WNT7A_XENLA
ID WNT7A_XENLA Reviewed; 135 AA.
AC P31288;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein Wnt-7a;
DE Short=XWnt-7a;
DE Flags: Fragment;
GN Name=wnt7a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=1408135;
RA Wolda S.L., Moon R.T.;
RT "Cloning and developmental expression in Xenopus laevis of seven additional
RT members of the Wnt family.";
RL Oncogene 7:1941-1947(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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P24383}. Secreted
CC {ECO:0000250|UniProtKB:P24383}.
CC -!- TISSUE SPECIFICITY: In embryo, in brain and ventral neural tube; in
CC adults, in brain. {ECO:0000269|PubMed:1408135}.
CC -!- DEVELOPMENTAL STAGE: Tailbud onwards. {ECO:0000269|PubMed:1408135}.
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; L07533; AAA49986.1; -; mRNA.
DR AlphaFoldDB; P31288; -.
DR SMR; P31288; -.
DR Proteomes; UP000186698; Genome assembly.
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 InterPro; IPR005817; Wnt.
DR InterPro; IPR013300; Wnt7.
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 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Wnt signaling pathway.
FT CHAIN <1..>135
FT /note="Protein Wnt-7a"
FT /id="PRO_0000200649"
FT REGION 41..69
FT /note="Disordered linker"
FT /evidence="ECO:0000250|UniProtKB:O00755"
FT LIPID 9
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3..17
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 5..12
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 81..112
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 97..107
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 111..134
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 130..131
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 127..131
FT /note="Missing (in Ref. 1; AAA49986)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 135
SQ SEQUENCE 135 AA; 15563 MW; F49B870AFA1F962C CRC64;
QECKCHGVSG SCTTKTCWTT LPKFRELGFI VKDKYKEAVQ VEPVRASRNK RPTFLKIKKP
LSYRKPMDTD LVYIEKSPNY CEEDPMTGSM GTQGRLCNKT AQHTSGCDLM CCGRGYNTHQ
YSRVWQFHWC CCNCK