WN11B_XENLA
ID WN11B_XENLA Reviewed; 353 AA.
AC P49893; Q5U5D9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein Wnt-11b;
DE AltName: Full=Protein Wnt-11;
DE Short=XWnt-11;
DE Flags: Precursor;
GN Name=wnt11b; Synonyms=wnt-11, wnt11;
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=Oocyte;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=7539356; DOI=10.1242/dev.121.2.287;
RA Kloc M., Etkin L.D.;
RT "Two distinct pathways for the localization of RNAs at the vegetal cortex
RT in Xenopus oocytes.";
RL Development 121:287-297(1995).
RN [4]
RP FUNCTION.
RX PubMed=7739543; DOI=10.1128/mcb.15.5.2625;
RA Du S.J., Purcell S.M., Christian J.L., McGrew L.L., Moon R.T.;
RT "Identification of distinct classes and functional domains of Wnts through
RT expression of wild-type and chimeric proteins in Xenopus embryos.";
RL Mol. Cell. Biol. 15:2625-2634(1995).
RN [5]
RP FUNCTION.
RX PubMed=8655584; DOI=10.1083/jcb.133.5.1123;
RA Torres M.A., Yang-Snyder J.A., Purcell S.M., DeMarais A.A., McGrew L.L.,
RA Moon R.T.;
RT "Activities of the Wnt-1 class of secreted signaling factors are
RT antagonized by the Wnt-5A class and by a dominant negative cadherin in
RT early Xenopus development.";
RL J. Cell Biol. 133:1123-1137(1996).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10525335; DOI=10.1006/dbio.1999.9426;
RA Schroeder K.E., Condic M.L., Eisenberg L.M., Yost H.J.;
RT "Spatially regulated translation in embryos: asymmetric expression of
RT maternal Wnt-11 along the dorsal-ventral axis in Xenopus.";
RL Dev. Biol. 214:288-297(1999).
RN [7]
RP FUNCTION.
RX PubMed=10751186; DOI=10.1242/dev.127.9.1981;
RA Sumanas S., Strege P., Heasman J., Ekker S.C.;
RT "The putative Wnt receptor Xenopus frizzled-7 functions upstream of beta-
RT catenin in vertebrate dorso-ventral mesoderm patterning.";
RL Development 127:1981-1990(2000).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10769246; DOI=10.1242/dev.127.10.2227;
RA Tada M., Smith J.C.;
RT "Xwnt11 is a target of Xenopus Brachyury: regulation of gastrulation
RT movements via Dishevelled, but not through the canonical Wnt pathway.";
RL Development 127:2227-2238(2000).
RN [9]
RP FUNCTION, INTERACTION WITH FZD7, AND SUBCELLULAR LOCATION.
RX PubMed=10862746; DOI=10.1242/dev.127.14.3091;
RA Djiane A., Riou J.-F., Umbhauer M., Boucaut J.-C., Shi D.-L.;
RT "Role of frizzled 7 in the regulation of convergent extension movements
RT during gastrulation in Xenopus laevis.";
RL Development 127:3091-3100(2000).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10585568; DOI=10.1016/s0925-4773(99)00228-2;
RA Pannese M., Cagliani R., Pardini C.L., Boncinelli E.;
RT "Xotx1 maternal transcripts are vegetally localized in Xenopus laevis
RT oocytes.";
RL Mech. Dev. 90:111-114(2000).
RN [11]
RP INDUCTION.
RX PubMed=10781937; DOI=10.1016/s0925-4773(00)00260-4;
RA Saka Y., Tada M., Smith J.C.;
RT "A screen for targets of the Xenopus T-box gene Xbra.";
RL Mech. Dev. 93:27-39(2000).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11128985; DOI=10.1098/rstb.2000.0627;
RA Smith J.C., Conlon F.L., Saka Y., Tada M.;
RT "Xwnt11 and the regulation of gastrulation in Xenopus.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 355:923-930(2000).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11784070; DOI=10.1006/dbio.2001.0495;
RA Heasman J., Wessely O., Langland R., Craig E.J., Kessler D.S.;
RT "Vegetal localization of maternal mRNAs is disrupted by VegT depletion.";
RL Dev. Biol. 240:377-386(2001).
RN [14]
RP LACK OF FUNCTION IN HEART INDUCTION.
RX PubMed=11159911; DOI=10.1101/gad.855601;
RA Schneider V.A., Mercola M.;
RT "Wnt antagonism initiates cardiogenesis in Xenopus laevis.";
RL Genes Dev. 15:304-315(2001).
RN [15]
RP FUNCTION.
RX PubMed=12167861; DOI=10.1038/nature00921;
RA Pandur P., Lasche M., Eisenberg L.M., Kuhl M.;
RT "Wnt-11 activation of a non-canonical Wnt signalling pathway is required
RT for cardiogenesis.";
RL Nature 418:636-641(2002).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=12946266; DOI=10.1023/a:1025099320362;
RA Shatilov D.V., Pshennikova E.S., Voronina A.S.;
RT "Transition of Xwnt-11 mRNA from inactive form to polyribosomes in frogs
RT during early embryogenesis.";
RL Biochemistry (Mosc.) 68:822-825(2003).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15543138; DOI=10.1038/ncb1191;
RA Kim S.-W., Park J.-I., Spring C.M., Sater A.K., Ji H., Otchere A.A.,
RA Daniel J.M., McCrea P.D.;
RT "Non-canonical Wnt signals are modulated by the Kaiso transcriptional
RT repressor and p120-catenin.";
RL Nat. Cell Biol. 6:1212-1220(2004).
RN [18]
RP FUNCTION, INTERACTION WITH TDGF1, AND TISSUE SPECIFICITY.
RX PubMed=15797385; DOI=10.1016/j.cell.2005.01.013;
RA Tao Q., Yokota C., Puck H., Kofron M., Birsoy B., Yan D., Asashima M.,
RA Wylie C.C., Lin X., Heasman J.;
RT "Maternal wnt11 activates the canonical wnt signaling pathway required for
RT axis formation in Xenopus embryos.";
RL Cell 120:857-871(2005).
RN [19]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15857909; DOI=10.1242/dev.01857;
RA De Calisto J., Araya C., Marchant L., Riaz C.F., Mayor R.;
RT "Essential role of non-canonical Wnt signalling in neural crest
RT migration.";
RL Development 132:2587-2597(2005).
RN [20]
RP FUNCTION.
RX PubMed=16169711; DOI=10.1016/j.mod.2005.06.007;
RA Carron C., Bourdelas A., Li H.Y., Boucaut J.C., Shi D.L.;
RT "Antagonistic interaction between IGF and Wnt/JNK signaling in convergent
RT extension in Xenopus embryo.";
RL Mech. Dev. 122:1234-1247(2005).
RN [21]
RP FUNCTION, INTERACTION WITH FRZB1; FRZB2 AND FZD7, AND TISSUE SPECIFICITY.
RX PubMed=16274967; DOI=10.1016/j.mod.2005.06.002;
RA Shibata M., Itoh M., Hikasa H., Taira S., Taira M.;
RT "Role of crescent in convergent extension movements by modulating Wnt
RT signaling in early Xenopus embryogenesis.";
RL Mech. Dev. 122:1322-1339(2005).
RN [22]
RP FUNCTION, AND INTERACTION WITH LRP6.
RX PubMed=17202189; DOI=10.1242/dev.02739;
RA Kofron M., Birsoy B., Houston D., Tao Q., Wylie C., Heasman J.;
RT "Wnt11/beta-catenin signaling in both oocytes and early embryos acts
RT through LRP6-mediated regulation of axin.";
RL Development 134:503-513(2007).
RN [23]
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 [24]
RP FUNCTION.
RX PubMed=17663724; DOI=10.1111/j.1365-2443.2007.01106.x;
RA Yamanaka H., Nishida E.;
RT "Wnt11 stimulation induces polarized accumulation of Dishevelled at apical
RT adherens junctions through Frizzled7.";
RL Genes Cells 12:961-967(2007).
RN [25]
RP FUNCTION, AND INDUCTION.
RX PubMed=18715946; DOI=10.1242/dev.026443;
RA Afouda B.A., Martin J., Liu F., Ciau-Uitz A., Patient R., Hoppler S.;
RT "GATA transcription factors integrate Wnt signalling during heart
RT development.";
RL Development 135:3185-3190(2008).
RN [26]
RP FUNCTION, HOMODIMERIZATION, IDENTIFICATION IN A COMPLEX WITH WNT5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18927149; DOI=10.1242/dev.029025;
RA Cha S.W., Tadjuidje E., Tao Q., Wylie C., Heasman J.;
RT "Wnt5a and Wnt11 interact in a maternal Dkk1-regulated fashion to activate
RT both canonical and non-canonical signaling in Xenopus axis formation.";
RL Development 135:3719-3729(2008).
RN [27]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18981481; DOI=10.1101/gad.1687308;
RA Li Y., Rankin S.A., Sinner D., Kenny A.P., Krieg P.A., Zorn A.M.;
RT "Sfrp5 coordinates foregut specification and morphogenesis by antagonizing
RT both canonical and noncanonical Wnt11 signaling.";
RL Genes Dev. 22:3050-3063(2008).
RN [28]
RP FUNCTION, AND INTERACTION WITH RYK.
RX PubMed=18809723; DOI=10.1083/jcb.200710188;
RA Kim G.H., Her J.H., Han J.K.;
RT "Ryk cooperates with Frizzled 7 to promote Wnt11-mediated endocytosis and
RT is essential for Xenopus laevis convergent extension movements.";
RL J. Cell Biol. 182:1073-1082(2008).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH WNT5A,
RP GLYCOSYLATION AT ASN-88 AND ASN-299, SULFATION AT TYR-274 AND TYR-281, AND
RP MUTAGENESIS OF ASN-88; TYR-274; TYR-281 AND ASN-299.
RX PubMed=19747829; DOI=10.1016/j.cub.2009.07.062;
RA Cha S.W., Tadjuidje E., White J., Wells J., Mayhew C., Wylie C.,
RA Heasman J.;
RT "Wnt11/5a complex formation caused by tyrosine sulfation increases
RT canonical signaling activity.";
RL Curr. Biol. 19:1573-1580(2009).
RN [30]
RP SUBCELLULAR LOCATION.
RX PubMed=19906850; DOI=10.1242/dev.032524;
RA Mii Y., Taira M.;
RT "Secreted Frizzled-related proteins enhance the diffusion of Wnt ligands
RT and expand their signalling range.";
RL Development 136:4083-4088(2009).
RN [31]
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).
RN [32]
RP REVIEW.
RX PubMed=12137733; DOI=10.1016/s1084-9521(02)00050-2;
RA Kuhl M.;
RT "Non-canonical Wnt signaling in Xenopus: regulation of axis formation and
RT gastrulation.";
RL Semin. Cell Dev. Biol. 13:243-249(2002).
RN [33]
RP REVIEW.
RX PubMed=19232955; DOI=10.1016/j.tcm.2008.12.001;
RA Flaherty M.P., Dawn B.;
RT "Noncanonical Wnt11 signaling and cardiomyogenic differentiation.";
RL Trends Cardiovasc. Med. 18:260-268(2008).
CC -!- FUNCTION: Ligand for the frizzled7 transmembrane receptor. Primarily
CC acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC,
CC or by JNK and dvl2/dsh. Depending on the cellular context, can also
CC signal via the canonical Wnt pathway mediated by beta-catenin and
CC dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally
CC initiates dorsal/ventral axis formation by a canonical route, which
CC signals via lrp6. In a complex with wnt5a, activates the canonical and
CC non-canonical processes involved in axis formation. In the non-
CC canonical pathway, acts through fzd7/fz7 to induce phosphorylation of
CC dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate
CC convergent extension movements during gastrulation. Interactions with
CC the secreted Wnt antagonist sfrp5 to coordinate foregut development,
CC acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b
CC activity to prevent inappropriate foregut formation. Mediates
CC cardiogenesis via non-canonical Wnt signaling involving JNK-activation
CC and PKC. Acts redundantly with wnt11/wnt11r during pronephros
CC induction. {ECO:0000269|PubMed:10751186, ECO:0000269|PubMed:10769246,
CC ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:11128985,
CC ECO:0000269|PubMed:12167861, ECO:0000269|PubMed:15543138,
CC ECO:0000269|PubMed:15797385, ECO:0000269|PubMed:15857909,
CC ECO:0000269|PubMed:16169711, ECO:0000269|PubMed:16274967,
CC ECO:0000269|PubMed:17202189, ECO:0000269|PubMed:17663724,
CC ECO:0000269|PubMed:18715946, ECO:0000269|PubMed:18809723,
CC ECO:0000269|PubMed:18927149, ECO:0000269|PubMed:18981481,
CC ECO:0000269|PubMed:19582868, ECO:0000269|PubMed:19747829,
CC ECO:0000269|PubMed:7739543, ECO:0000269|PubMed:8306880,
CC ECO:0000269|PubMed:8655584}.
CC -!- SUBUNIT: Homodimer. Secreted homodimers form a complex with wnt5a
CC homodimers; tyrosine sulfation of both wnt11 and wnt5a by tpst1 is
CC required for this interaction. Interacts with the transmembrane
CC receptor fzd7/fz7. Interacts with lrp6 and ryk. Interacts with
CC tdgf1/frl1. Interacts weakly with frzb1 and strongly with
CC frzb2/crescent. Interaction with frzb2/crescent antagonizes wnt11
CC function in the neuroectoderm, but enhances it in mesodermal tissue.
CC {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:15797385,
CC ECO:0000269|PubMed:16274967, ECO:0000269|PubMed:17202189,
CC ECO:0000269|PubMed:18809723, ECO:0000269|PubMed:18927149,
CC ECO:0000269|PubMed:19747829}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:18927149,
CC ECO:0000269|PubMed:19747829, ECO:0000269|PubMed:19906850}.
CC -!- TISSUE SPECIFICITY: Transcripts are expressed ubiquitously in early
CC oocytes but become vegetally localized during mid-oogenesis then
CC enriched on the dorsal side by the 8 to 16 cell stage. The protein
CC becomes asymmetrically concentrated on the dorsal side by the 64-cell
CC stage. During gastrulation, expressed in the lateral and ventral
CC marginal zone, and during tadpole stages in the somites and first
CC branchial arch. Weakly expressed in the pronephros from at least stage
CC 12.5, with kidney expression increasing until stage 35. Expressed in
CC the prospective posterior gut between stages 13 and 20, and in the deep
CC foregut endoderm. Prior to neural crest cell migration, expressed in a
CC domain flanking the neural crest on the lateral or epidermal side (the
CC opposite side to wnt11/wnt11-r). {ECO:0000269|PubMed:10525335,
CC ECO:0000269|PubMed:10585568, ECO:0000269|PubMed:10769246,
CC ECO:0000269|PubMed:11128985, ECO:0000269|PubMed:11784070,
CC ECO:0000269|PubMed:12946266, ECO:0000269|PubMed:15543138,
CC ECO:0000269|PubMed:15797385, ECO:0000269|PubMed:15857909,
CC ECO:0000269|PubMed:16274967, ECO:0000269|PubMed:18981481,
CC ECO:0000269|PubMed:19582868, ECO:0000269|PubMed:7539356,
CC ECO:0000269|PubMed:8306880}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC oocytes and embryos through to swimming tadpole stages.
CC {ECO:0000269|PubMed:8306880}.
CC -!- INDUCTION: By t/xbra. By gata4 and gata6. Repressed by zbtb33/kaiso.
CC {ECO:0000269|PubMed:10769246, ECO:0000269|PubMed:10781937,
CC ECO:0000269|PubMed:11128985, ECO:0000269|PubMed:15543138,
CC ECO:0000269|PubMed:18715946}.
CC -!- PTM: Glycosylation is required for protein secretion.
CC {ECO:0000269|PubMed:19747829}.
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 wnt-11 (PubMed:8306880) but was renamed to wnt11b
CC (PubMed:17436276) after the discovery of wnt11r (now called wnt11).
CC {ECO:0000305|PubMed:17436276, ECO:0000305|PubMed:8306880}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: PubMed:11159911 show a lack of role in heart induction but
CC PubMed:12167861 show a role in heart formation; the discrepancy may be
CC due to duplication of Xenopus wnt11 genes. {ECO:0000305}.
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DR EMBL; L23542; AAA19697.1; -; mRNA.
DR EMBL; BC084745; AAH84745.1; -; mRNA.
DR PIR; I51572; I51572.
DR RefSeq; NP_001084327.1; NM_001090858.1.
DR AlphaFoldDB; P49893; -.
DR SMR; P49893; -.
DR IntAct; P49893; 1.
DR iPTMnet; P49893; -.
DR DNASU; 399441; -.
DR GeneID; 399441; -.
DR KEGG; xla:399441; -.
DR CTD; 399441; -.
DR Xenbase; XB-GENE-6079153; wnt11b.L.
DR OMA; CCYVVCK; -.
DR OrthoDB; 797177at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 399441; Expressed in gastrula and 7 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IPI:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0060914; P:heart formation; IMP: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; IMP:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:UniProtKB.
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; IDA: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; IMP: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:0062009; P:secondary palate development; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:UniProtKB.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
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; Gastrulation;
KW Glycoprotein; Lipoprotein; Reference proteome; Secreted; Signal; Sulfation;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..353
FT /note="Protein Wnt-11b"
FT /id="PRO_0000041470"
FT MOD_RES 274
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:19747829"
FT MOD_RES 281
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:19747829"
FT LIPID 214
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000269|PubMed:19747829"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19747829"
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 208..222
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 210..217
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 282..313
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 298..308
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 312..352
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 328..343
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 330..340
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 335..336
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT MUTAGEN 88
FT /note="N->Q: Loss of glycosylation. Prevents secretion. No
FT effect on wnt5a-binding."
FT /evidence="ECO:0000269|PubMed:19747829"
FT MUTAGEN 274
FT /note="Y->F: Loss of sulfation. No effect on secretion or
FT homodimerization but severely reduces interaction with
FT wnt5a and canonical Wnt signaling activity; when associated
FT with F-281."
FT /evidence="ECO:0000269|PubMed:19747829"
FT MUTAGEN 281
FT /note="Y->F: Loss of sulfation. No effect on secretion or
FT homodimerization but severely reduces interaction with
FT wnt5a and canonical Wnt signaling activity; when associated
FT with F-274."
FT /evidence="ECO:0000269|PubMed:19747829"
FT MUTAGEN 299
FT /note="N->Q: Loss of glycosylation. Prevents secretion. No
FT effect on wnt5a-binding."
FT /evidence="ECO:0000269|PubMed:19747829"
FT CONFLICT 257
FT /note="L -> H (in Ref. 1; AAA19697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38785 MW; B59609AB88915554 CRC64;
MAPTRHWVTP LLLLCCSGIC GAIQWLGLTV NGSRVAWNES EHCRLLDGLV PDQSQLCKRN
LELMQSVVNA AKQTKLTCQM TLSDMRWNCS SVENAPSFTP DLSKGTRESA FVYALASATL
SHTIARACAS GELPTCSCGA TPAEVPGTGF RWGGCGDNLH YGLNMGSAFV DAPMKSSKSA
GTQATKIMNL HNNAVGRQVL MDSLETKCKC HGVSGSCSVK TCWKGLQDLP HIANELKSKY
LGATKVIHRQ TGTRRQLVPR ELDIRPVRES ELVYLVSSPD YCTKNPKLGS YGTQDRLCNK
TSVGSDSCNL MCCGRGYNAY TETIVERCQC KYHWCCYVMC KKCERTVERY VCK
