ID   CSTOS_XENLA             Reviewed;         237 AA.
AC   P0DPK0;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Protein CUSTOS {ECO:0000303|PubMed:25157132};
GN   Name=custos {ECO:0000303|PubMed:25157132};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2; CSNK1A1 AND
RP   CTNNB1, PHOSPHORYLATION, SUBCELLULAR LOCATION, 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:0000269|PubMed:25157132}.
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:25157132}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally and then widely throughout
CC       embryogenesis. During the neurula stage, highly expressed in the neural
CC       plate and neural fold. Strong expression also seen in brain, eyes and
CC       spinal cord at the tadpole stage. {ECO:0000269|PubMed:25157132}.
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}.
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DR   EMBL; KM235953; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_018117091.1; XM_018261602.1.
DR   AlphaFoldDB; P0DPK0; -.
DR   GeneID; 100381174; -.
DR   KEGG; xla:100381174; -.
DR   CTD; 100381174; -.
DR   Xenbase; XB-GENE-5925308; c12orf43.L.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 100381174; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Developmental protein; Nucleus; Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..237
FT                   /note="Protein CUSTOS"
FT                   /id="PRO_0000444887"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           182..190
FT                   /note="Nucleolar localization signal (NLS1)"
FT                   /evidence="ECO:0000305|PubMed:25157132"
FT   MOTIF           217..225
FT                   /note="Nucleolar localization signal (NLS2)"
FT                   /evidence="ECO:0000305|PubMed:25157132"
FT   COMPBIAS        50..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26515 MW;  1BFD0F91C95A4C02 CRC64;
     MAAPRRGTQK SDSDSSDEDL DRFREAAWVP PGAHQKVSDE QNEKIALPSL RVRPDCHEHD
     GNELQTTPEF RSHVAKKLAA ILDSSIREVS QNEAVHISKA GNGDSEDEGF RLFRTSLPGE
     AGIVTSTIPR RKLASSSSED SEEEQQRCRE AAVSACDILR HSTLQQEPQS TPSNVCDNQP
     PKKKRKKKKK DRGDTSQINS VEETMHIEPG KNELQAKRKK KKKQKLEMAH CDELGNE