
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1433S_MOUSE
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14-3-3 protein sigma (Stratifin)
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MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVKEYREKVETELRGVCDTVLGLLDSHLIKGAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADSAGEEGGEAPEEPQS
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Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.
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O70458
|
OSMR_MOUSE
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Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
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MAFSVVLHPAFLLAVLSLRASRSEVLEEPLPLTPEIHKVSFQLKLQEVNLEWTVPALTHEELNMIFQIEISRLNISNTIWVENYSTTVKREEAVRWNWTSDIPLECVKHFIRIRALVDDTKSLPQSSWGNWSSWKEVNAKVSVEPDKSLIFPKDKVLEEGSNVTICLMYGQNVYNVSCKLQDEPIHGEQLDSHVSLLKLNNVVFLSDTGTNINCQATKGPKRIFGTVLFVSKVLEEPKNVSCETRDFKTLDCSWEPGVDTTLTWRKQRFQNYTLCESFSKRCEVSNYRNSYTWQITEGSQEMYNFTLTAENQLRKRSVNINFNLTHRVHPKAPQDVTLKIIGATKANMTWKVHSHGNNYTLLCQVKLQYGEVIHEHNVSVHMSANYLFSDLDPDTKYKAFVRCASANHFWKWSDWTQKEFSTPETAPSQALDVWRQVWSENGRRIVTLFWKPLLKSQANGKIISYNIVVENEAKPTESEHYCVWAPALSTNLSLDLQPYKIRITTNNSMGASPESLMVLSNDSGHEEVKEKTIKGIKDAFNISWEPVSGDTMGYVVDWCAHSQDQRCDLQWKNLGPNTTSTTITSDDFKPGVRYNFRIFERSVEHKARLVEKQRGYTQELAPLVNPKVEIPYSTPNSFVLRWPDYDSDFQAGFIKGYLVYVKSKEMQCNQPWERTLLPDNSVLCKYDINGSETKTLTVENLQPESLYEFFVTPYTSAGPGPNETFTKVTTPDARSHMLLQIILPMTLCVLLSIIVCYWKSQWVKEKCYPDIPNPYKSSILSLIKSKKNPHLIMNVKDCIPDVLEVINKAEGSKTQCVGSGKLHIEDVPTKPPIVPTEKDSSGPVPCIFFENFTYDQSAFDSGSHGLIPGPLKDTAHQLGLLAPPNKFQNVLKNDYMKPLVESPTEETSLIYVSQLASPMCGDKDTLATEPPVPVHGSEYKRQMVVPGSLASPSLKEDNSLTSTVLLGQGEQ
|
Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5 (By similarity). Capable of transducing OSM-specific signaling events (By similarity).
|
O70460
|
CCL19_MOUSE
|
C-C motif chemokine 19 (Epstein-Barr virus-induced molecule 1 ligand chemokine) (EBI1 ligand chemokine) (ELC) (Small-inducible cytokine A19)
|
MAPRVTPLLAFSLLVLWTFPAPTLGGANDAEDCCLSVTQRPIPGNIVKAFRYLLNEDGCRVPAVVFTTLRGYQLCAPPDQPWVDRIIRRLKKSSAKNKGNSTRRSPVS
|
Strongly chemotactic for naive (L-selectinhi) CD4 T-cells and for CD8 T-cells and weakly attractive for resting B-cells and memory (L-selectinlo) CD4 T-cells. May play a role in promoting encounters between recirculating T-cells and dendritic cells and in the migration of activated B-cells into the T-zone of secondary lymphoid tissues. Binds to chemokine receptor CCR7. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
|
O70467
|
ANM3_RAT
|
Protein arginine N-methyltransferase 3 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3)
|
MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ
|
Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases. May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
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O70468
|
MYPC3_MOUSE
|
Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform)
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MPEPGKKPVSAFNKKPRSAEVTAGSAAVFEAETERSGVMVRWQRDGSDITANDKYGLAAEGKRHTLTVRDASPDDQGSYAVIAGSSKVKFDLKVTEPAPPEKAESEVAPGAPEEVPAPATELEESVSSPEGSVSVTQDGSAAEHQGAPDDPIGLFLMRPQDGEVTVGGSIVFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQTTSAGGYRCEVSTKDKFDSCNFNLTVHEAIGSGDLDLRSAFRRTSLAGAGRRTSDSHEDAGTPDFSSLLKKRDSFRRDSKLEAPAEEDVWEILRQAPPSEYERIAFQHGVEACHRPLKRLKGMKQDEKKSTAFQKKLEPAYQVNKGHKIRLTVELADPDAEVKWLKNGQEIQMSGSKYIFESVGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRSLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGRKHHLIINEATLEDAGHYAVRTSGGQSLAELIVQEKKLEVYQSIADLAVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDNRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGSTPDTIVVVTGNKLRLDVPISGDPAPTVVWQKTVTQGKKASAGPHPDAPEDAGADEEWVFDKKLLCETEGRVRVETTKDRSVFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCTVQWEPPAYDGGQPVLGYILERKKKKSYRWMRLNFDLLRELSHEARRMIEGVAYEMRVYAVNAVGMSRPSPASQPFMPIGPPGEPTHLAVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCQEGCSEWTPALQGLTERRSMLVKDLPTGARLLFRVRAHNVAGPGGPIVTKEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAARRTHSGTYQVTVRIENMEDKATLILQIVDKPSPPQDIRIVETWGFNVALEWKPPQDDGNTEIWGYTVQKADKKTMEWFTVLEHYRRTHCVVSELIIGNGYYFRVFSHNMVGSSDKAAATKEPVFIPRPGITYEPPKYKALDFSEAPSFTQPLANRSIIAGYNAILCCAVRGSPKPKISWFKNGLDLGEDARFRMFCKQGVLTLEIRKPCPYDGGVYVCRATNLQGEAQCECRLEVRVPQ
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Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
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O70469
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DOK2_MOUSE
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Docking protein 2 (Dok-related protein) (Dok-R) (Downstream of tyrosine kinase 2) (IL-four receptor-interacting protein) (FRIP) (p56(dok-2))
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MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPYSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFRGLLTGPPPHLPDPLYDSIQEDPGAPLPDHIYDEPEGVAALSLYDRTQRPSGETWREQATADGGPSSLQQDSSVPDWPQATEYDNVILKKGPK
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DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation.
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O70473
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AK1A1_CRIGR
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Aldo-keto reductase family 1 member A1 (EC 1.1.1.2) (EC 1.1.1.33) (EC 1.1.1.372) (EC 1.1.1.54) (Alcohol dehydrogenase [NADP(+)]) (Aldehyde reductase) (Glucuronate reductase) (EC 1.1.1.19) (Glucuronolactone reductase) (EC 1.1.1.20)
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MASCVLLHTGQKMPLIGLGTWKSNPGQVKAAIKYALSVGYRHIDCAAVYGNEIEIGEALKENVGPGKAVPREELFVTSKLWNTKHHPEDVEAALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNDDGTIRYDSTHYKETWKALEALVAKGLVKALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVVCIPKSITPSRILQNIQVFDFTFSPEEMKQLDALNKHWRYIVPMITVDGKSVPRDAGHPLYPFNDPY
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Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity). Plays an important role by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone. Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (By similarity).
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O70475
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UGDH_MOUSE
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UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22)
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MVEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQKAVRALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQVSRLVTISKDPYEACDGAHALVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHSELQTIGFQIETIGKKVSSKRIPYTPGEIPKFSLQDPPNKKPKV
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Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans. Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans. Required for proper brain and neuronal development (By similarity).
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O70477
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PKNX1_MOUSE
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Homeobox protein PKNOX1 (PBX/knotted homeobox 1)
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MMATQTLSIDSYQDGQQMQVVTELKTEQDPNCSDPDAEGVSPPPIESQTPMDADKQAIYRHPLFPLLALLFEKCEQSTQGSEGTTSASFDVDIENFVRKQEKDGKPFFCEDPETDNLMVKAIQVLRIHLLELEKVNELCKDFCSRYIACLKTKMNSETLLSGEPGSPYSPVQSQQIQSAITGTLSPQGIVVPASALQQGNVTMATVAGGTVYQPVTVVTPQGQVVTQALSPGTIRIQNSQLQLQLNQDLSILHQEDGSSKNKRGVLPKHATNVMRSWLFQHIGHPYPTEDEKKQIAAQTNLTLLQVNNWFINARRRILQPMLDSSCSETPKTKKKPAQNRPVQRFWPDSLASGVAQATPSELAMSEGAVVTITTPVNMNVDSLQSLSSDGATLAVQQVMMAGQSEDESVDSTEDEGGALAPTHISGLVLENSDSLQ
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Activates transcription in the presence of PBX1A and HOXA1. (Microbial infection) In complex with PBX1, binds to the 5'-TGATTGAC-3' consensus sequence in the U5 region of Moloney murine leukemia virus and promotes viral transcription.
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O70480
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VAMP4_MOUSE
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Vesicle-associated membrane protein 4 (VAMP-4)
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MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALAAAILLLMIIILIVVKFRT
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Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule (By similarity).
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O70481
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UBR1_MOUSE
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E3 ubiquitin-protein ligase UBR1 (EC 2.3.2.27) (N-recognin-1) (RING-type E3 ubiquitin transferase UBR1) (Ubiquitin-protein ligase E3-alpha-1) (Ubiquitin-protein ligase E3-alpha-I)
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MADEEMDGAERMDVSPEPPLAPQRPASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSILTPLEWYLFGEDPDICLEKLKHSGAFQLCGKVFKSGETTYSCRDCAIDPTCVLCMDCFQSSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVDHEPGRAGTTKESLHCPLNEEVIAQARRIFPSVIKYIVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGVYATCQEAKEDIKSHSENVSQHPLHVEVLHSVVMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLVEEPGSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHERSISITALSVQMLTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPVIWTERLRAQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEDLLLVAYKECHKAVMRCSTNFMSSTKTVVQLCGHSLETKSYKVSEDLVSIHLPLSRTLAGLHVRLSRLGAISRLHEFVPFDGFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASIMDPNKFLLLVLQRYELTDAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTREEVIMREITHLLCIEPMPHSAIARNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVVNLLSCDVMMYILRTIFERAVDMESNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVAFDFYHKASRLGSSAMNAQNIQMLLEKLKGIPQLESQKDMITWILQMFDTVKRLREKSCLVVATTSGLECVKSEEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEVTGKEDSIMEEESTSAVSEASRIALGPKRGPAVTEKEVLTCILCQEEQEVKLENNAMVLSACVQKSTALTQHRGKPVDHLGETLDPLFMDPDLAHGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENAEALAQLLTLARWIQTVLARISGYNIKHAKGEAPAVPVLFNQGMGDSTFEFHSILSFGVQSSVKYSNSIKEMVILFATTIYRIGLKVPPDELDPRVPMMTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRTTCPQVLIHKHLARLLSVILPNLQSENTPGLLSVDLFHVLVGAVLAFPSLYWDDTVDLQPSPLSSSYNHLYLFHLITMAHMLQILLTTDTDLSSGPPLAEGEEDSEEARCASAFFVEVSQHTDGLAGCGAPGWYLWLSLRNGITPYLRCAALLFHYLLGVAPPEELFANSAEGEFSALCSYLSLPTNLFLLFQEYWDTIRPLLQRWCGDPALLKSLKQKSAVVRYPRKRNSLIELPEDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACVFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL
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E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11689692, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:16311597}.
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O70490
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ACSM2_RAT
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Acyl-coenzyme A synthetase ACSM2, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 2) (Butyryl-coenzyme A synthetase 2) (Kidney-specific protein KS) (Middle-chain acyl-CoA synthetase 2)
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MHWLWKIPRLCTFWGTEMFHRTFHMNIKKLMPIQWGHQEVPAKFNFASDVIDHWASLEKAGKRSPGPALWWMNGSGEELKWNFRELSEISKQTANVLTGACGLQRGDRVAVVLPRVPEWWLVTLGCMRSGLVFMPGTTQMKSTDILYRLQSSKARAIVAGDEVVQEVDAVAPDCSFLKIKLLVSEKNREGWLNFKALLKDASPIHQCVETVSQESAAIYFTSGTSGPPKMAEHSHCSLGLKAKMDAGWTGLGPSDTMWTISDTGWILNILGSFLEPWVLGTCIFVHLLPKFDPQTVLKVLSSYPINTLLGAPLIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLESWKAKTGLEIREIYGQTETGITCRVSRTMKVKPGYLGTAIVPYDVQVIDEQGNVLPPGKEGDMALRVKPIRPIGMFSGYVDNPKKTQANIRGDFWLLGDRGIKDTEGYFHFMGRTDDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPIRREVVKAFVVLAPEFLSHDQDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTITGKIERAKLRAKEWKTSG
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Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (By similarity). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (By similarity).
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O70491
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STRA6_MOUSE
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Receptor for retinol uptake STRA6 (Retinoic acid-responsive protein) (Retinol-binding protein receptor STRA6) (Stimulated by retinoic acid gene 6 protein)
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MESQASENGSQTSSGVTDDYSSWYIEEPLGAEEVQPEGVIPLCQLTAPPALLHACLASLSFLVLLLLALLVRRRRLWPRCGHRGLGLPSPVDFLAGDLSWTVPAAVFVVLFSNLCLLLPDENPLPFLNLTAASSPDGEMETSRGPWKLLALLYYPALYYPLAACASAGHQAAFLLGTVLSWAHFGVQVWQKAECPQDPKIYKHYSLLASLPLLLGLGFLSLWYPVQLVQSLRHRTGAGSQGLQTSYSEKYLRTLLCPKKLDSCSHPASKRSLLSRAWAFSHHSIYTPQPGFRLPLKLVISATLTGTATYQVALLLLVSVVPTVQKVRAGINTDVSYLLAGFGIVLSEDRQEVVELVKHHLWTVEACYISALVLSCASTFLLLIRSLRTHRANLQALHRGAALDLDPPLQSIHPSRQAIVSWMSFCAYQTAFSCLGLLVQQVIFFLGTTSLAFLVFVPLLHGRNLLLLRSLESTWPFWLTVALAVILQNIAANWIFLRTHHGYPELTNRRMLCVATFLLFPINMLVGAIMAVWRVLISSLYNTVHLGQMDLSLLPQRAASLDPGYHTYQNFLRIEASQSHPGVIAFCALLLHAPSPQPRPPLAPQDSLRPAEEEEGMQLLQTKDLMAKGAGHKGSQSRARWGLAYTLLHNPSLQAFRKAALTSAKANGTQP
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Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A (By similarity). Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin. Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid and 11-cis-retinal. STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency. Does not transport retinoic acid (By similarity).
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O70492
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SNX3_MOUSE
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Sorting nexin-3 (SDP3 protein)
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MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRHVPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
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Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC). May act in part as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (By similarity). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G. Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (By similarity). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor Tfrc presuambly by delivering the transferrin:transferrin receptor complex to recycling endosomes the function may involve the CSC retromer subcomplex. Involved in regulation of neurite outgrowth in primary neurons.
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O70494
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SP3_MOUSE
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Transcription factor Sp3
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MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDVNETNADTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTTSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQDSQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGALTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKVIHSSSTVLASVEAGRDDALITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME
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Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping (By similarity). {ECO:0000250, ECO:0000269|PubMed:15554904}.
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O70496
|
CLCN7_MOUSE
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H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7)
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MANVSKKVSWSGRDRDDEEGAPLLRRTGQPDEETPLLNGAGPGARQSHSALFRIGQMNNVELDDELLDPEVDPPHTFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKDNIDKFTEKGGLSFSLLLWATLNSAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGILGAVFNALNYWLTMFRIRYIHRPCLQVIEAMLVAAVTATVAFVLIYSSRDCQPLQGSSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPMTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGIIVDVLSDTASNHNGFPVVEDVGDTQPARLQGLILRSQLIVLLKHKVFVERSNMGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNHNQVVGLVTRKDLARYRLGKGGLEELSLAQT
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Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).
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O70497
|
FCN2_MOUSE
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Ficolin-2 (Collagen/fibrinogen domain-containing protein 2) (Ficolin-B) (Ficolin-beta) (L-ficolin)
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MALGSAALFVLTLTVHAAGTCPELKVLDLEGYKQLTILQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPSQSCATGPRTCKELLTQGHFLTGWYTIYLPDCRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNIHALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMGYHGAWWYSQCHTSNLNGLYLRGPHKSYANGVNWKSWRGYNYSCKVSEMKVRLI
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May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin (By similarity).
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O70503
|
DHB12_MOUSE
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Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (KIK-I)
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MECAPPAAGFLYWVGASTIAYLALRASYSLFRAFQVWCVGNEALVGPRLGEWAVVTGGTDGIGKAYAEELAKRGMKIVLISRSQDKLNQVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSVCKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTIYSATKAFVDFFSQCLHEEYKSKGIFVQSVMPYLVATKLAKIQKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHSLMGSINSIMPRWMYFKIIMGFSKSLRNRYLKKRKKN
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Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation.
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O70507
|
HCN4_MOUSE
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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (Brain cyclic nucleotide-gated channel 3) (BCNG-3)
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MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDGEEEGAGGRQDPSRRSIRLRPLPSPSPSVAAGCSESRGAALGATESEGPGRSAGKSSTNGDCRRFRGSLASLGSRGGGSGGAGGGSSLGHLHDSAEERRLIAAEGDASPGEDRTPPGLATEPERPATAAQPAASPPPQQPPQPASASCEQPSADTAIKVEGGAAAIDHILPEAEVRLGQSGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFVVDFISSIPVEYIFLIVETRIDSEVYKTARAVRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPHDCWVSINGMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETRLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRKKNSILLHKVQHDLNSGVFNYQENEIIQQIVRHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGPGLGNLGAGQTPRHPRRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPPGLSPLLPSSSSSPPPGACGSPPAPTPSTSTAAAASTTGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPPPPLPGARGGLGLLEHFLPPPPSSRSPSSSPGQLGQPPGELSLGLAAGPSSTPETPPRPERPSFMAGASGGASPVAFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESVAAFSLYPRAGGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARAASSGGPPLTTAAPQREPGARSEPVRSKLPSNL
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Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih) (By similarity). May mediate responses to sour stimuli. {ECO:0000250, ECO:0000269|PubMed:11675786}.
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O70511
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ANK3_RAT
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Ankyrin-3 (ANK-3) (Ankyrin-G)
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MAHAASQLKKNRDLEINAEEETEKKKKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADIESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRAAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTLKVVTEEIMTTTTITEKHKMNVPETMNEVLDMSDDEVGKASAPEKLSDGEYISDGEEGEDAITGDTDKYLGPQDLKELGDDSLPAEGYVGFSLGARSASLRSFSSDRSYTLNRSSYARDSMMIEELLVPSKEQHLPFTREFDSDSLRHYSWAADTLDNVNLVSSPVHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLSELLNGMDEELDSPEELGTKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPEETVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPSLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLASQLYRELICVPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKAEKADRRQSFTSLALRKRYSYLTEPSMKTVERSSGTARSLPTTYSHKPFFSTRPYQSWTTTPITVPGPAKSGSLSSSPSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTISSPIRTVASPSPYNTQVASGTLGRVPTITEATPIKGVAPNSTLSSRTSPVTTAGSLLEKSSITMTPPASPKANITMYSSSLPFKSIITSAAPLISSPLKSVVSPTKSAADVISTAKAAMASTLSSPLKQMSGHAEVALVNGSVSPLKYPSSSALINGCKATATLQDKISTATNAVSSVVSAAPDTVEKALSTTTAMPFSPLRSYVSAAAPSAFQSLRAPSASALYNSLGPSVGVTTSSVTSSIITVPVYSVGNVLAEPALKKLPDSNSLTKSAAALLSPIKTLTTETRPQPHFNRTSSPVKSSLFLASSALKPSVPSSLSSSQEILKDVAEMKEDLMRMTAILQTDVPEEKPFQTDLPREGRIDDEEPFKIVEKVKEDLVKVSEILKKDVCVESKGPPKSPKSDKGHSPEDDWTEFSSEEIREARQAAASHAPSLPERVHGKANLTRVIDYLTNDIGSSSLTNLKYKFEEAKKEGEERQKRILKPAMALQEHKLKMPPASMRPSTSEKELCKMADSFFGTDAILESPDDFSQHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIPPVITETRTEVVHVIRSYEPSTGEIPQSQPEDPVSPKPPPTFMELEPKPTALSIKEKVKAFQMKASSEEEDHSRVLSKGMRVKEETHITTTTRMVYHSPPGSECASERIEETMSVHDIMKAFQSGRDPSKELAGLFEHKSAMSPDVAKSAAETSAQHAEKDNQMKPKLERIIEVHIEKGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETPSGSLESPAQARRITGGLLDRLDDSSDQVRDPITSYLTGEAGKFEANGNHAEVIPEAKAKAYFPESQNDIGKQSIKENLKPKTHGCGRAEEPVSPLTAYQKSLEETSKLVIEDAPKPCVPVGMKKMTRTPADGKARLNLQEEEGSARSEPKQGEGYKVKTKKEIRNVEKKAH
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Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:G5E8K5}.
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O70514
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FGFP1_MOUSE
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Fibroblast growth factor-binding protein 1 (FGF-BP) (FGF-BP1) (FGF-binding protein 1) (FGFBP-1)
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MRLHSLILLSFLLLATQAFSEKVRKRAKNAPHSTAEEGVEGSAPSLGKAQNKQRSRTSKSLTHGKFVTKDQATCRWAVTEEEQGISLKVQCTQADQEFSCVFAGDPTDCLKHDKDQIYWKQVARTLRKQKNICRNAKSVLKTRVCRKRFPESNLKLVNPNARGNTKPRKEKAEVSAREHNKVQEAVSTEPNRVKEDITLNPAATQTMAIRDPECLEDPDVLNQRKTALEFCGESWSSICTFFLNMLQATSC
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Acts as a carrier protein that releases fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhances the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity).
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O70521
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RGS19_RAT
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Regulator of G-protein signaling 19 (RGS19) (G-alpha-interacting protein) (GAIP)
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MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPEEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKTEADRHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
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Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity).
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O70523
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FXR1_CRIGR
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RNA-binding protein FXR1
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MADVTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESAEAVKKARGFMEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRETRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDEIPNVPRTPGEEKTKNLKEESTQEAAVLNGVS
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mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis. Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors. Required to activate translation of stored mRNAs during late spermatogenesis: acts by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules that recruit translation initiation factor EIF4G3 to activate translation of stored mRNAs in late spermatids (By similarity). Promotes translation of MYC transcripts by recruiting the eIF4F complex to the translation start site. Acts as a negative regulator of inflammation in response to IL19 by promoting destabilization of pro-inflammatory transcripts (By similarity). Also acts as an inhibitor of inflammation by binding to TNF mRNA, decreasing TNF protein production. Acts as a negative regulator of AMPA receptor GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting its translation. Regulates proliferation of adult neural stem cells by binding to CDKN1A mRNA and promoting its expression. Acts as a regulator of sleep and synaptic homeostasis by regulating translation of transcripts in neurons. Required for embryonic and postnatal development of muscle tissue by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules (By similarity). Involved in the nuclear pore complex localization to the nuclear envelope by preventing cytoplasmic aggregation of nucleoporins: acts by preventing ectopic phase separation of nucleoporins in the cytoplasm via a microtubule-dependent mechanism (By similarity).
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O70525
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PEX5_CAVPO
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Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1)
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MAMRELVEGECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASETVSKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGAATTDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESVAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQPFEEGLLRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRCTPAYAHLVTPAEEGAGGAGLGSSKRILGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYRAADARDLSALLALFGLSQ
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Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity). [Isoform 1]: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5.
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O70531
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S26A2_RAT
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Sulfate transporter (Diastrophic dysplasia protein homolog) (Solute carrier family 26 member 2)
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MSSENKEQHNLSPRDLPEEAYGFPPELPLGAQRGSSTDLRQFEPSDRRRAFRRIHMELHEKPDTNIRQLVMRKLQKSCQCNATKIRNRIFDFFPVLRWLPKYDLKKNILGDMMSGLIVGILLVPQSIAYSLLAGQEPIYGLYTSFFASIIYFLFGTSRHISVGIFGILCLMIGEVVDRELHKACPDIDTTSSSIAMFSNGCVVVNHTLDGLCDKSCYAIKIGSTVTFMAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLSLPRSNGVGSVITTWIHIFRNIHKTNICDLITSLLCLLVLVPTKELNEYFKSKLPAPIPTELIVVVAATLASHFGKLNENYNSSIAGQIPTGFMPPQAPDWSLIPNVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCITTSAALAKTLVKESTGCQTQLSAIVTSLVLLLVLLLIAPLFYSLQKCVLGVITIVNLRGALLKFRDLPKMWRLSRMDTVIWFVTMLSSALLSTEIGLLVGVCFSMFCVILRTQMPKISLLGLEEESEIFESISTYKNLRSKSGIKVFRFIAPLYYINKECFKSALYKKTLNPVLVKAAWKKAAKRKLKEETVTFHGDPDEVSMQLSHDPLELHTVVIDCSAIQFLDTAGIHTLKEVRRDYEAIGIQVLLAQCNPSVRDSLAKGEYCKKEEENLLFYSLSEAVAFAEESQKEKGVCVVNGLSLSGD
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Sulfate transporter which mediates sulfate uptake into chondrocytes in order to maintain adequate sulfation of proteoglycans which is needed for cartilage development. Mediates electroneutral anion exchange of sulfate ions for oxalate ions, sulfate and oxalate ions for chloride and/or hydroxyl ions and chloride ions for bromide, iodide and nitrate ions (By similarity). The coupling of sulfate transport to both hydroxyl and chloride ions likely serves to ensure transport at both acidic pH when most sulfate uptake is mediated by sulfate-hydroxide exchange and alkaline pH when most sulfate uptake is mediated by sulfate-chloride exchange (By similarity). Essential for chondrocyte proliferation, differentiation and cell size expansion (By similarity).
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O70534
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DLK1_RAT
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Protein delta homolog 1 (DLK-1) (Preadipocyte factor 1) (Pref-1) [Cleaved into: Fetal antigen 1 (FA1)]
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MIATGALLRVLLLLLAFGHSTYGAECDPACDPQHGFCEADNVCRCEPGWEGPLCEKCVTSPGCVNGLCEEPWQCVCKEGWDGKFCEIDIRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGRASHASCLCPPGFSGNFCEIVTNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCLNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGTSPVQVTHLPSGYGLTYRLTPGVHELPVQQPEHHILKVSMKELNKSAPLLTEGQAICFTILGVLTSLVVLGTVAIVFLNKCEAWVSNLRYNHMLRKKKNLLLQYNSGEELAVNIIFPEKIDMTTFNKEAGDEDI
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May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
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O70535
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LIFR_RAT
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Leukemia inhibitory factor receptor (LIF receptor) (LIF-R) (CD antigen CD118)
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MGAFSWWRQPSWMADNKRGRMTPSLPWLLSALTLLHLMMHVNGLKRGVQQDLKCTTNNMRVWDCSWPAPLGVSPGTVKDICIKDRPHSCHRLETTNVKIPALSPGDHEVTINYQNGFQSKFTLNEKDVSLVPDTPEILSLSADFSTSTLQLKWNDKGSALPYPSNATWEVKVLQNPRTEPVALVSLNTVLSGKDKGHHWNWTSELPLQCATHSVSIRWHIDYPRFSGYKEWSEWSPLKNISWTRNTETNVFPQDKVVLAGSNMTICCISTTKVLSGQIGNTFRPLIHLYGETVAINILNIPVSENSGSNVIFSTVDDVYGTVVFAGYPPDVPQKLSCETHDLKEIICSWNPGRITGLVGPRNTEYTLFESISGKSAVFHRFEELANETYWLTLKMAPDQEIHNFTLTARNPLGQTESAIVINATERVALHVPISLKVKDVNSTVVTLSWYLPGNFTKINLVCQIEICKANSKKEVRNVTMRGAEDSTYHVAVDKLNPYTIYTFRVRCSSETFWKWSKWSNEKRYLTTEATPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSSEETQSLSEILDPQHKAEIKVNKNDYIISVVARNSAGSSPPSKIASMEIPNDDITVEQAVGIGNRIFLSWQHNPNMTCDYVIKWCNSSWSEPCLLDWIKVPSNSTGTVIESDQFQPGVRYNFYLYGCTNQGYQLLRSTIGYIEELAPIVAPNFTVEDTSADSILVKWDDIPVEELRGFLRGYLFYFQKGERDTPKTRSLETSHSDIKLKNITDISQKTLRIADLQGKTSYHLVLRAYTHGGLGPEKSMFVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSNALKTLEMNPCTPNHVEVLESRSIPPKIEDTEITSPVSERPGESSETDPENQAAVSYCPPIIEEEITNPAADEAGGASQVVYIDVQSMYQPQAKAEDEQDTDPVMVAGYKPQMRLPINPTAEDTTAEDEADKTAGYRPQANVNTWNLVSPDSPRSTDSNSEVVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
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Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells (By similarity).
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O70536
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SOAT1_RAT
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Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
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MVGEETSLRNRLSRSAENPEQDEAQKNLLDTHRNGHITMKQLIAKKRQLAAEAEELKPLFLKEVGCHFDDFVTNLIDKSASLDNGGCALTTFSILEEMKNNHRAKDLRAPPEQGKIFISRRSLLDELFEVDHIRTIYHMFIALLIIFILSTLVVDYIDEGRLVLEFSLLAYAFGQFPIVIWTWWAMFLSTLAIPYFLFQRWAHGYSKSSHPLIYSLIHGAFFLVFQLGILGFIPTYVVLAYTLPPASRFILILEQIRLVMKAHSYVRENVPRVLSAAKEKSSTVPVPTVNQYLYFLFAPTLIYRDSYPRTPTVRWGYVAMQFLQVFGCLFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLMLFLSFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYVYKDLLWFFSKRFRPAAMLAVFALSAVVHEYALAVCLSYFYPVLFVLFMFFGMAFNFIVNDSRKRPVWNIMVRASLFLGHGVILCFYSQEWYARQRCPLKNPTFLDYVRPRTWTCRYVF
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Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrateb a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions.
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O70546
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KDM6A_MOUSE
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Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously transcribed TPR protein on the X chromosome) (Ubiquitously transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A)
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MKSCGVSLATAAAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATILQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAPPPVEQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGILNGPTVDSSLPTNSVSGQQPQLPLTRMPSVSQPGVHTACPRQTLANGPFSAGHVPCSTSRTLGSTDTVLIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGPSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTVPETSRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDKVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQNVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
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Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (By similarity). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression.
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