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P29288 (PPA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tartrate-resistant acid phosphatase type 5

Short name=TR-AP
EC=3.1.3.2
Alternative name(s):
Tartrate-resistant acid ATPase
Short name=TrATPase
Type 5 acid phosphatase
Gene names
Name:Acp5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandIron
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from expression pattern PubMed 20069278. Source: RGD

dephosphorylation

Inferred from direct assay PubMed 19854170. Source: GOC

metabolic process

Inferred from direct assay PubMed 11890682. Source: GOC

multicellular organismal response to stress

Inferred from expression pattern PubMed 19113077. Source: RGD

negative regulation of cell adhesion

Inferred from direct assay PubMed 19854170. Source: RGD

ossification

Inferred from expression pattern PubMed 19403161. Source: RGD

osteoclast differentiation

Inferred from expression pattern PubMed 19361364. Source: RGD

positive regulation of cell migration

Inferred from mutant phenotype PubMed 19854170. Source: RGD

response to L-ascorbic acid

Inferred from expression pattern PubMed 19110235. Source: RGD

response to cholesterol

Inferred from expression pattern PubMed 19110235. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 19264158. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 19369052. Source: RGD

   Cellular_componentextracellular space

Inferred from direct assay PubMed 20003323. Source: RGD

integral component of membrane

Traceable author statement PubMed 11890682. Source: RGD

lysosome

Traceable author statement PubMed 8127141. Source: RGD

   Molecular_functionacid phosphatase activity

Inferred from direct assay PubMed 19854170. Source: RGD

ferric iron binding

Inferred from sequence or structural similarity. Source: UniProtKB

ferrous iron binding

Inferred from sequence or structural similarity. Source: UniProtKB

hydrolase activity

Inferred from direct assay PubMed 11890682. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.3
Chain23 – 327305Tartrate-resistant acid phosphatase type 5
PRO_0000023985

Sites

Metal binding351Iron 1
Metal binding731Iron 1
Metal binding731Iron 2
Metal binding761Iron 1
Metal binding1121Iron 2
Metal binding2071Iron 2
Metal binding2421Iron 2
Metal binding2441Iron 1

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...)
Glycosylation1491N-linked (GlcNAc...) Potential
Disulfide bond163 ↔ 221

Secondary structure

............................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29288 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 5121A66A635ED854

FASTA32736,726
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone."
Ek-Rylander B., Bill P., Norgaard M., Nilsson S., Andersson G.
J. Biol. Chem. 266:24684-24689(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: hydrodynamic properties and N-terminal amino acid sequence."
Ek-Rylander B., Bergman T., Andersson G.
J. Bone Miner. Res. 6:365-373(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-42.
[4]"Crystal structure of a mammalian purple acid phosphatase."
Uppenberg J., Lindqvist F., Svensson C., Ek-Rylander B., Andersson G.
J. Mol. Biol. 290:201-211(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-327.
[5]"Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a gamma-(hydr)oxo bridged di-iron center."
Lindqvist Y., Johansson E., Kaija H., Vihko P., Schneider G.
J. Mol. Biol. 291:135-147(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76110 mRNA. Translation: AAA42305.1.
BC078847 mRNA. Translation: AAH78847.1.
PIRA41720.
RefSeqNP_001257818.1. NM_001270889.1.
NP_062017.2. NM_019144.2.
XP_006242754.1. XM_006242692.1.
XP_006242755.1. XM_006242693.1.
XP_006242756.1. XM_006242694.1.
UniGeneRn.171928.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFCX-ray2.70A22-327[»]
1QHWX-ray2.20A1-327[»]
ProteinModelPortalP29288.
SMRP29288. Positions 26-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP29288. 1 interaction.
MINTMINT-8283229.

Proteomic databases

PRIDEP29288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000075237; ENSRNOP00000066364; ENSRNOG00000046261.
GeneID25732.
KEGGrno:25732.

Organism-specific databases

CTD54.
RGD2022. Acp5.

Phylogenomic databases

GeneTreeENSGT00390000016735.
HOVERGENHBG000433.
KOK14379.
OMAGEEMDIN.
OrthoDBEOG7WHH9R.
PhylomeDBP29288.

Gene expression databases

ArrayExpressP29288.
GenevestigatorP29288.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR024927. Acid_Pase_5.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF000898. Acid_Ptase_5. 1 hit.
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP29288.
NextBio607863.
PMAP-CutDBP29288.
PROP29288.

Entry information

Entry namePPA5_RAT
AccessionPrimary (citable) accession number: P29288
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references