WNT2B_CHICK
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 03-AUG-2022, entry version 111.
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.ENSGALP00000034485; -.
DR PaxDb; Q98SN7; -.
DR PRIDE; Q98SN7; -.
DR GeneID; 374243; -.
DR KEGG; gga:374243; -.
DR CTD; 7482; -.
DR VEuPathDB; HostDB:geneid_374243; -.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; Q98SN7; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; Q98SN7; -.
DR PRO; PR:Q98SN7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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 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 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
