ID WNT8B_MOUSE Reviewed; 350 AA. AC Q9WUD6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 24-JAN-2024, entry version 133. DE RecName: Full=Protein Wnt-8b; DE Flags: Precursor; GN Name=Wnt8b; 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]. RC STRAIN=C57BL/6J; RX PubMed=10441746; DOI=10.1007/s003359901115; RA Richardson M., Redmond D., Watson C.J., Mason J.O.; RT "Mouse Wnt8B is expressed in the developing forebrain and maps to RT chromosome 19."; RL Mamm. Genome 10:923-925(1999). CC -!- FUNCTION: Ligand for members of the frizzled family of seven CC transmembrane receptors. May play an important role in the development CC and differentiation of certain forebrain structures, notably the CC hippocampus. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled CC receptors (By similarity). Depalmitoleoylation leads to Wnt signaling CC pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026, CC ECO:0000250|UniProtKB:P56704}. CC -!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and CC formation of large disulfide-bond oligomers, leading to inactivation of CC WNT8B. {ECO:0000250|UniProtKB:P28026}. 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; AF130349; AAD31816.1; -; mRNA. DR CCDS; CCDS50446.1; -. DR RefSeq; NP_035850.2; NM_011720.3. DR AlphaFoldDB; Q9WUD6; -. DR SMR; Q9WUD6; -. DR STRING; 10090.ENSMUSP00000042867; -. DR GlyCosmos; Q9WUD6; 2 sites, No reported glycans. DR GlyGen; Q9WUD6; 2 sites. DR PhosphoSitePlus; Q9WUD6; -. DR PaxDb; 10090-ENSMUSP00000042867; -. DR GeneID; 22423; -. DR KEGG; mmu:22423; -. DR AGR; MGI:109485; -. DR CTD; 7479; -. DR MGI; MGI:109485; Wnt8b. DR eggNOG; KOG3913; Eukaryota. DR InParanoid; Q9WUD6; -. DR PhylomeDB; Q9WUD6; -. DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking. DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR PRO; PR:Q9WUD6; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9WUD6; Protein. 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:0048018; F:receptor ligand activity; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; TAS:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; TAS:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0007165; P:signal transduction; TAS:MGI. DR Gene3D; 3.30.2460.20; -; 1. DR InterPro; IPR005817; Wnt. DR InterPro; IPR013301; Wnt8. DR InterPro; IPR043158; Wnt_C. DR InterPro; IPR018161; Wnt_CS. DR PANTHER; PTHR12027:SF94; PROTEIN WNT-8B; 1. DR PANTHER; PTHR12027; WNT RELATED; 1. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01892; WNT8PROTEIN. 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..21 FT /evidence="ECO:0000255" FT CHAIN 22..350 FT /note="Protein Wnt-8b" FT /id="PRO_0000041451" FT LIPID 185 FT /note="O-palmitoleoyl serine" FT /evidence="ECO:0000250|UniProtKB:P28026" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 258 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 53..64 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 103..111 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 113..131 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 179..193 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 181..188 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 255..293 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 271..286 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 290..332 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 308..323 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 310..320 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 315..316 FT /evidence="ECO:0000250|UniProtKB:P28026" SQ SEQUENCE 350 AA; 38576 MW; 69CEE7790461597A CRC64; MFLMKPVCVL LVTCVLHRSH AWSVNNFLMT GPKAYLVYSS SVAAGAQSGI EECKYQFAWD RWNCPERALQ LSSHGGLRSA NRETAFVHAI SSAGVMYTLT RNCSLGDFDN CGCDDSRNGQ LGGQGWLWGG CSDNVGFGEA ISKQFVDALE TGQDARAAMN LHNNEAGRKA VKGTMKRTCK CHGVSGSCTT QTCWLQLPEF REVGAHLKEK YHAALKVDLL QGAGNSAAGR GAIADTFRSI STRELVHLED SPDYCLENKT LGLLGTEGRE CLRRGRALGR WERRSCRRLC GDCGLAVEER RAETVSSCNC KFHWCCAVRC EQCRRRVTKY FCSRAERPPR GAAHKPGKNS //