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Q8CE08 (PPAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostatic acid phosphatase

EC=3.1.3.2
Alternative name(s):
5'-nucleotidase
Short name=5'-NT
EC=3.1.3.5
Ecto-5'-nucleotidase
Fluoride-resistant acid phosphatase
Short name=FRAP
Thiamine monophosphatase
Short name=TMPase
Gene names
Name:Acpp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma By similarity. Ref.6

Isoform 2:the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Ref.6

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.6

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. Ref.6

Subunit structure

Homodimer; dimer formation is required for phosphatase activity By similarity.

Subcellular location

Isoform 1: Secreted By similarity Ref.5.

Isoform 2: Cell membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note: Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles. Colocalizes with LAMP2 on the lysosome membrane By similarity. Ref.5

Tissue specificity

Isoform 1 is expressed in salivary gland, thymus and thyroid gland. Isoform 2 is widely expressed in prostate lobes, brain, kidney, liver, lung, muscle, placenta, salivary gland, spleen, thyroid and thymus. Locates to Schwann cells and fibroblasts. Expressed in peptidergic and non-peptidergic nociceptive (pain-sensing) neurons. Preferentially expressed in non-peptidergic doral root ganglia neurons. Ref.5 Ref.6 Ref.7

Disruption phenotype

Null mice display greater thermal hyperalgesia (pain sensitivity) and mechanical allodynia. No thiamine monophosphatase (TMPase) activity detected in dorsal root ganglion (DRG) neurons. Ref.6

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Cellular componentCell membrane
Lysosome
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenosine metabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

dephosphorylation

Inferred from sequence or structural similarity. Source: UniProt

nucleotide metabolic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of adenosine receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProt

purine nucleobase metabolic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of sensory perception of pain

Inferred from mutant phenotype Ref.6. Source: UniProt

thiamine metabolic process

Inferred from mutant phenotype Ref.6. Source: UniProt

   Cellular_componentGolgi cisterna

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from sequence or structural similarity. Source: UniProt

filopodium

Inferred from direct assay PubMed 17658863. Source: UniProtKB

integral component of membrane

Inferred from direct assay PubMed 17658863. Source: UniProtKB

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

multivesicular body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17658863. Source: UniProtKB

secretory granule

Inferred from electronic annotation. Source: Ensembl

vesicle membrane

Inferred from direct assay Ref.6. Source: UniProt

   Molecular_function5'-nucleotidase activity

Inferred from sequence or structural similarity. Source: UniProt

acid phosphatase activity

Inferred from sequence or structural similarity. Source: UniProt

choline binding

Inferred from electronic annotation. Source: Ensembl

lysophosphatidic acid phosphatase activity

Inferred from sequence or structural similarity. Source: UniProt

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProt

thiamine phosphate phosphatase activity

Inferred from mutant phenotype Ref.6. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CE08-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8CE08-2)

Also known as: TMPase; TM-PAP; cellular PAP; cPAP;

The sequence of this isoform differs from the canonical sequence as follows:
     378-381: QGRN → QVLRVILATTFCLVTGILVILLLVLIRHGPCWQRDVYRNI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 381350Prostatic acid phosphatase
PRO_0000356293

Sites

Active site431Nucleophile By similarity
Active site2891Proton donor By similarity
Binding site421Substrate By similarity
Binding site461Substrate By similarity
Binding site1101Substrate By similarity
Binding site2881Substrate By similarity
Site481Important for substrate specificity By similarity
Site1371Required for dimerization By similarity
Site1431Required for dimerization By similarity
Site2051Required for structural stability By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Disulfide bond160 ↔ 371 By similarity
Disulfide bond214 ↔ 312 By similarity
Disulfide bond346 ↔ 350 By similarity

Natural variations

Alternative sequence378 – 3814QGRN → QVLRVILATTFCLVTGILVI LLLVLIRHGPCWQRDVYRNI in isoform 2.
VSP_036024

Experimental info

Sequence conflict21R → G in AAI39827. Ref.4
Sequence conflict31A → S in BAC36318. Ref.2
Sequence conflict101R → P in AAI39827. Ref.4
Sequence conflict1451V → L in BAC36318. Ref.2
Sequence conflict2301A → P in BAC36318. Ref.2
Sequence conflict2641N → H in BAC36318. Ref.2
Sequence conflict3551F → L in BAC36318. Ref.2
Sequence conflict357 – 3582EL → DV in AAF23171. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C0077819D77CB251

FASTA38143,717
        10         20         30         40         50         60 
MRAVPLPLSR TASLSLGFLL LLSLCLDPGQ AKELKFVTLV FRHGDRGPIE TFPTDPITES 

        70         80         90        100        110        120 
SWPQGFGQLT QWGMEQHYEL GSYIRKRYGR FLNDTYKHDQ IYIRSTDVDR TLMSAMTNLA 

       130        140        150        160        170        180 
ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFEELKSET LESEEFLKRL 

       190        200        210        220        230        240 
HPYKSFLDTL SSLSGFDDQD LFGIWSKVYD PLFCESVHNF TLPSWATEDA MIKLKELSEL 

       250        260        270        280        290        300 
SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKYK KLVMYSAHDT TVSGLQMALD 

       310        320        330        340        350        360 
VYNGVLPPYA SCHMMELYHD KGGHFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD 

       370        380 
PVISQDWATE CMATSSHQGR N 

« Hide

Isoform 2 (TMPase) (TM-PAP) (cellular PAP) (cPAP) [UniParc].

Checksum: 505B9B551BA5CEF7
Show »

FASTA41747,863

References

« Hide 'large scale' references
[1]"Sequence and expression of mouse prostatic acid phosphatase."
Crew M.D., Chatta G.S., Borg C.D.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Head and Skin.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORM 2).
[5]"Prostatic acid phosphatase is not a prostate specific target."
Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M., Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J., Hirvikoski P.P., Vihko P.T.
Cancer Res. 67:6549-6554(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine."
Zylka M.J., Sowa N.A., Taylor-Blake B., Twomey M.A., Herrala A., Voikar V., Vihko P.
Neuron 60:111-122(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS AN ECTONUCLEOSIDASE, DISRUPTION PHENOTYPE, ENZYME ACTIVITY, TISSUE SPECIFICITY, FUNCTION.
[7]"Prostatic acid phosphatase is expressed in peptidergic and nonpeptidergic nociceptive neurons of mice and rats."
Taylor-Blake B., Zylka M.J.
PLoS ONE 5:E8674-E8674(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF210243 mRNA. Translation: AAF23171.1.
AK029273 mRNA. Translation: BAC26366.1.
AK076383 mRNA. Translation: BAC36318.1.
CT030733 Genomic DNA. Translation: CAX15527.1.
CT030733 Genomic DNA. Translation: CAX15528.1.
BC139826 mRNA. Translation: AAI39827.1.
RefSeqNP_062781.2. NM_019807.2.
NP_997551.1. NM_207668.2.
UniGeneMm.19941.

3D structure databases

ProteinModelPortalQ8CE08.
SMRQ8CE08. Positions 32-373.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8CE08.

Proteomic databases

PRIDEQ8CE08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062723; ENSMUSP00000059889; ENSMUSG00000032561. [Q8CE08-2]
ENSMUST00000112590; ENSMUSP00000108209; ENSMUSG00000032561. [Q8CE08-1]
GeneID56318.
KEGGmmu:56318.
UCSCuc009rhl.1. mouse. [Q8CE08-2]
uc009rhm.1. mouse. [Q8CE08-1]

Organism-specific databases

CTD55.
MGIMGI:1928480. Acpp.

Phylogenomic databases

eggNOGNOG85977.
GeneTreeENSGT00530000062956.
HOGENOMHOG000231439.
HOVERGENHBG002203.
InParanoidQ8C682.
KOK14410.
OMAFTLPSWA.
OrthoDBEOG7GXPBJ.
TreeFamTF312893.

Gene expression databases

BgeeQ8CE08.
GenevestigatorQ8CE08.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312276.
PROQ8CE08.
SOURCESearch...

Entry information

Entry namePPAP_MOUSE
AccessionPrimary (citable) accession number: Q8CE08
Secondary accession number(s): A4QPG2 expand/collapse secondary AC list , B8JJZ5, B8JJZ6, Q8C682, Q9QXH7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot