Reviewed, UniProtKB/Swiss-Prot P13686 (PPA5_HUMAN)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	325 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)

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). Ref.8 Ref.11
Subcellular location	Lysosome.
Involvement in disease	This relatively minor intracellular isozyme of acid phosphatase can become the dominant isozyme in certain pathological states (Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias).
Sequence similarities	Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Iron Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytosol Ref.7 Inferred from Experiment. Source: Reactome integral to membrane Ref.2 Traceable author statement. Source: ProtInc lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acid phosphatase activity Ref.6 Ref.7 Inferred from Experiment. Source: Reactome 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 – 21

21

Ref.8 Ref.7 Ref.9 Ref.10

Chain

22 – 325

304

Tartrate-resistant acid phosphatase type 5

PRO_0000023981

Sites

Metal binding

33

1

Iron 1 By similarity

Metal binding

71

1

Iron 1 By similarity

Metal binding

71

1

Iron 2 By similarity

Metal binding

74

1

Iron 1 By similarity

Metal binding

110

1

Iron 2 By similarity

Metal binding

205

1

Iron 2 By similarity

Metal binding

240

1

Iron 2 By similarity

Metal binding

242

1

Iron 1 By similarity

Amino acid modifications

Glycosylation

116

1

N-linked (GlcNAc...) Potential

Glycosylation

147

1

N-linked (GlcNAc...) Potential

Disulfide bond

161 ↔ 219

By similarity

Natural variations

Natural variant

148

1

V → M: dbSNP rs2305799. Ref.3

VAR_020602

Natural variant

200

1

V → M: dbSNP rs2229531. Ref.3

VAR_020603

Natural variant

221

1

V → I: dbSNP rs2229532.

VAR_029288

Experimental info

Sequence conflict

45 – 46

2

AR → GP in AAA76849. Ref.1

Sequence conflict

47

1

E → G AA sequence Ref.8

Sequence conflict

47

1

E → Q AA sequence Ref.7

Sequence conflict

50

1

N → W AA sequence Ref.7

Sequence conflict

177 – 180

4

DVKL → LT in AAA76849. Ref.1

Secondary structure

1

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325

Helix Strand Turn

Details...

Beta strand

26 – 31

6

Helix

45 – 60

16

Beta strand

64 – 68

5

Turn

74 – 76

3

Helix

85 – 89

5

Turn

90 – 93

4

Turn

97 – 101

5

Beta strand

104 – 106

3

Helix

112 – 114

3

Helix

117 – 122

6

Helix

123 – 125

3

Beta strand

134 – 142

9

Beta strand

149 – 154

6

Helix

157 – 161

5

Helix

164 – 166

3

Helix

178 – 194

17

Beta strand

198 – 203

6

Beta strand

211 – 214

4

Helix

218 – 223

6

Helix

225 – 230

6

Beta strand

235 – 238

4

Beta strand

240 – 248

9

Beta strand

254 – 258

5

Helix

271 – 273

3

Beta strand

279 – 283

5

Beta strand

291 – 297

7

Beta strand

299 – 308

10

Beta strand

313 – 320

8

Sequences

	Sequence		Length	Mass (Da)
	P13686-1 [UniParc]. Last modified December 21, 2004. Version 3. Checksum: 079174A71A5BA264	FASTA	325	36,599
	10 20 30 40 50 60 MDMWTALLIL QALLLPSLAD GATPALRFVA VGDWGGVPNA PFHTAREMAN AKEIARTVQI 70 80 90 100 110 120 LGADFILSLG DNFYFTGVQD INDKRFQETF EDVFSDRSLR KVPWYVLAGN HDHLGNVSAQ 130 140 150 160 170 180 IAYSKISKRW NFPSPFYRLH FKIPQTNVSV AIFMLDTVTL CGNSDDFLSQ QPERPRDVKL 190 200 210 220 230 240 ARTQLSWLKK QLAAAREDYV LVAGHYPVWS IAEHGPTHCL VKQLRPLLAT YGVTAYLCGH 250 260 270 280 290 300 DHNLQYLQDE NGVGYVLSGA GNFMDPSKRH QRKVPNGYLR FHYGTEDSLG GFAYVEISSK 310 320 EMTVTYIEAS GKSLFKTRLP RRARP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta." Ketcham C.M., Roberts R.M., Simmen R.C.M., Nick H.S. J. Biol. Chem. 264:557-563(1989) [PubMed: 2909539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage." Lord D.K., Cross N.C.P., Bevilacqua M.A., Roder S.H., Gorman P.A., Groves A.V., Moss D.W., Sheer D., Cox T.M. Eur. J. Biochem. 189:287-293(1990) [PubMed: 2338077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS MET-148 AND MET-200.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"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: Brain and Skin.
[6]	"Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase." Cassady A.I., King A.G., Cross N.C.P., Hume D.A. Gene 130:201-207(1993) [PubMed: 8359686] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
[7]	"Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas." Hayman A.R., Warburton M.J., Pringle J.A.S., Coles B., Chambers T.J. Biochem. J. 261:601-609(1989) [PubMed: 2775236] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-64 AND 183-202. Tissue: Osteoclastoma.
[8]	"Heterogeneity of hairy cell tartrate-resistant acid phosphatase." Janckila A.J., Latham M.D., Lam K.-W., Chow K.-C., Li C.-Y., Yam L.T. Clin. Biochem. 25:437-443(1992) [PubMed: 1477968] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-55 AND 183-203, SUBUNIT. Tissue: Spleen.
[9]	"Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen." Stepan J.J., Lau K.H.W., Mohan S., Kraenzlin M., Baylink D.J. Biochem. Biophys. Res. Commun. 165:1027-1034(1989) [PubMed: 2610679] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-37. Tissue: Osteoclastoma.
[10]	"Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure." Stepan J.J., Lau K.H.W., Mohan S., Singer F.R., Baylink D.J. Biochem. Biophys. Res. Commun. 168:792-800(1990) [PubMed: 2334436] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-31. Tissue: Osteoclastoma.
[11]	"Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide." Hayman A.R., Dryden A.J., Chambers T.J., Warburton M.J. Biochem. J. 277:631-634(1991) [PubMed: 1872798] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J04430 mRNA. Translation: AAA76849.1.
X14618 mRNA. Translation: CAA32771.1.
CR457078 mRNA. Translation: CAG33359.1.
AK290717 mRNA. Translation: BAF83406.1.
BC025414 mRNA. Translation: AAH25414.1.
BC111014 mRNA. Translation: AAI11015.1.
X67123 Genomic DNA. No translation available.

IPI

IPI00419240.

PIR

S15752.

RefSeq

NP_001104504.1.
NP_001104505.1.
NP_001104506.1.
NP_001602.1.

UniGene

Hs.1211

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WAR	X-ray	2.22	A	22-325	[»]
2BQ8	X-ray	2.20	X	22-325	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P13686. 8 interactions.

STRING

P13686.

Proteomic databases

PRIDE

P13686.

Genome annotation databases

Ensembl

ENST00000218758; ENSP00000218758; ENSG00000102575; Homo sapiens. [Genome view]
ENST00000412435; ENSP00000392374; ENSG00000102575; Homo sapiens. [Genome view]
ENST00000433365; ENSP00000413456; ENSG00000102575; Homo sapiens. [Genome view]
ENST00000438664; ENSP00000404885; ENSG00000102575; Homo sapiens. [Genome view]

GeneID

54.

KEGG

hsa:54.

UCSC

uc002msg.2. human.

Organism-specific databases

CTD

54.

GeneCards

GC19M011546.

H-InvDB

HIX0014776.

HGNC

HGNC:124. ACP5.

HPA

CAB002584.

MIM

171640. gene.

PharmGKB

PA24448.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P13686.

HOVERGEN

P13686.

OMA

PWYVIAG.

Enzyme and pathway databases

BRENDA

3.1.3.2. 247.

Reactome

REACT_11193. Metabolism of vitamins and cofactors.

Gene expression databases

ArrayExpress

P13686.

Bgee

P13686.

CleanEx

HS_ACP5.

Genevestigator

P13686.

GermOnline

ENSG00000102575. Homo sapiens.

Family and domain databases

InterPro

IPR004843. M-pesterase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

217.

PMAP-CutDB

P13686.

SOURCE

Search...

Entry information

Entry name

PPA5_HUMAN

Accession

Primary (citable) accession number: P13686
Secondary accession number(s): A8K3V2 , Q2TAB1, Q6IAS6, Q9UCJ5, Q9UCJ6, Q9UCJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.