WNT9A_MOUSE
ID WNT9A_MOUSE Reviewed; 365 AA.
AC Q8R5M2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein Wnt-9a;
DE AltName: Full=Protein Wnt-14;
DE Flags: Precursor;
GN Name=Wnt9a; Synonyms=Wnt14 {ECO:0000303|PubMed:11836627};
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], AND TISSUE SPECIFICITY.
RX PubMed=11836627;
RA Katoh M.;
RT "Molecular cloning and expression of mouse Wnt14, and structural comparison
RT between mouse Wnt14-Wnt3a gene cluster and human WNT14-WNT3A gene
RT cluster.";
RL Int. J. Mol. Med. 9:221-227(2002).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16818445; DOI=10.1242/dev.02471;
RA Spaeter D., Hill T.P., O'sullivan R.J., Gruber M., Conner D.A.,
RA Hartmann C.;
RT "Wnt9a signaling is required for joint integrity and regulation of Ihh
RT during chondrogenesis.";
RL Development 133:3039-3049(2006).
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 (By similarity). Required for normal
CC timing of IHH expression during embryonic bone development, normal
CC chondrocyte maturation and for normal bone mineralization during
CC embryonic bone development (PubMed:16818445). Plays a redundant role in
CC maintaining joint integrity (PubMed:16818445).
CC {ECO:0000250|UniProtKB:O42280, ECO:0000269|PubMed:16818445,
CC 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:O14904}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O14904}. Secreted
CC {ECO:0000250|UniProtKB:O14904}.
CC -!- TISSUE SPECIFICITY: Expressed in adult brain, lung, skeletal muscle,
CC heart, and 17-day embryo. {ECO:0000269|PubMed:11836627}.
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 -!- DISRUPTION PHENOTYPE: Mutant mice die during the first 12 hours after
CC birth. Heart, lung, liver, intestinal tract, kidney and brain appear
CC grossly normal, but the mice display skeletal abnormalities, with
CC slightly shortened long bones in their limbs. The region of bone
CC mineralization is reduced in scapula, humerus, ileum and femur.
CC Besides, hyoid bone and atlas are hypoplastic. In the scull, the
CC supraoccipital bone shows reduced mineralization, with increased
CC distance between the frontal bones. The basioccipital bone displays an
CC abnormal shape and is smaller than in wild-type. Ectopic cartilage
CC nodules are detected within the skull midline sutures. Ectopic
CC cartilaginous material is detected in the interfrontal and sagittal
CC suture regions between the frontal and parietal bones. In neonate
CC forelimbs, the synovial fold contains cells with a chondrocyte-like
CC appearance. Mutant mice display also partial joint fusions between the
CC navicular and intermediate cuneiform tarsal elements in the foot, and
CC between wrist carpal elements. {ECO:0000269|PubMed:16818445}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; AB072311; BAB84710.1; -; mRNA.
DR CCDS; CCDS36169.1; -.
DR RefSeq; NP_647459.1; NM_139298.2.
DR AlphaFoldDB; Q8R5M2; -.
DR SMR; Q8R5M2; -.
DR BioGRID; 229787; 3.
DR STRING; 10090.ENSMUSP00000000128; -.
DR GlyGen; Q8R5M2; 1 site.
DR iPTMnet; Q8R5M2; -.
DR PhosphoSitePlus; Q8R5M2; -.
DR MaxQB; Q8R5M2; -.
DR PaxDb; Q8R5M2; -.
DR PRIDE; Q8R5M2; -.
DR ProteomicsDB; 297562; -.
DR Antibodypedia; 2495; 243 antibodies from 29 providers.
DR DNASU; 216795; -.
DR Ensembl; ENSMUST00000108783; ENSMUSP00000104411; ENSMUSG00000000126.
DR GeneID; 216795; -.
DR KEGG; mmu:216795; -.
DR UCSC; uc007jdq.1; mouse.
DR CTD; 7483; -.
DR MGI; MGI:2446084; Wnt9a.
DR VEuPathDB; HostDB:ENSMUSG00000000126; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000159618; -.
DR HOGENOM; CLU_033039_2_0_1; -.
DR InParanoid; Q8R5M2; -.
DR OMA; AGRKCHR; -.
DR OrthoDB; 866763at2759; -.
DR PhylomeDB; Q8R5M2; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 216795; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8R5M2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R5M2; protein.
DR Bgee; ENSMUSG00000000126; Expressed in urethra and 195 other tissues.
DR ExpressionAtlas; Q8R5M2; baseline and differential.
DR Genevisible; Q8R5M2; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0048856; P:anatomical structure development; IGI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IDA:MGI.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IDA:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0061037; P:negative regulation of cartilage development; IDA:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013303; Wnt9a.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF75; PTHR12027:SF75; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01894; WNT14PROTEIN.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..365
FT /note="Protein Wnt-9a"
FT /id="PRO_0000041456"
FT REGION 254..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 221
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..104
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 141..149
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 151..168
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 215..229
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 217..224
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 299..324
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..319
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 323..363
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 339..354
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 341..351
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 346..347
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 365 AA; 40388 MW; C6EBBE1897D2FA8A CRC64;
MLDGSLLARW LAAAFGLTLL LAALRPSAAY FGLTGSEPLT ILPLTLETEA AAQAHYKACD
RLKLERKQRR MCRRDPGVAE TLVEAVSMSA LECQYQFRFE RWNCTLEGRY RASLLKRGFK
ETAFLYAISS AGLTHALAKA CSAGRMERCT CDEAPDLENR EAWQWGGCGD NLKYSSKFVK
EFLGRRSSKD LRARVDFHNN LVGVKVIKAG VETTCKCHGV SGSCTVRTCW RQLAPFHEVG
KHLKHKYETS LKVGSTTNEA TGEAGAISPP RGRASGSGGG DPLPRTPELV HLDDSPSFCL
AGRFSPGTAG RRCHREKNCE SICCGRGHNT QSRVVTRPCQ CQVRWCCYVE CRQCTQREEV
YTCKG
