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FA53B_DANRE
ID   FA53B_DANRE             Reviewed;         379 AA.
AC   F1QN48; Q6NYZ5; Q7ZUQ7;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Protein FAM53B {ECO:0000305};
DE   AltName: Full=Protein simplet {ECO:0000303|PubMed:19014929};
GN   Name=fam53b {ECO:0000312|ZFIN:ZDB-GENE-040426-2495};
GN   Synonyms=smp {ECO:0000303|PubMed:19014929};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19014929; DOI=10.1016/j.ydbio.2008.09.032;
RA   Kizil C., Otto G.W., Geisler R., Nuesslein-Volhard C., Antos C.L.;
RT   "Simplet controls cell proliferation and gene transcription during
RT   zebrafish caudal fin regeneration.";
RL   Dev. Biol. 325:329-340(2009).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   246-LYS--ARG-249.
RX   PubMed=25183871; DOI=10.1242/dev.108415;
RA   Kizil C., Kuechler B., Yan J.J., Oezhan G., Moro E., Argenton F., Brand M.,
RA   Weidinger G., Antos C.L.;
RT   "Simplet/Fam53b is required for Wnt signal transduction by regulating beta-
RT   catenin nuclear localization.";
RL   Development 141:3529-3539(2014).
CC   -!- FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating
CC       beta-catenin (ctnnb1) nuclear localization (PubMed:25183871). Required
CC       for appendage regeneration by regulating cell proliferation
CC       (PubMed:19014929). {ECO:0000269|PubMed:19014929,
CC       ECO:0000269|PubMed:25183871}.
CC   -!- SUBUNIT: Interacts with ctnnb1. {ECO:0000250|UniProtKB:Q14153}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25183871}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F1QN48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F1QN48-2; Sequence=VSP_059013;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in proliferating tissues
CC       (PubMed:19014929). {ECO:0000269|PubMed:19014929}.
CC   -!- INDUCTION: Following amputation, expressed in regenerating tissues
CC       (PubMed:19014929). {ECO:0000269|PubMed:19014929}.
CC   -!- DISRUPTION PHENOTYPE: Loss of posterior structures and beta-catenin
CC       (ctnnb1)-dependent gene transcription due to the absence of
CC       accumulation of beta-catenin (ctnnb1) in the nucleus (PubMed:25183871).
CC       Fishes show reduced regenerative outgrowth following amputation due to
CC       decreased cell proliferation (PubMed:19014929).
CC       {ECO:0000269|PubMed:19014929, ECO:0000269|PubMed:25183871}.
CC   -!- SIMILARITY: Belongs to the FAM53 family. {ECO:0000305}.
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DR   EMBL; AL953868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC048029; AAH48029.1; -; mRNA.
DR   EMBL; BC066405; AAH66405.1; -; mRNA.
DR   RefSeq; NP_001007188.1; NM_001007187.1.
DR   AlphaFoldDB; F1QN48; -.
DR   STRING; 7955.ENSDARP00000020465; -.
DR   PaxDb; F1QN48; -.
DR   Ensembl; ENSDART00000008312; ENSDARP00000020465; ENSDARG00000016156. [F1QN48-1]
DR   GeneID; 406586; -.
DR   KEGG; dre:406586; -.
DR   CTD; 9679; -.
DR   ZFIN; ZDB-GENE-040426-2495; fam53b.
DR   eggNOG; ENOG502QQM7; Eukaryota.
DR   GeneTree; ENSGT00530000063371; -.
DR   HOGENOM; CLU_054215_2_1_1; -.
DR   InParanoid; F1QN48; -.
DR   OMA; CSDELGG; -.
DR   OrthoDB; 1614405at2759; -.
DR   TreeFam; TF332095; -.
DR   PRO; PR:F1QN48; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000016156; Expressed in spleen and 34 other tissues.
DR   ExpressionAtlas; F1QN48; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048675; P:axon extension; IMP:ZFIN.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:ZFIN.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:ZFIN.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR029356; FAM53.
DR   PANTHER; PTHR28567; PTHR28567; 1.
DR   Pfam; PF15242; FAM53; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..379
FT                   /note="Protein FAM53B"
FT                   /id="PRO_0000440957"
FT   REGION          206..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           246..249
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:25183871"
FT   COMPBIAS        208..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_059013"
FT   MUTAGEN         246..249
FT                   /note="KRRR->EGGG: Abolishes nuclear localization and beta-
FT                   catenin (ctnnb1) import into the nucleus."
FT                   /evidence="ECO:0000269|PubMed:25183871"
FT   CONFLICT        136
FT                   /note="T -> A (in Ref. 2; AAH66405/AAH48029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="S -> T (in Ref. 2; AAH66405/AAH48029)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   379 AA;  41174 MW;  C11D301457EBA151 CRC64;
     MCVAMVIIHT KTLEKKAVDD VTSEASLQPQ EPLTMSQGTA LFSCGIMDSG RWADVGSVCG
     VQQRPVGSSL ESLWDSMREA GATGGISGLL RDLSLSEASP ASAAPPSKRQ CRSLSCSDEL
     GCRSSWRPQG SRVWTTVEKR RCHSGGSVQR GVFNPSGFPA MQRSSSFSLP AHSSHLEPFT
     HGFPFQAFSE CPQTPQTLYR SHEQICPAEA SSPESTPELQ RRSGQSGLAR SRSQPCVHNH
     QKIGVKRRRP ADSHKQRPSL DLLKMTQKLQ DFHSLSCPGF SGDDKTLPSS SPALLNDTCE
     RAQNDSSADA PIHQSESSSE DALIHQSDSS SADALIHQSE SSRPAGKERE CLWAGLCSRR
     GRDLFQLGGE LDIEQIERN
 
 
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