ID   WN10A_MOUSE             Reviewed;         417 AA.
AC   P70701;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Protein Wnt-10a;
DE   Flags: Precursor;
GN   Name=Wnt10a;
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   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary 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   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=28589954; DOI=10.1038/ncomms15397;
RA   Xu M., Horrell J., Snitow M., Cui J., Gochnauer H., Syrett C.M.,
RA   Kallish S., Seykora J.T., Liu F., Gaillard D., Katz J.P., Kaestner K.H.,
RA   Levin B., Mansfield C., Douglas J.E., Cowart B.J., Tordoff M., Liu F.,
RA   Zhu X., Barlow L.A., Rubin A.I., McGrath J.A., Morrisey E.E., Chu E.Y.,
RA   Millar S.E.;
RT   "WNT10A mutation causes ectodermal dysplasia by impairing progenitor cell
RT   proliferation and KLF4-mediated differentiation.";
RL   Nat. Commun. 8:15397-15397(2017).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors (Probable). Functions in the canonical
CC       Wnt/beta-catenin signaling pathway. Plays a role in normal ectoderm
CC       development. Required for normal tooth development. Required for normal
CC       postnatal development and maintenance of tongue papillae and sweat
CC       ducts. Required for normal proliferation of basal cells in tongue
CC       filiform papillae, plantar epithelium and sweat ducts. Required for
CC       normal expression of keratins in tongue papillae. Required for normal
CC       expression of KRT9 in foot plant epithelium. Required for normal hair
CC       follicle function. {ECO:0000269|PubMed:28589954, ECO:0000305}.
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:Q9GZT5}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q9GZT5}. Secreted
CC       {ECO:0000250|UniProtKB:Q9GZT5}.
CC   -!- TISSUE SPECIFICITY: Detected in foot plant epidermis, footpad
CC       epidermis, haired skin epidermis. Detected in adult epithelia,
CC       including filiform and fungiform papillae and sweat ducts. Detected in
CC       sweat gland myoepithelial cells, but not in sweat gland mesenchyme.
CC       {ECO:0000269|PubMed:28589954}.
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   ---------------------------------------------------------------------------
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; U61969; AAB08085.1; -; mRNA.
DR   EMBL; BC014737; AAH14737.1; -; mRNA.
DR   CCDS; CCDS15057.1; -.
DR   PIR; B59392; B59392.
DR   RefSeq; NP_033544.1; NM_009518.2.
DR   AlphaFoldDB; P70701; -.
DR   SMR; P70701; -.
DR   IntAct; P70701; 1.
DR   STRING; 10090.ENSMUSP00000006718; -.
DR   GlyCosmos; P70701; 2 sites, No reported glycans.
DR   GlyGen; P70701; 2 sites.
DR   iPTMnet; P70701; -.
DR   PhosphoSitePlus; P70701; -.
DR   PaxDb; 10090-ENSMUSP00000006718; -.
DR   ProteomicsDB; 299986; -.
DR   Antibodypedia; 2463; 231 antibodies from 35 providers.
DR   DNASU; 22409; -.
DR   Ensembl; ENSMUST00000006718.15; ENSMUSP00000006718.9; ENSMUSG00000026167.15.
DR   GeneID; 22409; -.
DR   KEGG; mmu:22409; -.
DR   UCSC; uc007bnf.2; mouse.
DR   AGR; MGI:108071; -.
DR   CTD; 80326; -.
DR   MGI; MGI:108071; Wnt10a.
DR   VEuPathDB; HostDB:ENSMUSG00000026167; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000160299; -.
DR   HOGENOM; CLU_033039_1_3_1; -.
DR   InParanoid; P70701; -.
DR   OMA; DAWEWGG; -.
DR   OrthoDB; 2874082at2759; -.
DR   PhylomeDB; P70701; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR   BioGRID-ORCS; 22409; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Wnt10a; mouse.
DR   PRO; PR:P70701; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P70701; Protein.
DR   Bgee; ENSMUSG00000026167; Expressed in calcareous tooth and 114 other cell types or tissues.
DR   ExpressionAtlas; P70701; baseline and differential.
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:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0048730; P:epidermis morphogenesis; ISO:MGI.
DR   GO; GO:0001942; P:hair follicle development; ISO:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; ISO:MGI.
DR   GO; GO:0014033; P:neural crest cell differentiation; IDA:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0042476; P:odontogenesis; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IDA:MGI.
DR   GO; GO:0048733; P:sebaceous gland development; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0043588; P:skin development; ISO:MGI.
DR   GO; GO:0043586; P:tongue development; ISO:MGI.
DR   CDD; cd19355; Wnt_Wnt10a; 1.
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:SF89; PROTEIN WNT-10A; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01893; WNT10PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; P70701; MM.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Phosphoprotein; Reference proteome; Secreted; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..417
FT                   /note="Protein Wnt-10a"
FT                   /id="PRO_0000041461"
FT   REGION          300..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O00744"
FT   LIPID           268
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..107
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        149..157
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        159..214
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        262..276
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        264..271
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        346..377
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        362..372
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        376..416
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        392..407
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        394..404
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        399..400
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   417 AA;  46454 MW;  048DEF5E4CB94284 CRC64;
     MGSAHPRPWL RLPQGPQPRP EFWALLFFLL LLAAAVPRSA PNDILGLRLP PEPVLNANTV
     CLTLPGLSRR QMEVCVRHPD VAASAIQGIQ IAIHECQHQF RDQRWNCSSL ETRNKVPYES
     PIFSRGFRES AFAYAIAAAG VVHAVSNACA LGKLKACGCD ASRRGDEEAF RRKLHRLQLD
     ALQRGKGLSH GVPEHPAILP ASPGLQDSWE WGGCSPDVGF GERFSKDFLD SREPHRDIHA
     RMRLHNNRVG RQAVMENMRR KCKCHGTSGS CQLKTCWQVT PEFRTVGALL RNRFHRATLI
     RPHNRNGGQL EPGPAGAPSP APGTPGLRRR ASHSDLVYFE KSPDFCEREP RLDSAGTVGR
     LCNKSSTGPD GCGSMCCGRG HNILRQTRSE RCHCRFHWCC FVVCEECRIT EWVSVCK
//