ID   APCD1_XENLA             Reviewed;         515 AA.
AC   Q66KI8; Q4R1K0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Protein APCDD1;
DE   AltName: Full=Adenomatosis polyposis coli down-regulated 1 protein homolog;
DE   AltName: Full=Protein primglo;
DE            Short=xPgo;
DE   Flags: Precursor;
GN   Name=apcdd1;
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].
RA   Kimura J., Kuroiwa A.;
RT   "Primglo, a Wnt target novel endoplasmic reticulum protein that modulates
RT   Wnt signaling.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=20393562; DOI=10.1038/nature08875;
RA   Shimomura Y., Agalliu D., Vonica A., Luria V., Wajid M., Baumer A.,
RA   Belli S., Petukhova L., Schinzel A., Brivanlou A.H., Barres B.A.,
RA   Christiano A.M.;
RT   "APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis
RT   simplex.";
RL   Nature 464:1043-1047(2010).
CC   -!- FUNCTION: Negative regulator of the Wnt signaling pathway. Inhibits Wnt
CC       signaling in a cell-autonomous manner and functions upstream of beta-
CC       catenin. {ECO:0000269|PubMed:20393562}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the APCDD1 family. {ECO:0000305}.
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DR   EMBL; AB196973; BAE02564.1; -; mRNA.
DR   EMBL; BC080377; AAH80377.1; -; mRNA.
DR   RefSeq; NP_001087578.1; NM_001094109.1.
DR   AlphaFoldDB; Q66KI8; -.
DR   GeneID; 447402; -.
DR   KEGG; xla:447402; -.
DR   CTD; 447402; -.
DR   Xenbase; XB-GENE-5762142; apcdd1.L.
DR   OMA; GRHTWPL; -.
DR   OrthoDB; 613671at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 447402; Expressed in ovary and 15 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR042425; APCDD1.
DR   InterPro; IPR029405; APCDD1_dom.
DR   PANTHER; PTHR31021; PTHR31021; 1.
DR   Pfam; PF14921; APCDDC; 2.
DR   SMART; SM01352; APCDDC; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Wnt signaling pathway.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..515
FT                   /note="Protein APCDD1"
FT                   /id="PRO_0000395840"
FT   TOPO_DOM        29..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          438..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        100
FT                   /note="N -> D (in Ref. 1; BAE02564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="D -> H (in Ref. 1; BAE02564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="K -> E (in Ref. 1; BAE02564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="L -> V (in Ref. 1; BAE02564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  58943 MW;  AB0D178A5EB980B4 CRC64;
     MGIPCFYSSL ISCLFSIITL VDVGQSSALT LSDSRLHPQS LEKSPWREFQ CQHMLKHLHN
     GARVTVQMPP NIEGHWVSMG CEVRSGPEFI TRSYRFYNNN TFKAYQHYYG NNHCTIPTYT
     LVIRGKIRLR QASWIIRGGT EADYQLHNVQ IIPHSETVAE KLTWLVNHTC AGFVPGDMPW
     EPGISYDLWR EEGGFKCTKA LNFAMHELQL IRVEKQYMHH NLDHLVEELF LGDIHTDPSQ
     RMYYRPSSYQ PPLQNAKNHN QNCVACRIIL RSDEHHPPIL PAKADLPVGL NGEWVSQRCE
     VRPEVLFLTR HFIFNDNNHT WEGFYYHYSD PICKHPSFTI YAKGRYSRGV YSSKVMGGTE
     FVFKVNHMKV TPMDFATASL LNVFNGDECG AEGSWKVGVE QDVTHTNGCV ALGIKLPHTE
     YELFRMEQDN RGRYLLYNGQ RPSDGSSPAR PEKRATSYQV PLVQCTSVSL NPEGAHDGQH
     KSQSRNSAAG HIFLYLFSNL FLLFICTLLH LEILS