WNT8B_MOUSE
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 03-AUG-2022, entry version 126.
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}.
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DR EMBL; AF130349; AAD31816.1; -; mRNA.
DR AlphaFoldDB; Q9WUD6; -.
DR SMR; Q9WUD6; -.
DR STRING; 10090.ENSMUSP00000042867; -.
DR GlyGen; Q9WUD6; 2 sites.
DR PhosphoSitePlus; Q9WUD6; -.
DR PaxDb; Q9WUD6; -.
DR PRIDE; Q9WUD6; -.
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; IPR034311; Protein_Wnt-8B.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013301; Wnt8.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF94; PTHR12027:SF94; 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
