W11B2_XENTR
ID W11B2_XENTR Reviewed; 353 AA.
AC Q28J82;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein Wnt-11b-2 {ECO:0000303|PubMed:17436276};
DE Flags: Precursor;
GN Name=wnt11b-2 {ECO:0000303|PubMed:17436276};
GN Synonyms=wnt11 {ECO:0000312|EMBL:CAJ82831.1},
GN wnt11b {ECO:0000312|Xenbase:XB-GENE-5858981}; ORFNames=TNeu076g04.1;
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:CAJ82831.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ82831.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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 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 induction
CC (By similarity). {ECO:0000250|UniProtKB:P49893}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P49893}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P49893}.
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 In addition, X.tropicalis has two very similar wnt11b genes suggesting
CC a further recent duplication event.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000255}.
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DR EMBL; CR760014; CAJ82831.1; -; mRNA.
DR RefSeq; NP_001016735.1; NM_001016735.2.
DR AlphaFoldDB; Q28J82; -.
DR SMR; Q28J82; -.
DR STRING; 8364.ENSXETP00000050201; -.
DR PaxDb; Q28J82; -.
DR GeneID; 549489; -.
DR KEGG; xtr:549489; -.
DR CTD; 549489; -.
DR Xenbase; XB-GENE-5858981; wnt11b.
DR eggNOG; KOG3913; Eukaryota.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; Q28J82; -.
DR OrthoDB; 797177at2759; -.
DR PhylomeDB; Q28J82; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000023227; Expressed in 4-cell stage embryo and 15 other tissues.
DR ExpressionAtlas; Q28J82; baseline.
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:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
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 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..353
FT /note="Protein Wnt-11b-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397209"
FT MOD_RES 274
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49893"
FT MOD_RES 281
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49893"
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:0000255"
FT CARBOHYD 299
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 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"
SQ SEQUENCE 353 AA; 38858 MW; F43C1FCAABB7166B CRC64;
MALIRHCVTL LLILCCSRLC GAIQWLGLTV NGSRVAWNES EHCRLLDGLV PEQSQLCKRN
LELMQSVVNA AKQAKLTCQM TFSDMRWNCS SVENAPNFTP DLSKGTRESA FVYALASATI
SHTIARACAS GELPTCSCGA TPAEVPGTGF RWGGCGDNLH YGLNMGSAFV DAPMKSSKSG
GTQATKMINL HNNAVGRQVL MDSLETKCKC HGVSGSCSVK TCWKGLQDLP HIANELKSKY
LGATKVIHRQ TGTRRQLVPR ELDIRPVRES ELVYLVSSPD YCAKNPKLGS YGTQDRVCNK
TSVGSDSCNL MCCGRGYNAY TETIVERCQC KYYWCCYVMC KKCERTVERY VCK
