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 16-JUN-2009, entry version 77. 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=Acid phosphatase 5, tartrate resistant; DE Flags: Precursor; GN Name=Acp5; Synonyms=T5ap, Trap; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93366175; 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 RT type-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 RT project: 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 MEDLINE=94078828; PubMed=8256664; 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). CC -!- FUNCTION: May play a role in the process of bone resorption. The CC osteoclastic trap acts on nucleotide tri- and diphosphates with CC higher affinity, compared with other substrates. CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol + CC phosphate. CC -!- COFACTOR: Binds 2 iron ions per subunit. CC -!- SUBUNIT: Exists either as monomer or, after proteolytic CC processing, as a dimer of two chains linked by disulfide bond(s). CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- TISSUE SPECIFICITY: Characteristic constituent of osteoclasts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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 IPI; IPI00137491; -. DR PIR; JN0787; JN0787. DR RefSeq; NP_001095874.1; -. DR RefSeq; NP_001095875.1; -. DR RefSeq; NP_031414.1; -. DR UniGene; Mm.46354; -. DR HSSP; P29288; 1QHW. DR SMR; Q05117; 27-325. DR Ensembl; ENSMUSG00000001348; Mus musculus. DR GeneID; 11433; -. DR KEGG; mmu:11433; -. DR MGI; MGI:87883; Acp5. DR HOGENOM; Q05117; -. DR HOVERGEN; Q05117; -. DR OMA; Q05117; HDHAGNV. DR BRENDA; 3.1.3.2; 244. DR NextBio; 278720; -. DR ArrayExpress; Q05117; -. DR Bgee; Q05117; -. DR CleanEx; MM_ACP5; -. DR GermOnline; ENSMUSG00000001348; Mus musculus. DR GO; GO:0005764; C:lysosome; IMP:MGI. DR GO; GO:0003993; F:acid phosphatase activity; IDA:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI. DR GO; GO:0045453; P:bone resorption; IMP:MGI. DR GO; GO:0016311; P:dephosphorylation; IDA:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0034097; P:response to cytokine stimulus; IDA:MGI. DR InterPro; IPR004843; M-pesterase. DR Pfam; PF00149; Metallophos; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Hydrolase; Iron; Lysosome; KW Metal-binding; Signal. FT SIGNAL 1 22 By similarity. FT CHAIN 23 327 Tartrate-resistant acid phosphatase type FT 5. FT /FTId=PRO_0000023982. FT METAL 35 35 Iron 1 (By similarity). FT METAL 73 73 Iron 1 (By similarity). FT METAL 73 73 Iron 2 (By similarity). FT METAL 76 76 Iron 1 (By similarity). FT METAL 112 112 Iron 2 (By similarity). FT METAL 207 207 Iron 2 (By similarity). FT METAL 242 242 Iron 2 (By similarity). FT METAL 244 244 Iron 1 (By similarity). FT CARBOHYD 118 118 N-linked (GlcNAc...) (Potential). FT CARBOHYD 149 149 N-linked (GlcNAc...) (Potential). FT DISULFID 163 221 By similarity. 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 //