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Prostatic acid phosphatase (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (Fluoride-resistant acid phosphatase) (FRAP) (Thiamine monophosphatase) (TMPase)

 PPAP_MOUSE              Reviewed;         381 AA.
Q8CE08; A4QPG2; B8JJZ5; B8JJZ6; Q8C682; Q9QXH7;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 103.
RecName: Full=Prostatic acid phosphatase;
EC=3.1.3.2;
AltName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
AltName: Full=Ecto-5'-nucleotidase;
AltName: Full=Fluoride-resistant acid phosphatase;
Short=FRAP;
AltName: Full=Thiamine monophosphatase;
Short=TMPase;
Flags: Precursor;
Name=Acpp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Crew M.D., Chatta G.S., Borg C.D.;
"Sequence and expression of mouse prostatic acid phosphatase.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Head, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17638863; DOI=10.1158/0008-5472.CAN-07-1651;
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.;
"Prostatic acid phosphatase is not a prostate specific target.";
Cancer Res. 67:6549-6554(2007).
[6]
IDENTIFICATION AS AN ECTONUCLEOSIDASE, DISRUPTION PHENOTYPE, ENZYME
ACTIVITY, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=18940592; DOI=10.1016/j.neuron.2008.08.024;
Zylka M.J., Sowa N.A., Taylor-Blake B., Twomey M.A., Herrala A.,
Voikar V., Vihko P.;
"Prostatic acid phosphatase is an ectonucleotidase and suppresses pain
by generating adenosine.";
Neuron 60:111-122(2008).
[7]
TISSUE SPECIFICITY.
PubMed=20084276; DOI=10.1371/journal.pone.0008674;
Taylor-Blake B., Zylka M.J.;
"Prostatic acid phosphatase is expressed in peptidergic and
nonpeptidergic nociceptive neurons of mice and rats.";
PLoS ONE 5:E8674-E8674(2010).
-!- 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). {ECO:0000250}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:18940592}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000269|PubMed:18940592}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate. {ECO:0000269|PubMed:18940592}.
-!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
activity. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted
{ECO:0000305|PubMed:17638863}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein
{ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863};
Single-pass type I membrane protein {ECO:0000255}. Note=Appears to
shuttle between the cell membrane and intracellular vesicles.
Colocalizes with FLOT1 at cell membrane and in intracellular
vesicles (PubMed:17638863). Colocalizes with LAMP2 on the lysosome
membrane (By similarity). {ECO:0000250|UniProtKB:P15309,
ECO:0000269|PubMed:17638863}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CE08-1; Sequence=Displayed;
Name=2; Synonyms=TMPase, TM-PAP, cellular PAP, cPAP;
IsoId=Q8CE08-2; Sequence=VSP_036024;
-!- 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.
{ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:18940592,
ECO:0000269|PubMed:20084276}.
-!- 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. {ECO:0000269|PubMed:18940592}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF210243; AAF23171.1; -; mRNA.
EMBL; AK029273; BAC26366.1; -; mRNA.
EMBL; AK076383; BAC36318.1; -; mRNA.
EMBL; CT030733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC139826; AAI39827.1; -; mRNA.
CCDS; CCDS23460.1; -. [Q8CE08-2]
CCDS; CCDS40750.1; -. [Q8CE08-1]
RefSeq; NP_062781.2; NM_019807.2. [Q8CE08-1]
RefSeq; NP_997551.1; NM_207668.2. [Q8CE08-2]
UniGene; Mm.19941; -.
ProteinModelPortal; Q8CE08; -.
SMR; Q8CE08; -.
STRING; 10090.ENSMUSP00000059889; -.
PhosphoSitePlus; Q8CE08; -.
PaxDb; Q8CE08; -.
PeptideAtlas; Q8CE08; -.
PRIDE; Q8CE08; -.
Ensembl; ENSMUST00000062723; ENSMUSP00000059889; ENSMUSG00000032561. [Q8CE08-2]
Ensembl; ENSMUST00000112590; ENSMUSP00000108209; ENSMUSG00000032561. [Q8CE08-1]
GeneID; 56318; -.
KEGG; mmu:56318; -.
UCSC; uc009rhl.1; mouse. [Q8CE08-2]
UCSC; uc009rhm.1; mouse. [Q8CE08-1]
CTD; 55; -.
MGI; MGI:1928480; Acpp.
eggNOG; KOG3720; Eukaryota.
eggNOG; ENOG410ZVBQ; LUCA.
GeneTree; ENSGT00530000062956; -.
HOGENOM; HOG000231439; -.
HOVERGEN; HBG002203; -.
InParanoid; Q8CE08; -.
KO; K19283; -.
OMA; YGIHKQK; -.
OrthoDB; EOG091G09FA; -.
TreeFam; TF312893; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:Q8CE08; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032561; -.
ExpressionAtlas; Q8CE08; baseline and differential.
Genevisible; Q8CE08; MM.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0012506; C:vesicle membrane; IDA:UniProtKB.
GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB.
GO; GO:0003993; F:acid phosphatase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:UniProtKB.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0042131; F:thiamine phosphate phosphatase activity; IMP:UniProtKB.
GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0009117; P:nucleotide metabolic process; IMP:UniProtKB.
GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0006144; P:purine nucleobase metabolic process; IMP:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
GO; GO:0006772; P:thiamine metabolic process; IMP:UniProtKB.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane;
Reference proteome; Secreted; Signal.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 381 Prostatic acid phosphatase.
/FTId=PRO_0000356293.
ACT_SITE 43 43 Nucleophile. {ECO:0000250}.
ACT_SITE 289 289 Proton donor. {ECO:0000250}.
BINDING 42 42 Substrate. {ECO:0000250}.
BINDING 46 46 Substrate. {ECO:0000250}.
BINDING 110 110 Substrate. {ECO:0000250}.
BINDING 288 288 Substrate. {ECO:0000250}.
SITE 48 48 Important for substrate specificity.
{ECO:0000250}.
SITE 137 137 Required for dimerization. {ECO:0000250}.
SITE 143 143 Required for dimerization. {ECO:0000250}.
SITE 205 205 Required for structural stability.
{ECO:0000250}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 160 371 {ECO:0000250}.
DISULFID 214 312 {ECO:0000250}.
DISULFID 346 350 {ECO:0000250}.
VAR_SEQ 378 381 QGRN -> QVLRVILATTFCLVTGILVILLLVLIRHGPCWQ
RDVYRNI (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_036024.
CONFLICT 2 2 R -> G (in Ref. 4; AAI39827).
{ECO:0000305}.
CONFLICT 3 3 A -> S (in Ref. 2; BAC36318).
{ECO:0000305}.
CONFLICT 10 10 R -> P (in Ref. 4; AAI39827).
{ECO:0000305}.
CONFLICT 145 145 V -> L (in Ref. 2; BAC36318).
{ECO:0000305}.
CONFLICT 230 230 A -> P (in Ref. 2; BAC36318).
{ECO:0000305}.
CONFLICT 264 264 N -> H (in Ref. 2; BAC36318).
{ECO:0000305}.
CONFLICT 355 355 F -> L (in Ref. 2; BAC36318).
{ECO:0000305}.
CONFLICT 357 358 EL -> DV (in Ref. 1; AAF23171).
{ECO:0000305}.
SEQUENCE 381 AA; 43717 MW; C0077819D77CB251 CRC64;
MRAVPLPLSR TASLSLGFLL LLSLCLDPGQ AKELKFVTLV FRHGDRGPIE TFPTDPITES
SWPQGFGQLT QWGMEQHYEL GSYIRKRYGR FLNDTYKHDQ IYIRSTDVDR TLMSAMTNLA
ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFEELKSET LESEEFLKRL
HPYKSFLDTL SSLSGFDDQD LFGIWSKVYD PLFCESVHNF TLPSWATEDA MIKLKELSEL
SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKYK KLVMYSAHDT TVSGLQMALD
VYNGVLPPYA SCHMMELYHD KGGHFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD
PVISQDWATE CMATSSHQGR N


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