WNT11_COTJA
ID WNT11_COTJA Reviewed; 354 AA.
AC P51891;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein Wnt-11;
DE Flags: Precursor;
GN Name=WNT11; Synonyms=WNT-11;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mesoderm;
RX PubMed=9053328; DOI=10.1242/dev.124.2.525;
RA Eisenberg C.A., Gourdie R.G., Eisenberg L.M.;
RT "Wnt-11 is expressed in early avian mesoderm and required for the
RT differentiation of the quail mesoderm cell line QCE-6.";
RL Development 124:525-536(1997).
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, both limb and feather buds. Is likely to signal over only
CC few cell 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}.
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DR EMBL; X97549; CAA66151.1; -; mRNA.
DR RefSeq; XP_015707967.1; XM_015852481.1.
DR AlphaFoldDB; P51891; -.
DR SMR; P51891; -.
DR PRIDE; P51891; -.
DR GeneID; 107308524; -.
DR KEGG; cjo:107308524; -.
DR CTD; 7481; -.
DR OrthoDB; 797177at2759; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
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:0061101; P:neuroendocrine cell differentiation; ISS: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: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: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; IEA:UniProtKB-KW.
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; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..354
FT /note="Protein Wnt-11"
FT /id="PRO_0000041468"
FT LIPID 215
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..91
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 130..138
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 140..157
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 313..353
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; 39457 MW; DEC1202B974739B6 CRC64;
MKPSPQFLLA AFLSLILQTG ICYGIKWIAL SKTPSALALN QTQHCKQLEG LVVSQVQLCR
SNLELMQTII QAAREVIKTC RKTFSDMRWN CSSIELAPNY LLDLERGTRE SAFVYALSAA
AISHTIARAC TTGDLPGCSC GPIPGETPGP GYRWGGCADN LNYGLIMGSK FSDAPMKMKK
SGSQANKLMH LHNSEVGRQV LKASLEMKCK CHGVSGSCSI KTCWKGLQEL RDIALDLKNK
YLSATKVVHR PMGTRKYLVP KDIDIRPVKE TELIYLQSSP DFCMKNEKVG SHGTQDRQCN
KTSNGSDSCD LMCCGRGYNP YMDKVVERCH CKYHWCCYVT CKKCERTVER YVCK
