WNT8A_MOUSE
ID WNT8A_MOUSE Reviewed; 354 AA.
AC Q64527; E9QL90;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein Wnt-8a;
DE AltName: Full=Protein Wnt-8d;
DE AltName: Full=Stimulated by retinoic acid gene 11 protein;
DE Flags: Precursor;
GN Name=Wnt8a; Synonyms=Stra11, Wnt8d;
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 INDUCTION BY RETINOIC ACID.
RC TISSUE=Embryo;
RX PubMed=8887323; DOI=10.1016/s0925-4773(96)00569-2;
RA Bouillet P., Oulad-Abdelghani M., Ward S.J., Bronner S., Chambon P.,
RA Dolle P.;
RT "A new mouse member of the Wnt gene family, mWnt-8, is expressed during
RT early embryogenesis and is ectopically induced by retinoic acid.";
RL Mech. Dev. 58:141-152(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Plays a role in embryonic patterning.
CC {ECO:0000250|UniProtKB:P51028}.
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:Q9H1J5}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9H1J5}. Secreted
CC {ECO:0000250|UniProtKB:Q9H1J5}.
CC -!- DEVELOPMENTAL STAGE: Expression in early stages of embryogenesis.
CC Expression begins in the posterior region of early primitive streak-
CC stage embryos and after it spreads into the embryonic ectoderm up to a
CC sharp rostral boundary at the base of the developing headfolds.
CC Expressed transiently in the newly formed mesoderm. Expression is down-
CC regulated during somitogenesis. The expression is highly restricted
CC during gastrulation and neurulation, both temporally and spatially.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8887323}.
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 WNT8A. {ECO:0000250|UniProtKB:P28026}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; Z68889; CAA93117.1; -; mRNA.
DR EMBL; AC074335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29129.1; -.
DR RefSeq; NP_033316.1; NM_009290.2.
DR AlphaFoldDB; Q64527; -.
DR SMR; Q64527; -.
DR BioGRID; 203552; 2.
DR STRING; 10090.ENSMUSP00000012426; -.
DR GlyGen; Q64527; 2 sites.
DR PhosphoSitePlus; Q64527; -.
DR PaxDb; Q64527; -.
DR PRIDE; Q64527; -.
DR Antibodypedia; 26566; 226 antibodies from 31 providers.
DR DNASU; 20890; -.
DR Ensembl; ENSMUST00000012426; ENSMUSP00000012426; ENSMUSG00000012282.
DR GeneID; 20890; -.
DR KEGG; mmu:20890; -.
DR CTD; 7478; -.
DR MGI; MGI:107924; Wnt8a.
DR VEuPathDB; HostDB:ENSMUSG00000012282; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000157840; -.
DR HOGENOM; CLU_033039_1_2_1; -.
DR InParanoid; Q64527; -.
DR OMA; LVAKHFC; -.
DR OrthoDB; 618621at2759; -.
DR PhylomeDB; Q64527; -.
DR TreeFam; TF105310; -.
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 BioGRID-ORCS; 20890; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q64527; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q64527; protein.
DR Bgee; ENSMUSG00000012282; Expressed in primitive streak and 70 other tissues.
DR Genevisible; Q64527; 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:0048018; F:receptor ligand activity; ISO: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:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0048561; P:establishment of animal organ orientation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:MGI.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IMP:MGI.
DR GO; GO:0003002; P:regionalization; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0062009; P:secondary palate development; ISO:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR034312; Protein_Wnt-8A/8C.
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:SF92; PTHR12027:SF92; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..354
FT /note="Protein Wnt-8a"
FT /id="PRO_0000041449"
FT LIPID 186
FT /note="O-palmitoleoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..65
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 104..112
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 114..132
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 180..194
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 182..189
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 259..297
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 275..290
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 294..336
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 312..327
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 314..324
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 319..320
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 32
FT /note="R -> G (in Ref. 1; CAA93117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39573 MW; A91D5245F5B6FE65 CRC64;
MGHLLMLWVA AGMCYPALGA SAWSVNNFLI TRPKAYLTYT ASVALGAQIG IEECKFQFAW
ERWNCPEHAF QFSTHNRLRA ATRETSFIHA IRSAAIMYAV TKNCSMGDLE NCGCDESQNG
KTGGHGWIWG GCSDNVEFGE KISRLFVDSL EKGKDARALV NLHNNRAGRL AVRASTKRTC
KCHGISGSCS IQTCWLQLAD FRQMGNYLKA KYDRALKIEM DKRQLRAGNR AEGRWALTEA
FLPSTEAELI FLEGSPDYCN RNASLSIQGT EGRECLQNAR SASRREQRSC GRLCTECGLQ
VEERRAEAVS SCDCNFQWCC TVKCGQCRRV VSRYYCTRPV GSARPRGRGK DSAW
