CSTOS_DANRE
ID CSTOS_DANRE Reviewed; 236 AA.
AC A9C3N6; A3KNH5; A8WGJ3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein CUSTOS {ECO:0000303|PubMed:25157132};
GN Name=custos {ECO:0000303|PubMed:25157132}; ORFNames=zgc:162025;
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].
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25157132; DOI=10.1073/pnas.1414437111;
RA Komiya Y., Mandrekar N., Sato A., Dawid I.B., Habas R.;
RT "Custos controls beta-catenin to regulate head development during
RT vertebrate embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:13099-13104(2014).
CC -!- FUNCTION: Essential for Spemann-Mangold organizer formation and
CC subsequent anterior head development in the embryo. Inhibits canonical
CC Wnt signaling pathway by antagonizing nuclear import of beta-catenin
CC (ctnnb1) during embryogenesis. {ECO:0000269|PubMed:25157132}.
CC -!- SUBUNIT: Interacts (via NLS1 and NLS2) with dvl2; the interaction is
CC negatively regulated by Wnt stimulation. Interacts with csnk1a1.
CC Interacts with ctnnb1; the interaction is positively regulated by Wnt
CC stimulation. {ECO:0000250|UniProtKB:P0DPK0}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:P0DPK0}.
CC -!- PTM: Phosphorylated by ck1/csnk1a1. {ECO:0000269|PubMed:25157132}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in embryos with
CC small eyes, head, and brain structures. {ECO:0000269|PubMed:25157132}.
CC -!- MISCELLANEOUS: Named Custos for the Latin term for 'guard' or 'keeper'.
CC {ECO:0000305|PubMed:25157132}.
CC -!- SIMILARITY: Belongs to the CUSTOS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR376731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC154734; AAI54735.1; -; mRNA.
DR EMBL; BC133840; AAI33841.1; -; mRNA.
DR RefSeq; NP_001082895.1; NM_001089426.1.
DR AlphaFoldDB; A9C3N6; -.
DR STRING; 7955.ENSDARP00000067842; -.
DR PaxDb; A9C3N6; -.
DR PeptideAtlas; A9C3N6; -.
DR Ensembl; ENSDART00000067843; ENSDARP00000067842; ENSDARG00000046141.
DR GeneID; 571775; -.
DR KEGG; dre:571775; -.
DR ZFIN; ZDB-GENE-070424-17; zgc:162025.
DR eggNOG; ENOG502S3AI; Eukaryota.
DR GeneTree; ENSGT00390000010771; -.
DR HOGENOM; CLU_092827_0_0_1; -.
DR InParanoid; A9C3N6; -.
DR OMA; HQGNGEQ; -.
DR OrthoDB; 1482758at2759; -.
DR TreeFam; TF336221; -.
DR PRO; PR:A9C3N6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000046141; Expressed in mature ovarian follicle and 19 other tissues.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0097065; P:anterior head development; IMP:ZFIN.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0060061; P:Spemann organizer formation; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR026694; CUSTOS.
DR PANTHER; PTHR14482; PTHR14482; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Nucleus; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..236
FT /note="Protein CUSTOS"
FT /id="PRO_0000444888"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 173..181
FT /note="Nucleolar localization signal (NLS1)"
FT /evidence="ECO:0000305|PubMed:25157132"
FT MOTIF 211..219
FT /note="Nucleolar localization signal (NLS2)"
FT /evidence="ECO:0000305|PubMed:25157132"
FT COMPBIAS 1..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 224
FT /note="K -> KK (in Ref. 2; AAI33841)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="K -> KKKK (in Ref. 2; AAI54735)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> E (in Ref. 2; AAI54735/AAI33841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26810 MW; DCD23D159BE66C73 CRC64;
MSESSSEDEN TARLKEAVWS FKPEDVKING KENNGRQSHR ADVSKHEHDG NELGTTPEFR
SHVAKKLGTY LDGCISEVCS DTVEPAQSEN REDEEGFRLF SSSTPGKWME QSPPPPPKRR
PVPSSSDSDS EMEMRFREAA VSLSDILGPV AQNLSEKTEE KSTKEETEDT VTKMKKKKKR
KTSSEESQDK VNHQTEKQSN VEGNQEQTTA GERLKKKKKK KKKKRKKLEK DIKKDE
