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WNT7A_GORGO
ID   WNT7A_GORGO             Reviewed;         349 AA.
AC   Q1KYK7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Protein Wnt-7a;
DE   Flags: Precursor;
GN   Name=WNT7A;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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; DQ367074; ABE73776.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1KYK7; -.
DR   SMR; Q1KYK7; -.
DR   STRING; 9593.ENSGGOP00000012339; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   InParanoid; Q1KYK7; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IEA:UniProt.
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_0000245335"
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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