Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P13686 (PPA5_HUMAN)

Last modified November 3, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Acid phosphatase 5, tartrate resistant
Gene names
Name: ACP5
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandIron
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytosol 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 functionacid 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.8 Ref.7 Ref.9 Ref.10
Chain22 – 325304Tartrate-resistant acid phosphatase type 5
PRO_0000023981

Sites

Metal binding331Iron 1 By similarity
Metal binding711Iron 1 By similarity
Metal binding711Iron 2 By similarity
Metal binding741Iron 1 By similarity
Metal binding1101Iron 2 By similarity
Metal binding2051Iron 2 By similarity
Metal binding2401Iron 2 By similarity
Metal binding2421Iron 1 By similarity

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Disulfide bond161 ↔ 219 By similarity

Natural variations

Natural variant1481V → M: dbSNP rs2305799. Ref.3
VAR_020602
Natural variant2001V → M: dbSNP rs2229531. Ref.3
VAR_020603
Natural variant2211V → I: dbSNP rs2229532.
VAR_029288

Experimental info

Sequence conflict45 – 462AR → GP in AAA76849. Ref.1
Sequence conflict471E → G AA sequence Ref.8
Sequence conflict471E → Q AA sequence Ref.7
Sequence conflict501N → W AA sequence Ref.7
Sequence conflict177 – 1804DVKL → LT in AAA76849. Ref.1

Secondary structure

....................................................... 325
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13686-1 [UniParc].

Last modified December 21, 2004. Version 3.
Checksum: 079174A71A5BA264

FASTA32536,599
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

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.
IPIIPI00419240.
PIRS15752.
RefSeqNP_001104504.1.
NP_001104505.1.
NP_001104506.1.
NP_001602.1.
UniGeneHs.1211

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WARX-ray2.22A22-325[»]
2BQ8X-ray2.20X22-325[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP13686. 8 interactions.
STRINGP13686.

Proteomic databases

PRIDEP13686.

Genome annotation databases

EnsemblENST00000218758; 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]
GeneID54.
KEGGhsa:54.
UCSCuc002msg.2. human.

Organism-specific databases

CTD54.
GeneCardsGC19M011546.
H-InvDBHIX0014776.
HGNCHGNC:124. ACP5.
HPACAB002584.
MIM171640. gene.
PharmGKBPA24448.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13686.
HOVERGENP13686.
OMAPWYVIAG.

Enzyme and pathway databases

BRENDA3.1.3.2. 247.
ReactomeREACT_11193. Metabolism of vitamins and cofactors.

Gene expression databases

ArrayExpressP13686.
BgeeP13686.
CleanExHS_ACP5.
GenevestigatorP13686.
GermOnlineENSG00000102575. Homo sapiens.

Family and domain databases

InterProIPR004843. M-pesterase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio217.
PMAP-CutDBP13686.
SOURCESearch...

Entry information

Entry namePPA5_HUMAN
AccessionPrimary (citable) accession number: P13686
Secondary accession number(s): A8K3V2 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents