ID WNT7A_CALJA Reviewed; 349 AA.
AC Q1KYK6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Protein Wnt-7a;
DE Flags: Precursor;
GN Name=WNT7A;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
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; DQ367075; ABE73777.1; -; Genomic_DNA.
DR RefSeq; XP_002758695.1; XM_002758649.3.
DR AlphaFoldDB; Q1KYK6; -.
DR SMR; Q1KYK6; -.
DR STRING; 9483.ENSCJAP00000031115; -.
DR GlyCosmos; Q1KYK6; 3 sites, No reported glycans.
DR Ensembl; ENSCJAT00000032881.4; ENSCJAP00000031115.3; ENSCJAG00000040771.3.
DR GeneID; 100387909; -.
DR KEGG; cjc:100387909; -.
DR CTD; 7476; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158523; -.
DR HOGENOM; CLU_033039_1_4_1; -.
DR InParanoid; Q1KYK6; -.
DR OMA; CRCRGFS; -.
DR OrthoDB; 2874082at2759; -.
DR TreeFam; TF105310; -.
DR Proteomes; UP000008225; Chromosome 15.
DR Bgee; ENSCJAG00000040771; Expressed in frontal cortex and 1 other cell type or tissue.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IEA:Ensembl.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0021846; P:cell proliferation in forebrain; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0060066; P:oviduct development; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:1904891; P:positive regulation of excitatory synapse assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0062009; P:secondary palate development; IEA:Ensembl.
DR GO; GO:0014719; P:skeletal muscle satellite cell activation; IEA:Ensembl.
DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0048864; P:stem cell development; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
DR CDD; cd19349; Wnt_Wnt7a; 1.
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:SF78; PROTEIN WNT-7A; 1.
DR PANTHER; PTHR12027; WNT RELATED; 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; Reference proteome; 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_0000245333"
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; 39005 MW; 259EF506CFCD7AB0 CRC64;
MNRKARRCLG HLFLSLGMVY LRIGGFSSVV 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
//
