ID   APCD1_CHICK             Reviewed;         515 AA.
AC   Q5R2I8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protein APCDD1;
DE   AltName: Full=Adenomatosis polyposis coli down-regulated 1 protein homolog;
DE            Short=cAPCDD1;
DE   AltName: Full=Protein primglo1;
DE   Flags: Precursor;
GN   Name=APCDD1; Synonyms=PGO1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=15642085; DOI=10.1111/j.1525-142x.2005.05002.x;
RA   Kuraku S., Usuda R., Kuratani S.;
RT   "Comprehensive survey of carapacial ridge-specific genes in turtle implies
RT   co-option of some regulatory genes in carapace evolution.";
RL   Evol. Dev. 7:3-17(2005).
RN   [2]
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   [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   -!- DEVELOPMENTAL STAGE: Expressed in the dorsal somite derivatives of the
CC       chicken as well as in the dorsal subpopulation of trunk crest cells.
CC       {ECO:0000269|PubMed:15642085}.
CC   -!- SIMILARITY: Belongs to the APCDD1 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; AB124571; BAD74121.1; -; mRNA.
DR   EMBL; AB196971; BAE02562.1; -; mRNA.
DR   RefSeq; NP_001012959.1; NM_001012941.2.
DR   AlphaFoldDB; Q5R2I8; -.
DR   STRING; 9031.ENSGALP00000001313; -.
DR   PaxDb; Q5R2I8; -.
DR   PRIDE; Q5R2I8; -.
DR   Ensembl; ENSGALT00000102628; ENSGALP00000065748; ENSGALG00000050840.
DR   GeneID; 426765; -.
DR   KEGG; gga:426765; -.
DR   CTD; 147495; -.
DR   VEuPathDB; HostDB:geneid_426765; -.
DR   eggNOG; ENOG502QQ0C; Eukaryota.
DR   GeneTree; ENSGT00640000091492; -.
DR   HOGENOM; CLU_035648_0_0_1; -.
DR   InParanoid; Q5R2I8; -.
DR   OMA; GRHTWPL; -.
DR   OrthoDB; 613671at2759; -.
DR   PhylomeDB; Q5R2I8; -.
DR   TreeFam; TF329491; -.
DR   PRO; PR:Q5R2I8; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000050840; Expressed in lung and 11 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..515
FT                   /note="Protein APCDD1"
FT                   /id="PRO_0000395838"
FT   TOPO_DOM        27..490
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..508
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   515 AA;  59100 MW;  B529D4B204B1385D CRC64;
     MFVPYGSLMR YLFPALLLHG LGEGSALLHP DSRSHPRSLE KSAWRAFKES QCHHMLKHLH
     NGARITVQMP PNIEGHWVST GCEVRAGPEF ITRSYRFYHN NTFKAYQFYY GGNRCTNPIY
     TLVIRGKIRL RQASWIIRGG TEADYQLRNI QIISHNEAVA KKLSELVNNT CPGFIPEDSP
     WEQDVSYDLL REENGCECTK ALNFAMHELQ LIRVEKQYLH HNLDHLVEEL FLGDIHTDAT
     QRRYYRPSSY QPPLQNAKNH DRTCIACRII YRSDEHHPPI LPPKADLTIG LHGEWVSQRC
     EVRPEVLFLT RHFIFHDNNN TWEGHYYHYS DPICKHPTFT IYAKGRYSRG VHSAKVMGGT
     EFVFKVNHMK VTPMDVSTAS LLNVFNGNEC GAQGSWQVGV QQDVTHTNGC IALGIRLPHT
     EYEIFKMEQD ARGRYLLYNG QRPSDGSSPD RPEKRATSYQ MPLIQCASSV PRSEESPEEN
     KIRLYSSRAP AKHPSASALA LVLFICTVSY WDILS