ID WNT11_DANRE Reviewed; 354 AA.
AC O73864;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Protein Wnt-11;
DE Flags: Precursor;
GN Name=wnt11; Synonyms=wnt-11;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9507106; DOI=10.1016/s0925-4773(98)00013-6;
RA Makita R., Mizuno T., Kuroiwa A., Koshida S., Takeda H.;
RT "Zebrafish wnt11: pattern and regulation of the expression by the yolk cell
RT and no tail activity.";
RL Mech. Dev. 71:165-176(1998).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. May play a role in the formation of dermal
CC structure in limb buds. Is likely to signal over only few cell
CC diameters (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
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 -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF067429; AAC17922.1; -; mRNA.
DR AlphaFoldDB; O73864; -.
DR SMR; O73864; -.
DR STRING; 7955.ENSDARP00000012233; -.
DR GlyCosmos; O73864; 4 sites, No reported glycans.
DR PaxDb; 7955-ENSDARP00000012233; -.
DR AGR; ZFIN:ZDB-GENE-990603-12; -.
DR ZFIN; ZDB-GENE-990603-12; wnt11f2.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; O73864; -.
DR PhylomeDB; O73864; -.
DR PRO; PR:O73864; -.
DR Proteomes; UP000000437; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
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:0046982; F:protein heterodimerization activity; IPI:ZFIN.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
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:0016477; P:cell migration; IMP:ZFIN.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:ZFIN.
DR GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0060026; P:convergent extension; IGI:ZFIN.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:ZFIN.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IMP:ZFIN.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
DR GO; GO:0060898; P:eye field cell fate commitment involved in camera-type eye formation; IMP:ZFIN.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IGI:ZFIN.
DR GO; GO:0070121; P:Kupffer's vesicle development; IGI:ZFIN.
DR GO; GO:0060031; P:mediolateral intercalation; IMP:ZFIN.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:ZFIN.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:ZFIN.
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 DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0001839; P:neural plate morphogenesis; IMP:ZFIN.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:ZFIN.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; 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:0008104; P:protein localization; IGI:ZFIN.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:ZFIN.
DR GO; GO:0062009; P:secondary palate development; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR CDD; cd19343; Wnt_Wnt11; 1.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027:SF34; PROTEIN WNT; 1.
DR PANTHER; PTHR12027; WNT RELATED; 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; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..354
FT /note="Protein Wnt-11"
FT /id="PRO_0000041469"
FT LIPID 215
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..137
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 139..156
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 209..223
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 211..218
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 283..314
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 299..309
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..344
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..341
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 336..337
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 354 AA; 39150 MW; D17615E576510A4C CRC64;
MTEYRNFLLL FITSLSVIYP CTGISWLGLT INGSSVGWNQ THHCKLLDGL VPDQQQLCKR
NLELMHSIVR AARLTKSACT SSFSDMRWNW SSIESAPHFT PDLAKGTREA AFVVSLAAAV
VSHAIARACA SGDLPSCSCA AMPSEQAAPD FRWGGCGDNL RYYGLQMGSA FSDAPMRNRR
SGPQDFRLMQ LHNNAVGRQV LMDSLEMKCK CHGVSGSCSV KTCWKGLQDI STISADLKSK
YLSATKVIPR QIGTRRQLVP REMEVRPVGE NELVYLVSSP DYCTQNAKQG SLGTTDRQCN
KTASGSESCG LMCCGRGYNA YTEVLVERCQ CKYHWCCYVS CKTCKRTVER YVSK
//
