WNT3A_CHICK
ID WNT3A_CHICK Reviewed; 352 AA.
AC Q2LMP1; Q9PWH1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein Wnt-3a;
DE Flags: Precursor;
GN Name=WNT3A;
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] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=11142678; DOI=10.1046/j.1440-169x.2000.00545.x;
RA Kawakami Y., Wada N., Nishimatsu S., Nohno T.;
RT "Involvement of frizzled-10 in Wnt-7a signaling during chick limb
RT development.";
RL Dev. Growth Differ. 42:561-569(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=17488271; DOI=10.1111/j.1440-169x.2007.00938.x;
RA Narita T., Nishimatsu S., Wada N., Nohno T.;
RT "A Wnt3a variant participates in chick apical ectodermal ridge formation:
RT Distinct biological activities of Wnt3a splice variants in chick limb
RT development.";
RL Dev. Growth Differ. 49:493-501(2007).
RN [4]
RP PRELIMINARY CYSTEINE PALMITOYLATION, AND PALMITOLEOYLATION AT SER-209.
RX PubMed=22046319; DOI=10.1371/journal.pone.0026636;
RA Galli L.M., Burrus L.W.;
RT "Differential palmit(e)oylation of Wnt1 on C93 and S224 residues has
RT overlapping and distinct consequences.";
RL PLoS ONE 6:E26636-E26636(2011).
CC -!- FUNCTION: [Isoform 1]: Ligand for members of the frizzled family of
CC seven transmembrane receptors (Probable). Functions in the canonical
CC Wnt signaling pathway that results in activation of transcription
CC factors of the TCF/LEF family (PubMed:17488271). Regulates chick apical
CC ectodermal ridge formation (PubMed:17488271). Required for normal
CC embryonic mesoderm development and formation of caudal somites.
CC Required for normal morphogenesis of the developing neural tube (By
CC similarity). {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:17488271,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space,
CC extracellular matrix {ECO:0000305}. Secreted
CC {ECO:0000269|PubMed:17488271}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:17488271}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2LMP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2LMP1-2; Sequence=VSP_038851;
CC -!- TISSUE SPECIFICITY: Expressed in cornea. Isoform 1 is expressed in the
CC primitive streak, dorsal neural tube, proximal otic vesicle, the apical
CC ectodermal ridge and the epithelium of feather buds.
CC {ECO:0000269|PubMed:16258938, ECO:0000269|PubMed:17488271}.
CC -!- DEVELOPMENTAL STAGE: In the eye, the expression was observed at stage
CC 23 in the ocular surface epithelium ventral to the corneal epithelium.
CC Strongly expressed in the entire ocular surface at stage 26 including
CC the corneal epithelium. Remained strongly expressed at stage 30.
CC {ECO:0000269|PubMed:16258938}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors (PubMed:22046319). Depalmitoleoylation leads to inhibit the
CC Wnt signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:22046319}.
CC -!- PTM: Disulfide bonds have critical and distinct roles in secretion and
CC activity. Loss of each conserved cysteine in WNT3A results in high
CC molecular weight oxidized Wnt oligomers, which are formed through
CC inter-Wnt disulfide bonding (By similarity).
CC {ECO:0000250|UniProtKB:P56704}.
CC -!- MISCELLANEOUS: [Isoform 2]: Not secreted.
CC {ECO:0000269|PubMed:17488271}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: A palmitoylation site was proposed at Cys-77, but it was later
CC shown that this cysteine is engaged in a disulfide bond.
CC {ECO:0000269|PubMed:22046319}.
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DR EMBL; AB024080; BAA83743.1; -; mRNA.
DR EMBL; DQ022307; AAY87456.1; -; mRNA.
DR EMBL; EF068232; ABK90821.1; -; mRNA.
DR RefSeq; NP_001165072.1; NM_001171601.1. [Q2LMP1-1]
DR RefSeq; NP_990006.2; NM_204675.2.
DR AlphaFoldDB; Q2LMP1; -.
DR SMR; Q2LMP1; -.
DR IntAct; Q2LMP1; 1.
DR STRING; 9031.ENSGALP00000030668; -.
DR PaxDb; Q2LMP1; -.
DR Ensembl; ENSGALT00000054282; ENSGALP00000045045; ENSGALG00000042657. [Q2LMP1-1]
DR GeneID; 395396; -.
DR KEGG; gga:395396; -.
DR CTD; 89780; -.
DR VEuPathDB; HostDB:geneid_395396; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160510; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; Q2LMP1; -.
DR OMA; GLTHVMA; -.
DR OrthoDB; 965867at2759; -.
DR PhylomeDB; Q2LMP1; -.
DR Reactome; R-GGA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-GGA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-GGA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-GGA-4641263; Regulation of FZD by ubiquitination.
DR PRO; PR:Q2LMP1; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000042657; Expressed in lung.
DR ExpressionAtlas; Q2LMP1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; NAS:AgBase.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
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:0061303; P:cornea development in camera-type eye; IEP:BHF-UCL.
DR GO; GO:0048263; P:determination of dorsal identity; TAS:AgBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; TAS:AgBase.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:AgBase.
DR GO; GO:0060173; P:limb development; TAS:AgBase.
DR GO; GO:0035108; P:limb morphogenesis; NAS:AgBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:AgBase.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:AgBase.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; TAS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:AgBase.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:CACAO.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:AgBase.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; TAS:AgBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009141; Wnt3.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01843; WNT3PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..352
FT /note="Protein Wnt-3a"
FT /id="PRO_0000392924"
FT LIPID 209
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000269|PubMed:22046319"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..88
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 128..136
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 138..155
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 203..217
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 205..212
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 281..312
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 297..307
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 311..351
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 327..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..335
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 1..24
FT /note="MASFGYFLFLCGLSQALSSYPIWW -> MKSFCSEVVAKSRLGLKQWGWCGW
FT TPMGSAWKKWISEQRSSLELWDVG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11142678"
FT /id="VSP_038851"
SQ SEQUENCE 352 AA; 39629 MW; EE558AC4B2225B3A CRC64;
MASFGYFLFL CGLSQALSSY PIWWSLAIGH QYSSLGTQPI LCGSIPGLVP KQLRFCRNYV
EIMPSVAEGV KIGIQECQHQ FRGRRWNCTT VNDSLAIFGP VLDKATRESA FVHAIASAGV
AFAVTRSCAE GSATICGCDT RHKGSPGEGW KWGGCSEDVE FGSMVSREFA DARENRPDAR
SAMNRHNNEA GRTSIIELMH LKCKCHGLSG SCEVKTCWWS QPDFRVIGDY LKDKYDSASE
MVVEKHRESR GWVETLRPKY NFFKAPTEKD LVYYENSPNF CEPNPETGSF GTRDRICNVT
SHGIDGCDLL CCGRGHNTRT EKRKEKCHCI FHWCCYVRCQ ECIRVYDVHT CK
