PPA5_MOUSE
ID PPA5_MOUSE Reviewed; 327 AA.
AC Q05117;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Tartrate-resistant acid phosphatase type 5;
DE Short=TR-AP;
DE EC=3.1.3.2;
DE AltName: Full=Tartrate-resistant acid ATPase;
DE Short=TrATPase;
DE AltName: Full=Type 5 acid phosphatase;
DE Flags: Precursor;
GN Name=Acp5; Synonyms=T5ap, Trap;
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].
RX PubMed=8359686; DOI=10.1016/0378-1119(93)90420-8;
RA Cassady A.I., King A.G., Cross N.C.P., Hume D.A.;
RT "Isolation and characterization of the genes encoding mouse and human type-
RT 5 acid phosphatase.";
RL Gene 130:201-207(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC TISSUE=Spleen;
RX PubMed=8256664; DOI=10.1002/jbmr.5650081015;
RA Reddy S.V., Scarcez T., Windle J.J., Leach R.J., Hundley J.E.,
RA Chirgwin J.M., Chou J.Y., Roodman G.D.;
RT "Cloning and characterization of the 5'-flanking region of the mouse
RT tartrate-resistant acid phosphatase gene.";
RL J. Bone Miner. Res. 8:1263-1270(1993).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in the process of bone resorption. The
CC osteoclastic trap acts on nucleotide tri- and diphosphates with higher
CC affinity, compared with other substrates.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per subunit.;
CC -!- SUBUNIT: Exists either as monomer or, after proteolytic processing, as
CC a dimer of two chains linked by disulfide bond(s).
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Characteristic constituent of osteoclasts.
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DR EMBL; M99054; AAA37245.1; -; Genomic_DNA.
DR EMBL; BC012911; AAH12911.1; -; mRNA.
DR EMBL; BC019160; AAH19160.1; -; mRNA.
DR EMBL; BC029644; AAH29644.1; -; mRNA.
DR EMBL; M85212; AAA40479.1; -; Genomic_DNA.
DR CCDS; CCDS22923.1; -.
DR PIR; JN0787; JN0787.
DR RefSeq; NP_001095874.1; NM_001102404.1.
DR RefSeq; NP_001095875.1; NM_001102405.1.
DR RefSeq; NP_031414.1; NM_007388.3.
DR RefSeq; XP_006510007.1; XM_006509944.3.
DR RefSeq; XP_006510008.1; XM_006509945.2.
DR RefSeq; XP_006510009.1; XM_006509946.1.
DR RefSeq; XP_011240686.1; XM_011242384.2.
DR AlphaFoldDB; Q05117; -.
DR SMR; Q05117; -.
DR IntAct; Q05117; 1.
DR STRING; 10090.ENSMUSP00000127128; -.
DR ChEMBL; CHEMBL3120042; -.
DR GlyGen; Q05117; 2 sites.
DR iPTMnet; Q05117; -.
DR PhosphoSitePlus; Q05117; -.
DR EPD; Q05117; -.
DR jPOST; Q05117; -.
DR MaxQB; Q05117; -.
DR PaxDb; Q05117; -.
DR PeptideAtlas; Q05117; -.
DR PRIDE; Q05117; -.
DR ProteomicsDB; 289727; -.
DR Antibodypedia; 25921; 587 antibodies from 34 providers.
DR DNASU; 11433; -.
DR Ensembl; ENSMUST00000069330; ENSMUSP00000065425; ENSMUSG00000001348.
DR Ensembl; ENSMUST00000115315; ENSMUSP00000110970; ENSMUSG00000001348.
DR Ensembl; ENSMUST00000165735; ENSMUSP00000127128; ENSMUSG00000001348.
DR Ensembl; ENSMUST00000213815; ENSMUSP00000149597; ENSMUSG00000001348.
DR Ensembl; ENSMUST00000217643; ENSMUSP00000150903; ENSMUSG00000001348.
DR GeneID; 11433; -.
DR KEGG; mmu:11433; -.
DR UCSC; uc009onz.1; mouse.
DR CTD; 54; -.
DR MGI; MGI:87883; Acp5.
DR VEuPathDB; HostDB:ENSMUSG00000001348; -.
DR eggNOG; KOG2679; Eukaryota.
DR GeneTree; ENSGT00390000016735; -.
DR HOGENOM; CLU_043332_1_0_1; -.
DR InParanoid; Q05117; -.
DR OMA; VTVAIFM; -.
DR OrthoDB; 711825at2759; -.
DR PhylomeDB; Q05117; -.
DR TreeFam; TF313175; -.
DR BRENDA; 3.1.3.2; 3474.
DR Reactome; R-MMU-196843; Vitamin B2 (riboflavin) metabolism.
DR BioGRID-ORCS; 11433; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ssr4; mouse.
DR PRO; PR:Q05117; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q05117; protein.
DR Bgee; ENSMUSG00000001348; Expressed in diaphysis of femur and 192 other tissues.
DR Genevisible; Q05117; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:MGI.
DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0016311; P:dephosphorylation; IDA:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; IMP:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IMP:MGI.
DR CDD; cd07378; MPP_ACP5; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024927; Acid_PPase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Iron; Lysosome; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..327
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /id="PRO_0000023982"
FT BINDING 35
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..221
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 36807 MW; 6D3975C4EF714C56 CRC64;
MDSWVVLLGL QIIWLPLLTH GTAPTPTLRF VAVGDWGGVP NAPFHTAREM ANAKEIARTV
QTMGADFIMS LGDNFYFTGV HDASDKRFQE TFEDVFSDRA LRNIPWYVLA GNHDHLGNVS
AQIAYSKISK RWNFPSPYYR LRFKIPRTNI TVAIFMLDTV MLCGNSDDFA SQQPKMPRDL
GVARTQLSWL KKQLAAAKED YVLVAGHYPI WSIAEHGPTR CLVKNLRPLL ATYGVTAYLC
GHDHNLQYLQ DENGVGYVLS GAGNFMDPSV RHQRKVPNGY LRFHYGSEDS LGGFTHVEIS
PKEMTIIYVE ASGKSLFKTS LPRRPRP
