ID   WNT2B_CHICK             Reviewed;         385 AA.
AC   Q98SN7; Q9PUI3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Protein Wnt-2b;
DE   Flags: Precursor;
GN   Name=WNT2B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11290326; DOI=10.1016/s0092-8674(01)00285-9;
RA   Kawakami Y., Capdevila J., Buscher D., Itoh T., Esteban C.R.,
RA   Belmonte J.C.;
RT   "WNT signals control FGF-dependent limb initiation and AER induction in the
RT   chick embryo.";
RL   Cell 104:891-900(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 71-385, AND TISSUE SPECIFICITY.
RC   TISSUE=Head;
RX   PubMed=10398532;
RX   DOI=10.1002/(sici)1097-0177(199907)215:3<215::aid-aja4>3.0.co;2-w;
RA   Jasoni C., Hendrickson A., Roelink H.;
RT   "Analysis of chicken Wnt-13 expression demonstrates coincidence with cell
RT   division in the developing eye and is consistent with a role in
RT   induction.";
RL   Dev. Dyn. 215:215-224(1999).
RN   [3]
RP   FUNCTION, INTERACTION WITH FZD4 AND FZD5, AND TISSUE SPECIFICITY.
RX   PubMed=12490564; DOI=10.1242/dev.00244;
RA   Kubo F., Takeichi M., Nakagawa S.;
RT   "Wnt2b controls retinal cell differentiation at the ciliary marginal
RT   zone.";
RL   Development 130:587-598(2003).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16258938; DOI=10.1002/dvdy.20621;
RA   Fokina V.M., Frolova E.I.;
RT   "Expression patterns of Wnt genes during development of an anterior part of
RT   the chicken eye.";
RL   Dev. Dyn. 235:496-505(2006).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors (PubMed:12490564). Functions in the canonical
CC       Wnt/beta-catenin signaling pathway (PubMed:12490564). Acts as an
CC       upstream regulator of FGF10 in the lateral plate mesoderm during limb
CC       initiation in the embryo (PubMed:11290326).
CC       {ECO:0000269|PubMed:11290326, ECO:0000269|PubMed:12490564}.
CC   -!- SUBUNIT: Interacts with FZD4 and FZD5. {ECO:0000269|PubMed:12490564}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q93097}. Secreted
CC       {ECO:0000250|UniProtKB:Q93097}.
CC   -!- TISSUE SPECIFICITY: Detected at the marginal tip of the developing
CC       retina (PubMed:12490564). Expressed in the intermediate and the lateral
CC       plate mesoderm in the presumptive chick forelimb region. Expressed in
CC       the eye, head ectoderm, prospective forelimb mesenchyme, lung bud,
CC       pharyngeal arches, the brain and otic vesicle.
CC       {ECO:0000269|PubMed:10398532, ECO:0000269|PubMed:11290326,
CC       ECO:0000269|PubMed:12490564, ECO:0000269|PubMed:16258938}.
CC   -!- DEVELOPMENTAL STAGE: At stage 11, expressed in the medial sites of the
CC       embryonic right and left coelom, as well as in the medial region of the
CC       forming somites. Between stages 14 and 16, expression in the
CC       presumptive wing field, with strongest expression at stage 15. At stage
CC       17, a faint expression is detected in the posterior region of the
CC       nascent limb bud. Expressed in the ocular surface ectoderm, including
CC       the corneal epithelium, starting from the onset of the lens vesicle
CC       closing at stage 16. {ECO:0000269|PubMed:11290326,
CC       ECO:0000269|PubMed:16258938}.
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: Was initially thought to be WNT13.
CC       {ECO:0000305|PubMed:10398532}.
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DR   EMBL; AF346628; AAK38108.1; -; mRNA.
DR   EMBL; AF182403; AAD55446.1; -; mRNA.
DR   RefSeq; NP_989667.2; NM_204336.2.
DR   AlphaFoldDB; Q98SN7; -.
DR   SMR; Q98SN7; -.
DR   IntAct; Q98SN7; 2.
DR   STRING; 9031.ENSGALP00000044963; -.
DR   GlyCosmos; Q98SN7; 1 site, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000034485; -.
DR   Ensembl; ENSGALT00010066481.1; ENSGALP00010040732.1; ENSGALG00010027417.1.
DR   GeneID; 374243; -.
DR   KEGG; gga:374243; -.
DR   CTD; 7482; -.
DR   VEuPathDB; HostDB:geneid_374243; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000159166; -.
DR   InParanoid; Q98SN7; -.
DR   OMA; GRVCNKM; -.
DR   OrthoDB; 2874082at2759; -.
DR   PhylomeDB; Q98SN7; -.
DR   PRO; PR:Q98SN7; -.
DR   Proteomes; UP000000539; Chromosome 26.
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; IPI:UniProtKB.
DR   GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IEP:AgBase.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:AgBase.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IDA:AgBase.
DR   GO; GO:0061303; P:cornea development in camera-type eye; IEP:BHF-UCL.
DR   GO; GO:0060900; P:embryonic camera-type eye formation; IEP:AgBase.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:AgBase.
DR   GO; GO:0061072; P:iris morphogenesis; IEP:BHF-UCL.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEP:BHF-UCL.
DR   GO; GO:0060173; P:limb development; TAS:AgBase.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IDA:AgBase.
DR   GO; GO:0045686; P:negative regulation of glial cell differentiation; IDA:AgBase.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:AgBase.
DR   GO; GO:0003407; P:neural retina development; TAS:AgBase.
DR   GO; GO:0030182; P:neuron differentiation; IEP:AgBase.
DR   GO; GO:0090271; P:positive regulation of fibroblast growth factor production; TAS:AgBase.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:AgBase.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:AgBase.
DR   GO; GO:0090270; P:regulation of fibroblast growth factor production; IMP:AgBase.
DR   GO; GO:0010842; P:retina layer formation; IDA:AgBase.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:AgBase.
DR   CDD; cd19346; Wnt_Wnt2b; 1.
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:SF93; PROTEIN WNT-2B; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 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   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..385
FT                   /note="Protein Wnt-2b"
FT                   /id="PRO_0000392925"
FT   LIPID           237
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        152..160
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        162..182
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        231..245
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        233..240
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        303..334
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        319..329
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        333..373
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        349..364
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        351..361
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        356..357
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   385 AA;  42953 MW;  FE3204C08A3E6EF5 CRC64;
     MLSPNRLAAS PGIAVAPGRA ECGAFPRTAG AAPRICLPFV LILLALTPRA DSSWWYIGAL
     GARVICDNIP GLVNKQRQLC QRYPDIMQSV GEGAKEWIRE CQYQFRHHRW NCSTLDRDHT
     VFGRVMLRSS REAAFVYAIS SAGVVYAITR ACSQGELKAC GCDPLKRGRA KDERGEFDWG
     GCSDNINYGI RFAKAFVDAK EKKVKDARAL MNLHNNRCGR MAVKRFLKLE CKCHGVSGSC
     TLRTCWLAMS DFRKTGDYLQ KKYNGAIQVI MNQDGTGFTV ANKNFRKPTK TDLVYFENSP
     DYCVMDKSAG SLGTAGRVCN KVSRGTDGCE VMCCGRGYDT TRVTRVTKCE CKFHWCCAVR
     CKECEDTVDV HTCKAPKRAE WLDQT
//