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   24-JAN-2024, entry version 177.
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).
RN   [5]
RP   INDUCTION BY TNFSF11.
RX   PubMed=23478294; DOI=10.1038/cr.2013.33;
RA   Choi H.K., Kang H.R., Jung E., Kim T.E., Lin J.J., Lee S.Y.;
RT   "Early estrogen-induced gene 1, a novel RANK signaling component, is
RT   essential for osteoclastogenesis.";
RL   Cell Res. 23:524-536(2013).
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.
CC   -!- INDUCTION: Induced by TNFSF11/RANKL-stimulation of bone marrow-derived
CC       macrophages. {ECO:0000269|PubMed:23478294}.
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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.ENSMUSP00000150903; -.
DR   ChEMBL; CHEMBL3120042; -.
DR   GlyCosmos; Q05117; 2 sites, No reported glycans.
DR   GlyGen; Q05117; 2 sites.
DR   iPTMnet; Q05117; -.
DR   PhosphoSitePlus; Q05117; -.
DR   SwissPalm; Q05117; -.
DR   EPD; Q05117; -.
DR   jPOST; Q05117; -.
DR   MaxQB; Q05117; -.
DR   PaxDb; 10090-ENSMUSP00000127128; -.
DR   PeptideAtlas; Q05117; -.
DR   ProteomicsDB; 289727; -.
DR   Antibodypedia; 25921; 671 antibodies from 34 providers.
DR   DNASU; 11433; -.
DR   Ensembl; ENSMUST00000069330.14; ENSMUSP00000065425.7; ENSMUSG00000001348.16.
DR   Ensembl; ENSMUST00000115315.3; ENSMUSP00000110970.3; ENSMUSG00000001348.16.
DR   Ensembl; ENSMUST00000165735.9; ENSMUSP00000127128.2; ENSMUSG00000001348.16.
DR   Ensembl; ENSMUST00000213815.2; ENSMUSP00000149597.2; ENSMUSG00000001348.16.
DR   Ensembl; ENSMUST00000217643.2; ENSMUSP00000150903.2; ENSMUSG00000001348.16.
DR   GeneID; 11433; -.
DR   KEGG; mmu:11433; -.
DR   UCSC; uc009onz.1; mouse.
DR   AGR; MGI:87883; -.
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; 364192at2759; -.
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 79 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 195 other cell types or tissues.
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   PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   Genevisible; Q05117; MM.
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
//