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Q8CE08

- PPAP_MOUSE

UniProt

Q8CE08 - PPAP_MOUSE

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Protein
Prostatic acid phosphatase
Gene
Acpp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication
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.1 Publication

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.1 Publication
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421Substrate By similarity
Active sitei43 – 431Nucleophile By similarity
Binding sitei46 – 461Substrate By similarity
Sitei48 – 481Important for substrate specificity By similarity
Binding sitei110 – 1101Substrate By similarity
Sitei137 – 1371Required for dimerization By similarity
Sitei143 – 1431Required for dimerization By similarity
Sitei205 – 2051Required for structural stability By similarity
Binding sitei288 – 2881Substrate By similarity
Active sitei289 – 2891Proton donor By similarity

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: UniProt
  2. acid phosphatase activity Source: UniProt
  3. choline binding Source: Ensembl
  4. lysophosphatidic acid phosphatase activity Source: UniProt
  5. phosphatase activity Source: UniProt
  6. thiamine phosphate phosphatase activity Source: UniProt

GO - Biological processi

  1. adenosine metabolic process Source: UniProtKB
  2. dephosphorylation Source: UniProt
  3. nucleotide metabolic process Source: UniProtKB
  4. positive regulation of adenosine receptor signaling pathway Source: UniProt
  5. purine nucleobase metabolic process Source: UniProtKB
  6. regulation of sensory perception of pain Source: UniProt
  7. thiamine metabolic process Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Prostatic acid phosphatase (EC:3.1.3.2)
Alternative name(s):
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Ecto-5'-nucleotidase
Fluoride-resistant acid phosphatase
Short name:
FRAP
Thiamine monophosphatase
Short name:
TMPase
Gene namesi
Name:Acpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1928480. Acpp.

Subcellular locationi

Isoform 1 : Secreted By similarity 1 Publication
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.1 Publication

GO - Cellular componenti

  1. Golgi cisterna Source: Ensembl
  2. apical part of cell Source: Ensembl
  3. extracellular space Source: UniProt
  4. filopodium Source: UniProtKB
  5. integral component of membrane Source: UniProtKB
  6. lysosomal membrane Source: UniProtKB-SubCell
  7. multivesicular body Source: Ensembl
  8. plasma membrane Source: UniProtKB
  9. secretory granule Source: Ensembl
  10. vesicle membrane Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lysosome, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Null mice display greater thermal hyperalgesia (pain sensitivity) and mechanical allodynia. No thiamine monophosphatase (TMPase) activity detected in dorsal root ganglion (DRG) neurons.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 381350Prostatic acid phosphatase
PRO_0000356293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi160 ↔ 371 By similarity
Disulfide bondi214 ↔ 312 By similarity
Glycosylationi219 – 2191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi332 – 3321N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi346 ↔ 350 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8CE08.

PTM databases

PhosphoSiteiQ8CE08.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ8CE08.
GenevestigatoriQ8CE08.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ8CE08.
SMRiQ8CE08. Positions 32-373.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85977.
GeneTreeiENSGT00530000062956.
HOGENOMiHOG000231439.
HOVERGENiHBG002203.
InParanoidiQ8C682.
KOiK14410.
OMAiFTLPSWA.
OrthoDBiEOG7GXPBJ.
TreeFamiTF312893.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CE08-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRAVPLPLSR TASLSLGFLL LLSLCLDPGQ AKELKFVTLV FRHGDRGPIE    50
TFPTDPITES SWPQGFGQLT QWGMEQHYEL GSYIRKRYGR FLNDTYKHDQ 100
IYIRSTDVDR TLMSAMTNLA ALFPPEGISI WNPRLLWQPI PVHTVSLSED 150
RLLYLPFRDC PRFEELKSET LESEEFLKRL HPYKSFLDTL SSLSGFDDQD 200
LFGIWSKVYD PLFCESVHNF TLPSWATEDA MIKLKELSEL SLLSLYGIHK 250
QKEKSRLQGG VLVNEILKNM KLATQPQKYK KLVMYSAHDT TVSGLQMALD 300
VYNGVLPPYA SCHMMELYHD KGGHFVEMYY RNETQNEPYP LTLPGCTHSC 350
PLEKFAELLD PVISQDWATE CMATSSHQGR N 381
Length:381
Mass (Da):43,717
Last modified:March 1, 2003 - v1
Checksum:iC0077819D77CB251
GO
Isoform 2 (identifier: Q8CE08-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:417
Mass (Da):47,863
Checksum:i505B9B551BA5CEF7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei378 – 3814QGRN → QVLRVILATTFCLVTGILVI LLLVLIRHGPCWQRDVYRNI in isoform 2.
VSP_036024

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21R → G in AAI39827. 1 Publication
Sequence conflicti3 – 31A → S in BAC36318. 1 Publication
Sequence conflicti10 – 101R → P in AAI39827. 1 Publication
Sequence conflicti145 – 1451V → L in BAC36318. 1 Publication
Sequence conflicti230 – 2301A → P in BAC36318. 1 Publication
Sequence conflicti264 – 2641N → H in BAC36318. 1 Publication
Sequence conflicti355 – 3551F → L in BAC36318. 1 Publication
Sequence conflicti357 – 3582EL → DV in AAF23171. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23460.1. [Q8CE08-2]
CCDS40750.1. [Q8CE08-1]
RefSeqiNP_062781.2. NM_019807.2. [Q8CE08-1]
NP_997551.1. NM_207668.2. [Q8CE08-2]
UniGeneiMm.19941.

Genome annotation databases

EnsembliENSMUST00000062723; ENSMUSP00000059889; ENSMUSG00000032561. [Q8CE08-2]
ENSMUST00000112590; ENSMUSP00000108209; ENSMUSG00000032561. [Q8CE08-1]
GeneIDi56318.
KEGGimmu:56318.
UCSCiuc009rhl.1. mouse. [Q8CE08-2]
uc009rhm.1. mouse. [Q8CE08-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23460.1. [Q8CE08-2 ]
CCDS40750.1. [Q8CE08-1 ]
RefSeqi NP_062781.2. NM_019807.2. [Q8CE08-1 ]
NP_997551.1. NM_207668.2. [Q8CE08-2 ]
UniGenei Mm.19941.

3D structure databases

ProteinModelPortali Q8CE08.
SMRi Q8CE08. Positions 32-373.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8CE08.

Proteomic databases

PRIDEi Q8CE08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000062723 ; ENSMUSP00000059889 ; ENSMUSG00000032561 . [Q8CE08-2 ]
ENSMUST00000112590 ; ENSMUSP00000108209 ; ENSMUSG00000032561 . [Q8CE08-1 ]
GeneIDi 56318.
KEGGi mmu:56318.
UCSCi uc009rhl.1. mouse. [Q8CE08-2 ]
uc009rhm.1. mouse. [Q8CE08-1 ]

Organism-specific databases

CTDi 55.
MGIi MGI:1928480. Acpp.

Phylogenomic databases

eggNOGi NOG85977.
GeneTreei ENSGT00530000062956.
HOGENOMi HOG000231439.
HOVERGENi HBG002203.
InParanoidi Q8C682.
KOi K14410.
OMAi FTLPSWA.
OrthoDBi EOG7GXPBJ.
TreeFami TF312893.

Miscellaneous databases

NextBioi 312276.
PROi Q8CE08.
SOURCEi Search...

Gene expression databases

Bgeei Q8CE08.
Genevestigatori Q8CE08.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiPPAP_MOUSE
AccessioniPrimary (citable) accession number: Q8CE08
Secondary accession number(s): A4QPG2
, B8JJZ5, B8JJZ6, Q8C682, Q9QXH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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