WNT5B_MOUSE
ID WNT5B_MOUSE Reviewed; 359 AA.
AC P22726; Q91XF5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein Wnt-5b;
DE Flags: Precursor;
GN Name=Wnt5b; Synonyms=Wnt-5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA Gavin B.J., McMahon J.A., McMahon A.P.;
RT "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT adult mouse development.";
RL Genes Dev. 4:2319-2332(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Liver, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH PORCN.
RX PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT "The evolutionarily conserved porcupine gene family is involved in the
RT processing of the Wnt family.";
RL Eur. J. Biochem. 267:4300-4311(2000).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Probable developmental protein. May be a
CC signaling molecule which affects the development of discrete regions of
CC tissues. Is likely to signal over only few cell diameters.
CC -!- SUBUNIT: Interacts with PORCN. {ECO:0000269|PubMed:10866835}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA40568.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M89799; AAA40568.1; ALT_INIT; mRNA.
DR EMBL; BC010775; AAH10775.1; ALT_INIT; mRNA.
DR EMBL; BC051406; AAH51406.1; -; mRNA.
DR CCDS; CCDS20474.2; -.
DR PIR; E36470; E36470.
DR RefSeq; NP_001258686.1; NM_001271757.1.
DR RefSeq; NP_001258687.1; NM_001271758.1.
DR RefSeq; NP_033551.2; NM_009525.3.
DR RefSeq; XP_006505987.1; XM_006505924.1.
DR AlphaFoldDB; P22726; -.
DR SMR; P22726; -.
DR BioGRID; 204578; 1.
DR STRING; 10090.ENSMUSP00000112448; -.
DR GlyGen; P22726; 4 sites.
DR iPTMnet; P22726; -.
DR PhosphoSitePlus; P22726; -.
DR MaxQB; P22726; -.
DR PaxDb; P22726; -.
DR PRIDE; P22726; -.
DR ProteomicsDB; 297855; -.
DR Antibodypedia; 10357; 249 antibodies from 30 providers.
DR DNASU; 22419; -.
DR Ensembl; ENSMUST00000117171; ENSMUSP00000113188; ENSMUSG00000030170.
DR Ensembl; ENSMUST00000178696; ENSMUSP00000137065; ENSMUSG00000030170.
DR GeneID; 22419; -.
DR KEGG; mmu:22419; -.
DR UCSC; uc009dmg.3; mouse.
DR CTD; 81029; -.
DR MGI; MGI:98959; Wnt5b.
DR VEuPathDB; HostDB:ENSMUSG00000030170; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000157617; -.
DR HOGENOM; CLU_033039_0_1_1; -.
DR InParanoid; P22726; -.
DR OMA; EHARMLM; -.
DR OrthoDB; 695671at2759; -.
DR PhylomeDB; P22726; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR BioGRID-ORCS; 22419; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Wnt5b; mouse.
DR PRO; PR:P22726; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P22726; protein.
DR Bgee; ENSMUSG00000030170; Expressed in urethra mesenchymal layer and 272 other tissues.
DR ExpressionAtlas; P22726; baseline and differential.
DR Genevisible; P22726; MM.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
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:0005102; F:signaling receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
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:0007267; P:cell-cell signaling; TAS:MGI.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1904105; P:positive regulation of convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IGI:MGI.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026537; Wnt5b.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF87; PTHR12027:SF87; 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; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..359
FT /note="Protein Wnt-5b"
FT /id="PRO_0000041435"
FT LIPID 223
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 133..141
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..161
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 217..231
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 219..226
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 288..319
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 304..314
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 318..358
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 336..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 341..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 359 AA; 40343 MW; 308ED393D3020DEB CRC64;
MPSLLLVVVA ALLSSWAQLL TDANSWWSLA LNPVQRPEMF IIGAQPVCSQ LPGLSPGQRK
LCQLYQEHMS YIGEGAKTGI RECQHQFRQR RWNCSTVDNT SVFGRVMQIG SRETAFTYAV
SAAGVVNAIS RACREGELST CGCSRAARPK DLPRDWLWGG CGDNVEYGYR FAKEFVDARE
REKNFAKGSE EQGRALMNLQ NNEAGRRAVY KMADVACKCH GVSGSCSLKT CWLQLAEFRK
VGDRLKEKYD SAAAMRITRQ GKLELANSRF NQPTPEDLVY VDPSPDYCLR NETTGSLGTQ
GRLCNKTSEG MDGCELMCCG RGYDRFKSVQ VERCHCRFHW CCFVRCKKCT EVVDQYVCK
