WNT7B_XENLA
ID WNT7B_XENLA Reviewed; 135 AA.
AC P31289;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein Wnt-7b;
DE Short=XWnt-7b;
DE Flags: Fragment;
GN Name=wnt7b;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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). Required for normal fusion
CC of the chorion and the allantois during placenta development (By
CC similarity). Required for central nervous system (CNS) angiogenesis and
CC blood-brain barrier regulation (By similarity).
CC {ECO:0000250|UniProtKB:P28047, ECO:0000250|UniProtKB:P56706}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P56706}. Secreted
CC {ECO:0000250|UniProtKB:P56706}.
CC -!- TISSUE SPECIFICITY: In adults, in brain and lung.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07534; AAA49987.1; -; mRNA.
DR PIR; I51576; I51576.
DR AlphaFoldDB; P31289; -.
DR SMR; P31289; -.
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 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 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-7b"
FT /id="PRO_0000200654"
FT REGION 41..69
FT /note="Disordered linker"
FT /evidence="ECO:0000250|UniProtKB:P56706"
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 134..135
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT NON_TER 1
FT NON_TER 135
SQ SEQUENCE 135 AA; 15613 MW; 033485E57F34E0F9 CRC64;
QECKCHGVSG SCTTKTCWNT LPKFREIGFV LKEKYNDAVH VEVVRANRLR QPTFLKIKKV
RSYQKPMETD LVYIERSPNY CEEDSTTGSV GTQGRLCNRT SPHTDGCDLM CCGRGYNTHQ
YTKVWQCNCK FHWCC