WN2BA_XENLA
ID WN2BA_XENLA Reviewed; 351 AA.
AC P87387;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein Wnt-2b-A;
DE Short=Wnt-2b;
DE Short=XWnt-2b {ECO:0000303|PubMed:9203142};
DE AltName: Full=XWnt-2;
DE Flags: Precursor;
GN Name=wnt2b-a;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=9203142; DOI=10.1016/s0925-4773(97)00041-5;
RA Landesman Y., Sokol S.Y.;
RT "Xwnt-2b is a novel axis-inducing Xenopus Wnt, which is expressed in
RT embryonic brain.";
RL Mech. Dev. 63:199-209(1997).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12084573; DOI=10.1016/s0167-4781(02)00344-5;
RA Landesman Y., Goodenough D.A., Paul D.L.;
RT "Xwnt-2 (Xwnt-2b) is maternally expressed in Xenopus oocytes and embryos.";
RL Biochim. Biophys. Acta 1576:265-268(2002).
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 -!- TISSUE SPECIFICITY: Expressed maternally in both vegetal and animal
CC blastomeres with enrichment in the animal hemisphere. Expressed
CC zygotically near the prosencephalic-mesencephalic boundary of the
CC developing brain in neurula and tailbud stages, and also in non-brain
CC areas at tadpole stages. {ECO:0000269|PubMed:12084573,
CC ECO:0000269|PubMed:9203142}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression accumulates from stage 17 (neurula stage) onwards.
CC {ECO:0000269|PubMed:12084573}.
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 wnt-2b by PubMed:9203142. Although
CC PubMed:12084573 renames it as wnt-2, it is considered to be a wnt2b
CC paralog by Xenbase. {ECO:0000305}.
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DR EMBL; U66288; AAC60218.1; -; mRNA.
DR RefSeq; NP_001079279.1; NM_001085810.1.
DR AlphaFoldDB; P87387; -.
DR SMR; P87387; -.
DR PRIDE; P87387; -.
DR GeneID; 378566; -.
DR KEGG; xla:378566; -.
DR CTD; 378566; -.
DR Xenbase; XB-GENE-960151; wnt2b.L.
DR OrthoDB; 745245at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 378566; Expressed in lung and 12 other tissues.
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; IPR009140; Wnt2.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01842; WNT2PROTEIN.
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; Signal; Wnt signaling pathway.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..351
FT /note="Protein Wnt-2b-A"
FT /id="PRO_0000041415"
FT LIPID 203
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..78
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 118..126
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 128..148
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 197..211
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 199..206
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 269..300
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 285..295
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 299..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..330
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 317..327
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 322..323
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 351 AA; 40119 MW; 44E163F6BB4D75F5 CRC64;
MHFAYILILL ILTPRVDSSW WYIGALGARV ICDNIPGLVN KQRQLCQKHP DIMQAIGEGA
KEWIRECQHQ FRHHRWNCST LDRDHTVFGR VMLRSSRETA FVYAISYAGV VYAITRACSQ
GELKSCNCDP KKRGRSKDER GEFDWGGCSD HIDFGIKFPK DFVDAKEKRL KDARALMNLH
NNRCGRMAVK RFMNLECKCH GVSGSCTLRT CWRAMSDFRK TGDFLRRRYN GAIQVTMNQD
GSGFAVANQN FRKATKKDLV YFENSPDYCV MDKTAGSLGT AGRVCDKVSR GTDGCEVMCC
GRGYDTTRVT RITKCECKFH WCCAVRCKEC EETVDVHTCK APKRAEWLDQ T
