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WNT16_MOUSE
ID   WNT16_MOUSE             Reviewed;         364 AA.
AC   Q9QYS1; Q14BF7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Protein Wnt-16;
DE   Flags: Precursor;
GN   Name=Wnt16;
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 [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=10500199; DOI=10.1073/pnas.96.20.11464;
RA   McWhirter J.R., Neuteboom S.T., Wancewicz E.V., Monia B.P., Downing J.R.,
RA   Murre C.;
RT   "Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT
RT   gene in pre-B acute lymphoblastoid leukemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11464-11469(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Probable developmental protein. May be a
CC       signaling molecule which affects the development of discrete regions of
CC       tissues. Is likely to signal over only few cell diameters (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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; AF172064; AAD49352.2; -; Genomic_DNA.
DR   EMBL; AF169964; AAD49352.2; JOINED; Genomic_DNA.
DR   EMBL; CH466533; EDL13846.1; -; Genomic_DNA.
DR   EMBL; BC115811; AAI15812.1; -; mRNA.
DR   EMBL; BC115925; AAI15926.1; -; mRNA.
DR   CCDS; CCDS19936.1; -.
DR   RefSeq; NP_444346.3; NM_053116.4.
DR   AlphaFoldDB; Q9QYS1; -.
DR   SMR; Q9QYS1; -.
DR   STRING; 10090.ENSMUSP00000031681; -.
DR   GlyGen; Q9QYS1; 3 sites.
DR   PhosphoSitePlus; Q9QYS1; -.
DR   PaxDb; Q9QYS1; -.
DR   PRIDE; Q9QYS1; -.
DR   ProteomicsDB; 297853; -.
DR   Antibodypedia; 17566; 216 antibodies from 31 providers.
DR   DNASU; 93735; -.
DR   Ensembl; ENSMUST00000031681; ENSMUSP00000031681; ENSMUSG00000029671.
DR   GeneID; 93735; -.
DR   KEGG; mmu:93735; -.
DR   UCSC; uc009bax.2; mouse.
DR   CTD; 51384; -.
DR   MGI; MGI:2136018; Wnt16.
DR   VEuPathDB; HostDB:ENSMUSG00000029671; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000157480; -.
DR   HOGENOM; CLU_033039_1_0_1; -.
DR   InParanoid; Q9QYS1; -.
DR   OMA; RGRECNR; -.
DR   OrthoDB; 745245at2759; -.
DR   PhylomeDB; Q9QYS1; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR   BioGRID-ORCS; 93735; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q9QYS1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QYS1; protein.
DR   Bgee; ENSMUSG00000029671; Expressed in secondary palatal shelf mesenchyme and 93 other tissues.
DR   ExpressionAtlas; Q9QYS1; baseline and differential.
DR   Genevisible; Q9QYS1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0046849; P:bone remodeling; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
DR   GO; GO:0043616; P:keratinocyte proliferation; ISO:MGI.
DR   GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0090403; P:oxidative stress-induced premature senescence; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR   GO; GO:0090399; P:replicative senescence; ISO:MGI.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013304; Wnt16.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01895; WNT16PROTEIN.
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..364
FT                   /note="Protein Wnt-16"
FT                   /id="PRO_0000041472"
FT   LIPID           226
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..92
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        138..146
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        148..167
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        220..234
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        222..229
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        293..324
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..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"
FT   CONFLICT        265
FT                   /note="K -> N (in Ref. 1; AAD49352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  40727 MW;  68A71C82DDE2D3A2 CRC64;
     MDRAALLALP SLCALWAAVL SLLPCGTQGN WMWLGIASFG VPEKLGCADL PLNSRQKELC
     KRKPYLLPSI REGARLGIQE CRSQFRHERW NCMVATTTST QLATAPLFGY ELSSGTKETA
     FIYAIMAAGL VHSVTRSCSA GNMTECSCDT TLQNGGSPSE GWHWGGCSDD VQYGMWFSRK
     FLDLPIRNTT GKESRVLLAM NLHNNEAGRQ AVAKLMSVDC RCHGVSGSCA VKTCWKTMSS
     FEKIGHFLKD KYENSIQISD KTKRKMRRRE KDQRQTPILK DDLLYVHKSP NYCVENKKLG
     IPGTQGRECN RTSGGADGCN LLCCGRGYNT HVVRHVERCE CKFIWCCYVR CRRCESMTDV
     HTCK
 
 
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