Reviewed, UniProtKB/Swiss-Prot P29288 (PPA5_RAT)

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
    Acid phosphatase 5, tartrate resistant

Gene names

Name:

Acp5

Organism

Rattus norvegicus (Rat)

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 Direct protein sequencing
Gene Ontology (GO)
Biological process	bone resorption Ref.1 Traceable author statement. Source: RGD
Cellular component	integral to membrane Traceable author statement. Source: RGD lysosome Traceable author statement. Source: RGD
Molecular function	acid phosphatase activity Traceable author statement. Source: RGD iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.3

Chain

23 – 327

305

Tartrate-resistant acid phosphatase type 5

PRO_0000023985

Sites

Metal binding

35

1

Iron 1

Metal binding

73

1

Iron 1

Metal binding

73

1

Iron 2

Metal binding

76

1

Iron 1

Metal binding

112

1

Iron 2

Metal binding

207

1

Iron 2

Metal binding

242

1

Iron 2

Metal binding

244

1

Iron 1

Amino acid modifications

Glycosylation

118

1

N-linked (GlcNAc...)

Glycosylation

149

1

N-linked (GlcNAc...) Potential

Disulfide bond

163 ↔ 221

Secondary structure

1

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327

Helix Strand Turn

Details...

Beta strand

28 – 33

6

Helix

47 – 63

17

Beta 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

Beta strand

130 – 133

4

Beta strand

136 – 144

9

Beta strand

146 – 148

3

Beta strand

151 – 156

6

Helix

159 – 163

5

Helix

166 – 168

3

Helix

180 – 194

15

Beta strand

200 – 205

6

Beta strand

214 – 216

3

Helix

220 – 225

6

Helix

227 – 233

7

Beta strand

237 – 240

4

Beta strand

242 – 250

9

Beta strand

256 – 260

5

Helix

273 – 275

3

Beta strand

281 – 285

5

Beta strand

293 – 299

7

Beta strand

301 – 310

10

Beta strand

315 – 322

8

Sequences

	Sequence		Length	Mass (Da)
	P29288-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 5121A66A635ED854	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

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: 1722212] [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: 15489334] [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: 1830446] [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: 10388567] [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: 10438611] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M76110 mRNA. Translation: AAA42305.1.
BC078847 mRNA. Translation: AAH78847.1.

IPI

IPI00202717.

PIR

A41720.

RefSeq

NP_062017.1.

UniGene

Rn.171928

3D structure databases

PDBPDBe

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

ModBase

Search...

Genome annotation databases

GeneID

25732.

KEGG

rno:25732.

Organism-specific databases

RGD

2022. Acp5.

Phylogenomic databases

HOVERGEN

P29288.

Enzyme and pathway databases

BRENDA

3.1.3.2. 248.

Family and domain databases

InterPro

IPR004843. M-pesterase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)