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WNT7A_CALJA
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   03-AUG-2022, entry version 91.
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   Ensembl; ENSCJAT00000032881; ENSCJAP00000031115; ENSCJAG00000040771.
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; VQHISGC; -.
DR   OrthoDB; 745245at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000008225; Chromosome 15.
DR   Bgee; ENSCJAG00000040771; Expressed in frontal cortex and 1 other 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: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   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; 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
 
 
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