ID   WNT7A_ALOVU             Reviewed;         123 AA.
AC   P28105;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein Wnt-7a;
DE   Flags: Fragment;
GN   Name=WNT-7A;
OS   Alopias vulpinus (Common thresher shark) (Squalus vulpinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Lamniformes; Alopiidae; Alopias.
OX   NCBI_TaxID=7852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1534411; DOI=10.1073/pnas.89.11.5098;
RA   Sidow A.;
RT   "Diversification of the Wnt gene family on the ancestral lineage of
RT   vertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5098-5102(1992).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors that functions in the canonical Wnt/beta-
CC       catenin signaling pathway (By similarity). Plays an important role in
CC       embryonic development, including dorsal versus ventral patterning
CC       during limb development, skeleton development and urogenital tract
CC       development. Required for central nervous system (CNS) angiogenesis and
CC       blood-brain barrier regulation (By similarity).
CC       {ECO:0000250|UniProtKB:O00755, ECO:0000250|UniProtKB:P24383}.
CC   -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC       oligomerization and is required for prolonged biological activity. The
CC       complex with AFM may represent the physiological form in body fluids
CC       (By similarity). Interacts with FZD5. Interacts with PORCN (By
CC       similarity). {ECO:0000250|UniProtKB:O00755,
CC       ECO:0000250|UniProtKB:P24383}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P24383}. Secreted
CC       {ECO:0000250|UniProtKB:P24383}.
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}.
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DR   EMBL; M91256; AAA48542.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28105; -.
DR   SMR; P28105; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013300; Wnt7.
DR   InterPro; IPR043158; Wnt_C.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
DR   SMART; SM00097; WNT1; 1.
PE   3: Inferred from homology;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Secreted; Wnt signaling pathway.
FT   CHAIN           <1..>123
FT                   /note="Protein Wnt-7a"
FT                   /id="PRO_0000200645"
FT   REGION          33..61
FT                   /note="Disordered linker"
FT                   /evidence="ECO:0000250|UniProtKB:O00755"
FT   LIPID           1
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        89..104
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         123
SQ   SEQUENCE   123 AA;  14274 MW;  A14C64948BBB1DA4 CRC64;
     SGSCTTKTCW TMLPKFRELG YILKEKYNEA VQVEPVRTHR NKRPVFLKIK KPLSYRKPMV
     TDLVYIEKSP NYCEEDPITG SVGTQGRMCN KTSSQNNSCD LMCCGRGYNT HQYSRVWQCN
     CKF