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PPAT_MOUSE
ID   PPAT_MOUSE              Reviewed;         425 AA.
AC   D3YTS9;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Testicular acid phosphatase {ECO:0000305};
DE            EC=3.1.3.2;
DE   AltName: Full=Acid phosphatase 4 {ECO:0000312|MGI:MGI:3644563};
DE   Flags: Precursor;
GN   Name=Acp4 {ECO:0000312|MGI:MGI:3644563};
GN   Synonyms=Acpt {ECO:0000312|MGI:MGI:3644563};
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 [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).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=27843125; DOI=10.1016/j.ajhg.2016.09.018;
RA   Seymen F., Kim Y.J., Lee Y.J., Kang J., Kim T.H., Choi H., Koruyucu M.,
RA   Kasimoglu Y., Tuna E.B., Gencay K., Shin T.J., Hyun H.K., Kim Y.J.,
RA   Lee S.H., Lee Z.H., Zhang H., Hu J.C., Simmer J.P., Cho E.S., Kim J.W.;
RT   "Recessive mutations in ACPT, encoding testicular acid phosphatase, cause
RT   hypoplastic amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 99:1199-1205(2016).
CC   -!- FUNCTION: May dephosphorylate receptor tyrosine-protein kinase ERBB4
CC       and inhibits its ligand-induced proteolytic cleavage. May play a role
CC       in odontogenesis. {ECO:0000250|UniProtKB:Q9BZG2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BZG2}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: In the developing tooth from 8-day-old mice it is
CC       expressed in secretory-stage ameloblasts, follicular cells,
CC       odontoblasts, and osteoblasts (at protein level).
CC       {ECO:0000269|PubMed:27843125}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9BZG2}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AC152939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS57546.1; -.
DR   RefSeq; NP_001181963.1; NM_001195034.1.
DR   AlphaFoldDB; D3YTS9; -.
DR   SMR; D3YTS9; -.
DR   STRING; 10090.ENSMUSP00000103578; -.
DR   iPTMnet; D3YTS9; -.
DR   PhosphoSitePlus; D3YTS9; -.
DR   PaxDb; D3YTS9; -.
DR   PRIDE; D3YTS9; -.
DR   Antibodypedia; 32366; 81 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000118216; ENSMUSP00000112922; ENSMUSG00000012777.
DR   GeneID; 100503991; -.
DR   KEGG; mmu:100503991; -.
DR   CTD; 93650; -.
DR   MGI; MGI:3644563; Acp4.
DR   VEuPathDB; HostDB:ENSMUSG00000012777; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000161433; -.
DR   HOGENOM; CLU_030431_1_1_1; -.
DR   OMA; PCHGSRE; -.
DR   OrthoDB; 1221585at2759; -.
DR   BioGRID-ORCS; 100503991; 5 hits in 71 CRISPR screens.
DR   PRO; PR:D3YTS9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; D3YTS9; protein.
DR   Bgee; ENSMUSG00000012777; Expressed in testis and 26 other tissues.
DR   ExpressionAtlas; D3YTS9; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR   GO; GO:0120154; P:negative regulation of ERBB4 signaling pathway; ISS:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0010955; P:negative regulation of protein processing; ISS:UniProtKB.
DR   GO; GO:0042476; P:odontogenesis; ISS:UniProtKB.
DR   GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..425
FT                   /note="Testicular acid phosphatase"
FT                   /id="PRO_5006722351"
FT   TOPO_DOM        28..392
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   ACT_SITE        288
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   DISULFID        158..378
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   DISULFID        213..311
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   DISULFID        353..357
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
SQ   SEQUENCE   425 AA;  46405 MW;  487B981362A49E97 CRC64;
     MAEPGSQGHT VGPLLLLLLL LLPRALPEGP LLFVALVFRH GDRAPLASYP TDPHKEAAST
     LWPRGLGQLT KEGIRQQLEL GRFLRRRYKA FLSPEYKREE VYIRSTDFDR TLESAQANLA
     GLFPEAAPGS PETDWKPIPV HTVPVSEDKL LRFPMRSCPR YHELLRESTE AADYQEALEG
     WTDFLTRLGN FTGLSLVGEP LRRAWKVLDT LICQRAHGLD LPSWASPDVL RTLSQISALD
     IRAHVGPPRA AEKAQLTGGI LLDAILSNFS RTQRLGLPLK MVMYSAHDST LLALQGALGL
     YDGNTPPYAA CMAFEFRGSS REPEEEDGEN VTVSLIYRND TSRPPLPLRV PGCPAPCPLG
     RFQQLTAPAR PPAHGAPCHG SYEPASPPAT VPLLAGAVAV LAVLSLGLGL LAWRPRCLRA
     LGGTV
 
 
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