WNT11_XENTR
ID WNT11_XENTR Reviewed; 352 AA.
AC B2GUT4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein Wnt-11 {ECO:0000303|PubMed:17436276};
DE AltName: Full=Protein Wnt-11-related {ECO:0000250|UniProtKB:Q670P5};
DE Flags: Precursor;
GN Name=wnt11; Synonyms=wnt11r {ECO:0000312|EMBL:AAI66399.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI66399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine {ECO:0000312|EMBL:AAI66399.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NOMENCLATURE.
RX PubMed=17436276; DOI=10.1002/dvdy.21156;
RA Garriock R.J., Warkman A.S., Meadows S.M., D'Agostino S., Krieg P.A.;
RT "Census of vertebrate Wnt genes: isolation and developmental expression of
RT Xenopus Wnt2, Wnt3, Wnt9a, Wnt9b, Wnt10a, and Wnt16.";
RL Dev. Dyn. 236:1249-1258(2007).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (By similarity). Shares much functionality with
CC wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N-
CC terminal kinase (JNK) to regulate gastrulation movements. Acts in a
CC non-cell-autonomous manner to control neural crest migration, probably
CC acting as an extracellular signal from surrounding tissue, but is not
CC required for neural crest induction. Acts redundantly with wnt11b
CC during pronephros induction. Regulates cardiac morphogenesis through
CC the activation of JNK, but is not required for cardiac differentiation.
CC Essential for dorsal fin development; required for an epithelial to
CC mesenchymal transformation event prior to migration of cells into the
CC fin, and ultimately for maintenance of fin structure. Mediates dorsal
CC fin development through a non-canonical pathway mediated by Ca(2+) (By
CC similarity). {ECO:0000250|UniProtKB:Q670P5}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q670P5}.
CC -!- PTM: Glycosylation is required for protein secretion.
CC {ECO:0000250|UniProtKB:P49893}.
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 -!- MISCELLANEOUS: Xenopus and other lower vertebrates contain duplicated
CC wnt11 genes (wnt11 and wnt11b) resulting from an ancient gene
CC duplication event, but the second copy has since been lost in mammals.
CC {ECO:0000269|PubMed:17436276}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000255}.
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DR EMBL; BC166399; AAI66399.1; -; mRNA.
DR RefSeq; NP_001121530.1; NM_001128058.1.
DR AlphaFoldDB; B2GUT4; -.
DR SMR; B2GUT4; -.
DR STRING; 8364.ENSXETP00000021058; -.
DR PaxDb; B2GUT4; -.
DR GeneID; 100158655; -.
DR KEGG; xtr:100158655; -.
DR CTD; 7481; -.
DR Xenbase; XB-GENE-854158; wnt11.
DR eggNOG; KOG3913; Eukaryota.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; B2GUT4; -.
DR OrthoDB; 797177at2759; -.
DR PhylomeDB; B2GUT4; -.
DR Reactome; R-XTR-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-XTR-4086398; Ca2+ pathway.
DR Reactome; R-XTR-4086400; PCP/CE pathway.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000019408; Expressed in neurula embryo and 11 other tissues.
DR ExpressionAtlas; B2GUT4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0033337; P:dorsal fin development; ISS:UniProtKB.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0048884; P:neuromast development; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0062009; P:secondary palate development; ISS:UniProtKB.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026536; Wnt-11.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF7; PTHR12027:SF7; 1.
DR Pfam; PF00110; wnt; 1.
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; Gastrulation;
KW Glycoprotein; Lipoprotein; Reference proteome; Secreted; Signal; Sulfation;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..352
FT /note="Protein Wnt-11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397207"
FT MOD_RES 273
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49893"
FT MOD_RES 280
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49893"
FT LIPID 213
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..89
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 207..221
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 209..216
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"
SQ SEQUENCE 352 AA; 39517 MW; 0DD8ECACF8972D55 CRC64;
MKIYFLLGIF LTFLLHTRIC QGIKWLALAK TPLSLALNQS QHCKQLEGLV SSQMQLCRSN
LELMQTIIHA AKEVKKTCIK AFTDMRWNCS SIELAPTFHQ DLERGTRESA FVYALSAAAI
SHTIARACTT GDIPGCSCAP IPGESPGPGY RWGGCADNLN YGILMGSKFS DAPMKMKKSG
SQANKLMHLH NSEVGRQVLK ASLEMKCKCH GVSGSCSIKT CWRGLQELRE IALDLKTKYL
SATKVVHRPM GTRKQLVPKD IDIRPVQETE MIYLQSSPDY CLKNEKMGSH GTHERQCNKT
SNGSDSCDLM CCGRGYNPYM DKVVERCHCK YHWCCYVTCK KCERTVERYV CK
