ID   WNT7C_XENLA             Reviewed;         135 AA.
AC   P31290;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein Wnt-7c;
DE            Short=XWnt-7c;
DE   Flags: Fragment;
GN   Name=wnt7c;
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].
RX   PubMed=1408135;
RA   Wolda S.L., Moon R.T.;
RT   "Cloning and developmental expression in Xenopus laevis of seven additional
RT   members of the Wnt family.";
RL   Oncogene 7:1941-1947(1992).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Probable developmental protein. May be a
CC       signaling molecule which affects the development of discrete regions of
CC       tissues. Is likely to signal over only few cell diameters.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC       inhibition. {ECO:0000250|UniProtKB:P27467,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- SIMILARITY: Belongs to the Wnt 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; L07535; AAA49988.1; -; mRNA.
DR   PIR; I51577; I51577.
DR   AlphaFoldDB; P31290; -.
DR   SMR; P31290; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Wnt signaling pathway.
FT   CHAIN           <1..>135
FT                   /note="Protein Wnt-7c"
FT                   /id="PRO_0000200655"
FT   LIPID           9
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        5..12
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        81..112
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        97..107
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        134..135
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         135
SQ   SEQUENCE   135 AA;  15345 MW;  8456A5DA03A39B4C CRC64;
     QECKCHGVSG SCTLKTCWVT LPHFREVGYA LKDKYEQAVM VEAVRGRRHV VPTFLKLKIP
     QNNSKPAETD LVYVDRSPNF CEKDNATGSI GTYGRFCNRT STQADSCELL CCGRGYKTFQ
     YTRTGQCHCK FHWCC