WN10B_MOUSE
ID WN10B_MOUSE Reviewed; 389 AA.
AC P48614; P70702;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein Wnt-10b;
DE AltName: Full=Protein Wnt-12;
DE Flags: Precursor;
GN Name=Wnt10b; Synonyms=Wnt-10b, Wnt10, Wnt12;
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=Swiss Webster; TISSUE=Embryo;
RX PubMed=7892260; DOI=10.1073/pnas.92.6.2268;
RA Lee F.S., Lane T.F., Kuo A., Shackleford G.M., Leder P.;
RT "Insertional mutagenesis identifies a member of the Wnt gene family as a
RT candidate oncogene in the mammary epithelium of int-2/Fgf-3 transgenic
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2268-2272(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8682303; DOI=10.1016/0378-1119(96)00109-6;
RA Hardiman G., Albright S., Tsunoda J., McClanahan T., Lee F.;
RT "The mouse Wnt-10B gene isolated from helper T cells is widely expressed
RT and a possible oncogene in BR6 mouse mammary tumorigenesis.";
RL Gene 172:199-205(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Brain;
RX PubMed=8875992;
RA Wang J., Shackleford G.M.;
RT "Murine Wnt10a and Wnt10b: cloning and expression in developing limbs, face
RT and skin of embryos and in adults.";
RL Oncogene 13:1537-1544(1996).
RN [4]
RP REVIEW ON FUNCTION.
RX PubMed=21447090; DOI=10.1111/j.1748-1716.2011.02296.x;
RA Wend P., Wend K., Krum S.A., Miranda-Carboni G.A.;
RT "The role of WNT10B in physiology and disease.";
RL Acta Physiol. 204:34-51(2012).
CC -!- FUNCTION: Member of the Wnt ligand gene family that encodes for
CC secreted proteins, which activate the Wnt signaling cascade.
CC Specifically activates canonical Wnt/beta-catenin signaling and thus
CC triggers beta-catenin/LEF/TCF-mediated transcriptional programs.
CC Involved in signaling networks controlling stemness, pluripotency and
CC cell fate decisions. Acts in the immune system, mammary gland, adipose
CC tissue, bone and skin. {ECO:0000305|PubMed:21447090}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity. The
CC complex with AFM may represent the physiological form in body fluids.
CC {ECO:0000250|UniProtKB:O00744}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O00744}. Secreted
CC {ECO:0000250|UniProtKB:O00744}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P48614-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P48614-2; Sequence=VSP_006796;
CC -!- TISSUE SPECIFICITY: Expressed in embryos and in the mammary gland of
CC non-pregnant mice.
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; U20658; AAA80110.1; -; mRNA.
DR EMBL; U30464; AAA84399.1; -; mRNA.
DR EMBL; U61970; AAB08086.1; -; mRNA.
DR EMBL; U61971; AAB08087.1; -; mRNA.
DR CCDS; CCDS27806.1; -. [P48614-1]
DR PIR; A59393; A59392.
DR PIR; I49263; I49263.
DR RefSeq; NP_035848.1; NM_011718.2. [P48614-1]
DR RefSeq; XP_006520954.1; XM_006520891.3. [P48614-1]
DR RefSeq; XP_006520955.1; XM_006520892.3. [P48614-2]
DR AlphaFoldDB; P48614; -.
DR SMR; P48614; -.
DR BioGRID; 204569; 1.
DR STRING; 10090.ENSMUSP00000023732; -.
DR GlyGen; P48614; 2 sites.
DR iPTMnet; P48614; -.
DR PhosphoSitePlus; P48614; -.
DR PaxDb; P48614; -.
DR PRIDE; P48614; -.
DR Antibodypedia; 25755; 238 antibodies from 34 providers.
DR DNASU; 22410; -.
DR Ensembl; ENSMUST00000023732; ENSMUSP00000023732; ENSMUSG00000022996. [P48614-1]
DR Ensembl; ENSMUST00000166022; ENSMUSP00000131056; ENSMUSG00000022996. [P48614-1]
DR Ensembl; ENSMUST00000226610; ENSMUSP00000153817; ENSMUSG00000022996. [P48614-1]
DR Ensembl; ENSMUST00000226846; ENSMUSP00000154513; ENSMUSG00000022996. [P48614-2]
DR Ensembl; ENSMUST00000228594; ENSMUSP00000153930; ENSMUSG00000022996. [P48614-1]
DR GeneID; 22410; -.
DR KEGG; mmu:22410; -.
DR UCSC; uc007xns.2; mouse. [P48614-2]
DR UCSC; uc007xnt.2; mouse. [P48614-1]
DR CTD; 7480; -.
DR MGI; MGI:108061; Wnt10b.
DR VEuPathDB; HostDB:ENSMUSG00000022996; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160653; -.
DR HOGENOM; CLU_033039_1_3_1; -.
DR InParanoid; P48614; -.
DR OMA; GHNVLQQ; -.
DR OrthoDB; 1241694at2759; -.
DR PhylomeDB; P48614; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 22410; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Wnt10b; mouse.
DR PRO; PR:P48614; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P48614; protein.
DR Bgee; ENSMUSG00000022996; Expressed in prostate bud and 88 other tissues.
DR ExpressionAtlas; P48614; baseline and differential.
DR Genevisible; P48614; MM.
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; TAS:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR GO; GO:0060346; P:bone trabecula formation; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IDA:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0061196; P:fungiform papilla development; IMP:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IGI:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0048627; P:myoblast development; IMP:MGI.
DR GO; GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IMP:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:MGI.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:MGI.
DR GO; GO:0051885; P:positive regulation of timing of anagen; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0051246; P:regulation of protein metabolic process; IMP:MGI.
DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050909; P:sensory perception of taste; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
DR GO; GO:0030217; P:T cell differentiation; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013302; Wnt10.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01893; WNT10PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..389
FT /note="Protein Wnt-10b"
FT /id="PRO_0000041464"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00744"
FT LIPID 253
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 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 136..144
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 146..199
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 247..261
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 249..256
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 318..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..344
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 348..388
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 364..379
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 366..376
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 371..372
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 143..238
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8875992"
FT /id="VSP_006796"
SQ SEQUENCE 389 AA; 43119 MW; F990AB33B7C84633 CRC64;
MLEEPRSRPP PLGLAGLLFL ALFSRALSNE ILGLKLPGEP PLTANTVCLT LSGLSKRQLG
LCLRSPDVTA SALQGLHIAV HECQHQLRDQ RWNCSALEGG GRLPHHSAIL KRGFRESAFS
FSMLAAGVMH AVATACSLGK LVSCGCGWKG SGEQDRLRAK LLQLQALSRG KTFPISQPSP
VPGSVPSPGP QDTWEWGGCN HDMDFGEKFS RDFLDSREAP RDIQARMRIH NNRVGRQVVT
ENLKRKCKCH GTSGSCQFKT CWRAAPEFRA IGAALRERLS RAIFIDTHNR NSGAFQPRLR
PRRLSGELVY FEKSPDFCER DPTLGSPGTR GRACNKTSRL LDGCGSLCCG RGHNVLRQTR
VERCHCRFHW CCYVLCDECK VTEWVNVCK
