WNT11_XENLA
ID WNT11_XENLA Reviewed; 352 AA.
AC Q670P5; Q66KR3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein Wnt-11 {ECO:0000303|PubMed:17436276};
DE AltName: Full=Protein Wnt-11-related {ECO:0000303|PubMed:15708567};
DE Short=Wnt11-R {ECO:0000303|PubMed:15708567};
DE Short=Wnt11r {ECO:0000303|PubMed:15708567};
DE Flags: Precursor;
GN Name=wnt11 {ECO:0000312|Xenbase:XB-GENE-866540}; Synonyms=wnt11r;
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, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Tadpole heart {ECO:0000269|PubMed:15708567};
RX PubMed=15708567; DOI=10.1016/j.ydbio.2004.12.013;
RA Garriock R.J., D'Agostino S.L., Pilcher K.C., Krieg P.A.;
RT "Wnt11-R, a protein closely related to mammalian Wnt11, is required for
RT heart morphogenesis in Xenopus.";
RL Dev. Biol. 279:179-192(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH78589.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RX PubMed=8306880; DOI=10.1242/dev.119.4.1161;
RA Ku M., Melton D.A.;
RT "Xwnt-11: a maternally expressed Xenopus wnt gene.";
RL Development 119:1161-1173(1993).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17240368; DOI=10.1016/j.ydbio.2006.12.020;
RA Garriock R.J., Krieg P.A.;
RT "Wnt11-R signaling regulates a calcium sensitive EMT event essential for
RT dorsal fin development of Xenopus.";
RL Dev. Biol. 304:127-140(2007).
RN [5]
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18942153; DOI=10.1002/dvdy.21758;
RA Matthews H.K., Broders-Bondon F., Thiery J.P., Mayor R.;
RT "Wnt11r is required for cranial neural crest migration.";
RL Dev. Dyn. 237:3404-3409(2008).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19582868; DOI=10.1002/dvdy.22012;
RA Tetelin S., Jones E.A.;
RT "Xenopus Wnt11b is identified as a potential pronephric inducer.";
RL Dev. Dyn. 239:148-159(2010).
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+).
CC {ECO:0000250, ECO:0000269|PubMed:15708567, ECO:0000269|PubMed:17240368,
CC ECO:0000269|PubMed:18942153, ECO:0000269|PubMed:19582868}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18942153}.
CC -!- TISSUE SPECIFICITY: In embryos, expressed in the neural tube, dorsal
CC somite, mesenchymal cells within the dorsal fin, branchial arches and
CC heart muscle, becoming expressed throughout the myocardium by the
CC tadpole stage (stage 45). Prior to neural crest cell migration,
CC expressed in a domain flanking the neural crest on the medial or neural
CC (the opposite side to wnt11b). Weakly expressed in the developing
CC pronephros from stage 25, with expression increasing from stages 30 to
CC 35. {ECO:0000269|PubMed:15708567, ECO:0000269|PubMed:17240368,
CC ECO:0000269|PubMed:18942153, ECO:0000269|PubMed:19582868}.
CC -!- DEVELOPMENTAL STAGE: Expressed after gastrulation (post stage 13).
CC {ECO:0000269|PubMed:15708567}.
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 resulting from an ancient gene duplication event, but the
CC second copy has since been lost in mammals. This gene was originally
CC called wnt11r (PubMed:8306880). but was renamed to wnt11 to reflect its
CC orthology (PubMed:17436276). {ECO:0000303|PubMed:17436276,
CC ECO:0000303|PubMed:8306880}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000255}.
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DR EMBL; AY695415; AAU05603.1; -; mRNA.
DR EMBL; BC078589; AAH78589.1; -; mRNA.
DR EMBL; BC169466; AAI69466.1; -; mRNA.
DR EMBL; BC169468; AAI69468.1; -; mRNA.
DR RefSeq; NP_001087079.1; NM_001093610.1.
DR AlphaFoldDB; Q670P5; -.
DR SMR; Q670P5; -.
DR BioGRID; 103775; 1.
DR PRIDE; Q670P5; -.
DR GeneID; 446915; -.
DR KEGG; xla:446915; -.
DR CTD; 446915; -.
DR Xenbase; XB-GENE-866540; wnt11.S.
DR OrthoDB; 797177at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 446915; Expressed in neurula embryo and 12 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0033337; P:dorsal fin development; IMP:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; IDA:BHF-UCL.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:DFLAT.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; IMP: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_0000397206"
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 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"
FT CONFLICT 31
FT /note="T -> G (in Ref. 2; AAH78589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39470 MW; 3B98AD8296EC438E CRC64;
MKIYFLLGTF LTFLLHTRIC QGIKWLALSK TPLSLPLNQT QHCKQLEGLV SSQMQLCRSN
LELMQTIIHA AKEVKKTCVK AFTDMRWNCS SIELAPTFHQ DLERGTRESA FVHALSAAAI
SHTIARACTT GDIPGCSCAP IPGESPGPGY RWGGCADNLN YGILMGSKFS DAPMKMKKSG
SQANKLMHLH NSEVGRQVLK ASLEMKCKCH GVSGSCSIKT CWRGLQELRE IALDLKTKYL
SATKVVHRPM GTRKHLVPKD IDIRPVQETE LIYLQSSPDY CLKNEKIGSH GTHERQCNKT
SNGSDSCDLM CCGRGYNPYM DKVVERCLCK YHWCCYVTCK KCERTVERYV CK
