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UniProtKB/Swiss-Prot entry P29288


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPA5_RAT
Primary accession number P29288
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Tartrate-resistant acid phosphatase type 5 [Precursor]
Synonyms TR-AP
EC 3.1.3.2
Tartrate-resistant acid ATPase
TrATPase
Acid phosphatase 5, tartrate resistant
Gene name
Name: Acp5
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone;
PubMed=1722212 [NCBI, ExPASy, EBI, Israel, Japan]
Ek-Rylander B., Bill P., Norgaard M., Nilsson S., Andersson G.;
"Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone.";
J. Biol. Chem. 266:24684-24689(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 23-42.
PubMed=1830446 [NCBI, ExPASy, EBI, Israel, Japan]
Ek-Rylander B., Bergman T., Andersson G.;
"Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: hydrodynamic properties and N-terminal amino acid sequence.";
J. Bone Miner. Res. 6:365-373(1991).
[4]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-327.
DOI=10.1006/jmbi.1999.2896; PubMed=10388567 [NCBI, ExPASy, EBI, Israel, Japan]
Uppenberg J., Lindqvist F., Svensson C., Ek-Rylander B., Andersson G.;
"Crystal structure of a mammalian purple acid phosphatase.";
J. Mol. Biol. 290:201-211(1999).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1006/jmbi.1999.2962; PubMed=10438611 [NCBI, ExPASy, EBI, Israel, Japan]
Lindqvist Y., Johansson E., Kaija H., Vihko P., Schneider G.;
"Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a gamma-(hydr)oxo bridged di-iron center.";
J. Mol. Biol. 291:135-147(1999).
Comments
  • FUNCTION: May play a role in the process of bone resorption. The osteoclastic trap acts on nucleotide tri- and diphosphates with higher affinity, compared with other substrates.
  • CATALYTIC ACTIVITY: A phosphate monoester + H2O = an alcohol + phosphate.
  • COFACTOR: Binds 2 iron ions per subunit.
  • SUBUNIT: Exists either as monomer or, after proteolytic processing, as a dimer of two chains linked by disulfide bond(s).
  • SUBCELLULAR LOCATION: Lysosome.
  • TISSUE SPECIFICITY: Characteristic constituent of osteoclasts and some mononuclear preosteoclasts. Preferentially expressed in skeletal tissues.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M76110; AAA42305.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078847; AAH78847.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41720; A41720.
RefSeq NP_062017.1; -.
UniGene Rn.171928
3D structure databases
PDB
1QFC; X-ray; 2.70 A; A=22-327.[ExPASy / RCSB / EBI]
1QHW; X-ray; 2.20 A; A=1-327.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QFC; -.
1QHW; -.
ModBase P29288.
Organism-specific databases
RGD 2022; Acp5.
Ontologies
GO
GO:0005764; Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0003993; Molecular function: acid phosphatase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004843; M-pesterase.
Graphical view of domain structure.
Pfam PF00149; Metallophos; 1.
Pfam graphical view of domain structure.
BLOCKS P29288.
ProtoNet P29288.
Genome annotation databases
GeneID 25732; -.
KEGG rno:25732; -.
Phylogenomic databases
HOVERGEN P29288; -.
Other
NextBio 607863; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Iron; Lysosome; Metal-binding; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   327  305     Tartrate-resistant acid phosphatase type 5. PRO_0000023985
METAL   35    35        Iron 1. 
METAL   73    73        Iron 1. 
METAL   73    73        Iron 2. 
METAL   76    76        Iron 1. 
METAL   112   112        Iron 2. 
METAL   207   207        Iron 2. 
METAL   242   242        Iron 2. 
METAL   244   244        Iron 1. 
CARBOHYD   118   118        N-linked (GlcNAc...). 
CARBOHYD   149   149        N-linked (GlcNAc...) (Potential). 
DISULFID   163   221         
STRAND   28    33  6      
HELIX   47    63  17      
STRAND   66    70  5      
TURN   76    78  3      
HELIX   87    90  4      
TURN   91    95  5      
HELIX   99   101  3      
HELIX   114   116  3      
HELIX   119   124  6      
HELIX   125   127  3      
STRAND   130   133  4      
STRAND   136   144  9      
STRAND   146   148  3      
STRAND   151   156  6      
HELIX   159   163  5      
HELIX   166   168  3      
HELIX   180   194  15      
STRAND   200   205  6      
STRAND   214   216  3      
HELIX   220   225  6      
HELIX   227   233  7      
STRAND   237   240  4      
STRAND   242   250  9      
STRAND   256   260  5      
HELIX   273   275  3      
STRAND   281   285  5      
STRAND   293   299  7      
STRAND   301   310  10      
STRAND   315   322  8      
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 36726 Da [This is the MW of the unprocessed precursor] CRC64: 5121A66A635ED854 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDTWMVLLGL QILLLPLLAH CTAPASTLRF VAVGDWGGVP NAPFHTAREM ANAKEIARTV 

        70         80         90        100        110        120 
QIMGADFIMS LGDNFYFTGV HDANDKRFQE TFEDVFSDRA LRNIPWYVLA GNHDHLGNVS 

       130        140        150        160        170        180 
AQIAYSKISK RWNFPSPYYR LRFKVPRSNI TVAIFMLDTV MLCGNSDDFV SQQPEMPRDL 

       190        200        210        220        230        240 
GVARTQLSWL KKQLAAAKED YVLVAGHYPI WSIAEHGPTR CLVKNLRPLL AAYGVTAYLC 

       250        260        270        280        290        300 
GHDHNLQYLQ DENGVGYVLS GAGNFMDPSV RHQRKVPNGY LRFHYGSEDS LGGFTYVEIG 

       310        320 
SKEMSITYVE ASGKSLFKTS LPRRPRP 

P29288 in FASTA format

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