ID   WN2BB_XENLA             Reviewed;         128 AA.
AC   P31283;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein Wnt-2b-B;
DE   AltName: Full=Protein Xwnt-2;
DE   Flags: Fragment;
GN   Name=wnt2b-b; Synonyms=wnt2;
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], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Tail bud;
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. Functions in the canonical Wnt/beta-catenin
CC       signaling pathway. {ECO:0000250|UniProtKB:Q98SN7}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q93097}. Secreted
CC       {ECO:0000250|UniProtKB:Q93097}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from neurula stage onwards.
CC       {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   -!- CAUTION: Originally called wnt2 by PubMed:1408135 but it is considered
CC       to be a wnt2b paralog by Xenbase. {ECO:0000305}.
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DR   EMBL; L07531; AAA49984.1; -; mRNA.
DR   PIR; I51573; I51573.
DR   AlphaFoldDB; P31283; -.
DR   SMR; P31283; -.
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:0048856; P:anatomical structure 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; IPR043158; Wnt_C.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; 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..>128
FT                   /note="Protein Wnt-2b-B"
FT                   /id="PRO_0000200609"
FT   LIPID           8
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        3..16
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        5..11
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        90..105
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        127..128
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         128
SQ   SEQUENCE   128 AA;  14312 MW;  21B8656371A5F669 CRC64;
     QECKCHVSGS CTLRTCWRAL SDFRRTGDYL RRRMNGAVQV MATQDGANFT SARQGYRRAT
     RTDLVYFDNS PDYCVLDKAA GSLGTAGRVC SKTSKGTDGC EIMCCGRGYD TTRVTRVTQC
     ECKFHWCC