Tartrate-resistant acid phosphatase type 5 precursor

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P29288 (PPA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Domain	Signal
Ligand	Iron Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bone resorption Inferred from expression pattern PubMed 20069278. Source: RGD 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 zinc ion Inferred from expression pattern PubMed 19369052. Source: RGD
Cellular_component	extracellular space Inferred from direct assay PubMed 20003323. Source: RGD integral to membrane Traceable author statement PubMed 11890682. Source: RGD lysosome Traceable author statement PubMed 8127141. Source: RGD
Molecular_function	acid 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Ref.3

Chain

23 – 327

305

Tartrate-resistant acid phosphatase type 5

PRO_0000023985

Sites

Metal binding

Iron 1

Metal binding

Iron 1

Metal binding

Iron 2

Metal binding

Iron 1

Metal binding

112

Iron 2

Metal binding

207

Iron 2

Metal binding

242

Iron 2

Metal binding

244

Iron 1

Amino acid modifications

Glycosylation

118

N-linked (GlcNAc...)

Glycosylation

149

N-linked (GlcNAc...) Potential

Disulfide bond

163 ↔ 221

Secondary structure

327

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29288 [UniParc].

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

FASTA

327

36,726

        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' referencesShow '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.

IPI

IPI00202717.

PIR

A41720.

RefSeq

NP_001257818.1. NM_001270889.1.
NP_062017.2. NM_019144.2.

UniGene

Rn.171928.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QFC	X-ray	2.70	A	22-327	[»]
1QHW	X-ray	2.20	A	1-327	[»]

ProteinModelPortal

P29288.

SMR

P29288. Positions 26-325.

ModBase

Search...

Proteomic databases

PRIDE

P29288.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000075237; ENSRNOP00000066364; ENSRNOG00000046261.

GeneID

25732.

KEGG

rno:25732.

Organism-specific databases

CTD

54.

RGD

2022. Acp5.

Phylogenomic databases

GeneTree

ENSGT00390000016735.

HOVERGEN

HBG000433.

K14379.

Gene expression databases

Genevestigator

P29288.

Family and domain databases

InterPro

IPR024927. Acid_Pase_5.
IPR004843. Metallo_PEstase_dom.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PIRSF

PIRSF000898. Acid_Ptase_5. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P29288.

NextBio

607863.

PMAP-CutDB

P29288.

Entry information

Entry name

PPA5_RAT

Accession

Primary (citable) accession number: P29288

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents