WNT7A_CHLAE
ID WNT7A_CHLAE Reviewed; 349 AA.
AC Q1KYL3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Protein Wnt-7a;
DE Flags: Precursor;
GN Name=WNT7A;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stern R., Cox J., Nicholas A., Al-Gazali L., Woods G.;
RT "WNT7A and limb development.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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). Required for normal,
CC sexually dimorphic development of the Mullerian ducts, and for normal
CC fertility in both sexes. Required for normal neural stem cell
CC proliferation in the hippocampus dentate gyrus. Required for normal
CC progress through the cell cycle in neural progenitor cells, for self-
CC renewal of neural stem cells, and for normal neuronal differentiation
CC and maturation. Promotes formation of synapses via its interaction with
CC FZD5 (By similarity). {ECO:0000250|UniProtKB:O00755,
CC 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). Interacts (via intrinsically disordered linker region)
CC with RECK; interaction with RECK confers ligand selectivity for Wnt7 in
CC brain endothelial cells and allows these cells to selectively respond
CC to Wnt7 (By 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 -!- DOMAIN: The intrinsically disordered linker region is required for
CC recognition by RECK in brain endothelial cells.
CC {ECO:0000250|UniProtKB:O00755}.
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; DQ367068; ABE73770.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KYL3; -.
DR SMR; Q1KYL3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0009888; P:tissue 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; IPR013300; Wnt7.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01891; WNT7PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 3: Inferred from homology;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..349
FT /note="Protein Wnt-7a"
FT /id="PRO_0000245334"
FT REGION 238..266
FT /note="Disordered linker"
FT /evidence="ECO:0000250|UniProtKB:O00755"
FT LIPID 206
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..84
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 123..131
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 133..152
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 200..214
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 202..209
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 278..309
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 294..304
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 308..348
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 324..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 326..336
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..332
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 349 AA; 39019 MW; 26476F169EDEF32B CRC64;
MNRKARRCLG HLFLSLGMVY LRIGGFSTVV ALGASIICNK IPGLAPRQRA ICQSRPDAII
VIGEGSQMGL DECQFQFRNG RWNCSALGER TVFGKELKVG SREAAFTYAI IAAGVAHAIT
AACTQGNLSD CGCDKEKQGQ YHRDEGWKWG GCSADIRYGI GFAKVFVDAR EIKQNARTLM
NLHNNEAGRK ILEENMKLEC KCHGVSGSCT TKTCWTTLPQ FRELGYVLKD KYNEAVHVEP
VRASRNKRPT FLKIKKPLSY RKPMDTDLVY IEKSPNYCEE DPVTGSVGTQ GRACNKTAPQ
ASGCDLMCCG RGYNTHQYAR VWQCNCKFHW CCYVKCNTCS ERTEMYTCK
