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Prostatic acid phosphatase (PAP) (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (Thiamine monophosphatase) (TMPase) [Cleaved into: PAPf39]

 PPAP_HUMAN              Reviewed;         386 AA.
P15309; D3DNC6; Q5FBY0; Q96KY0; Q96QK9; Q96QM0;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 3.
30-AUG-2017, entry version 172.
RecName: Full=Prostatic acid phosphatase;
Short=PAP;
EC=3.1.3.2;
AltName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
AltName: Full=Ecto-5'-nucleotidase;
AltName: Full=Thiamine monophosphatase;
Short=TMPase;
Contains:
RecName: Full=PAPf39;
Flags: Precursor;
Name=ACPP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1375464; DOI=10.1016/S0006-291X(05)80048-8;
Sharief F.S., Li S.S.-L.;
"Structure of human prostatic acid phosphatase gene.";
Biochem. Biophys. Res. Commun. 184:1468-1476(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
DISULFIDE BONDS, AND ACTIVE SITE.
PubMed=1989985;
van Etten R.L., Davidson R., Stevis P.E., Macarthur H., Moore D.L.;
"Covalent structure, disulfide bonding, and identification of reactive
surface and active site residues of human prostatic acid
phosphatase.";
J. Biol. Chem. 266:2313-2319(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2712834; DOI=10.1016/0006-291X(89)91623-9;
Sharief F.S., Lee H., Leuderman M.M., Lundwall A., Deaven L.L.,
Lee C.-L., Li S.S.-L.;
"Human prostatic acid phosphatase: cDNA cloning, gene mapping and
protein sequence homology with lysosomal acid phosphatase.";
Biochem. Biophys. Res. Commun. 160:79-86(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Prostate;
PubMed=2842184; DOI=10.1016/0014-5793(88)80037-1;
Vihko P., Virkkunen P., Henttu P., Roiko K., Solin T., Huhtala M.L.;
"Molecular cloning and sequence analysis of cDNA encoding human
prostatic acid phosphatase.";
FEBS Lett. 236:275-281(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=2395659; DOI=10.1093/nar/18.16.4928;
Tailor P.G., Govindan M.V., Patel P.C.;
"Nucleotide sequence of human prostatic acid phosphatase determined
from a full-length cDNA clone.";
Nucleic Acids Res. 18:4928-4928(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=7951074;
Sharief F.S., Li S.S.-L.;
"Nucleotide sequence of human prostatic acid phosphatase ACPP gene,
including seven Alu repeats.";
Biochem. Mol. Biol. Int. 33:561-565(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S.,
Furuya T., Saito T.;
"Acid phosphatase prostate mRNA,nirs splice variant1.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ASN-15; VAL-124; ARG-226; HIS-330 AND ALA-360.
TISSUE=Prostate;
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).
[12]
STRUCTURE OF CARBOHYDRATES.
PubMed=3674882; DOI=10.1016/0003-9861(87)90361-4;
Risley J.M., Van Etten R.L.;
"Structures of the carbohydrate moieties of human prostatic acid
phosphatase elucidated by H1 nuclear magnetic resonance
spectroscopy.";
Arch. Biochem. Biophys. 258:404-412(1987).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, AND
MUTAGENESIS OF TRP-206.
PubMed=9584846;
Zhang Z., Ostanin K., Van Etten R.L.;
"Covalent modification and site-directed mutagenesis of an active site
tryptophan of human prostatic acid phosphatase.";
Acta Biochim. Pol. 44:659-672(1997).
[14]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=15280042; DOI=10.1016/j.febslet.2004.06.083;
Tanaka M., Kishi Y., Takanezawa Y., Kakehi Y., Aoki J., Arai H.;
"Prostatic acid phosphatase degrades lysophosphatidic acid in seminal
plasma.";
FEBS Lett. 571:197-204(2004).
[15]
ALTERNATIVE SPLICING, 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).
[16]
PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, AND ROLE
IN HIV INFECTION.
PubMed=18083097; DOI=10.1016/j.cell.2007.10.014;
Munch J., Rucker E., Standker L., Adermann K., Goffinet C.,
Schindler M., Wildum S., Chinnadurai R., Rajan D., Specht A.,
Gimenez-Gallego G., Sanchez P.C., Fowler D.M., Koulov A., Kelly J.W.,
Mothes W., Grivel J.C., Margolis L., Keppler O.T., Forssmann W.G.,
Kirchhoff F.;
"Semen-derived amyloid fibrils drastically enhance HIV infection.";
Cell 131:1059-1071(2007).
[17]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[18]
PROTEOLYTIC PROCESSING, AND ROLE IN XMRV INFECTION.
PubMed=19403677; DOI=10.1128/JVI.00268-09;
Hong S., Klein E.A., Das Gupta J., Hanke K., Weight C.J., Nguyen C.,
Gaughan C., Kim K.A., Bannert N., Kirchhoff F., Munch J.,
Silverman R.H.;
"Fibrils of prostatic acid phosphatase fragments boost infections with
XMRV (xenotropic murine leukemia virus-related virus), a human
retrovirus associated with prostate cancer.";
J. Virol. 83:6995-7003(2009).
[19]
DEGRADATION OF SEVI AMYLOID FIBRILS.
PubMed=19451623; DOI=10.1073/pnas.0811827106;
Hauber I., Hohenberg H., Holstermann B., Hunstein W., Hauber J.;
"The main green tea polyphenol epigallocatechin-3-gallate counteracts
semen-mediated enhancement of HIV infection.";
Proc. Natl. Acad. Sci. U.S.A. 106:9033-9038(2009).
[20]
INHIBITION OF SEVI ACTIVITY.
PubMed=19897482; DOI=10.1074/jbc.M109.066167;
Roan N.R., Sowinski S., Munch J., Kirchhoff F., Greene W.C.;
"Aminoquinoline surfen inhibits the action of SEVI (semen-derived
enhancer of viral infection).";
J. Biol. Chem. 285:1861-1869(2010).
[21]
FUNCTION.
PubMed=20498373; DOI=10.1074/jbc.M109.098301;
Chuang T.D., Chen S.J., Lin F.F., Veeramani S., Kumar S., Batra S.K.,
Tu Y., Lin M.F.;
"Human prostatic acid phosphatase, an authentic tyrosine phosphatase,
dephosphorylates ErbB-2 and regulates prostate cancer cell growth.";
J. Biol. Chem. 285:23598-23606(2010).
[22]
TISSUE SPECIFICITY.
PubMed=21487525;
Graddis T.J., McMahan C.J., Tamman J., Page K.J., Trager J.B.;
"Prostatic acid phosphatase expression in human tissues.";
Int. J. Clin. Exp. Pathol. 4:295-306(2011).
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH
N-PROPYL-L-TARTRAMATE.
PubMed=9804805; DOI=10.1074/jbc.273.46.30406;
Lacount M.W., Handy G., Lebioda L.;
"Structural origins of L(+)-tartrate inhibition of human prostatic
acid phosphatase.";
J. Biol. Chem. 273:30406-30409(1998).
[24]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 33-374, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-94 AND ASN-220.
PubMed=10639192;
DOI=10.1002/(SICI)1097-0045(20000215)42:3<211::AID-PROS7>3.0.CO;2-U;
Jakob C.G., Lewinski K., Kuciel R., Ostrowski W., Lebioda L.;
"Crystal structure of human prostatic acid phosphatase.";
Prostate 42:211-218(2000).
[25]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-386 IN COMPLEX WITH A
PHOSPHATE ION AND INHIBITOR ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-220 AND ASN-333.
PubMed=12525165; DOI=10.1021/bi0265067;
Ortlund E., LaCount M.W., Lebioda L.;
"Crystal structures of human prostatic acid phosphatase in complex
with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update
the mechanistic picture and offer new insights into inhibitor
design.";
Biochemistry 42:383-389(2003).
[26]
STRUCTURE BY NMR OF 248-286.
PubMed=19995078; DOI=10.1021/ja908170s;
Nanga R.P., Brender J.R., Vivekanandan S., Popovych N.,
Ramamoorthy A.;
"NMR structure in a membrane environment reveals putative
amyloidogenic regions of the SEVI precursor peptide PAP(248-286).";
J. Am. Chem. Soc. 131:17972-17979(2009).
-!- 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.
-!- 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. Acts
as a tumor suppressor of prostate cancer through dephosphorylation
of ERBB2 and deactivation of MAPK-mediated signaling.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000269|PubMed:15280042}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate. {ECO:0000269|PubMed:15280042}.
-!- ENZYME REGULATION: Phosphatase activity inhibited by L(+)-
tartrate, and by its derivative, alpha-benzylaminobenzylphosphonic
acid. {ECO:0000269|PubMed:9584846}.
-!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
activity. {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1222012, EBI-1222012;
P04626:ERBB2; NbExp=3; IntAct=EBI-1222012, EBI-641062;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted
{ECO:0000305|PubMed:17638863}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319};
Single-pass type I membrane protein {ECO:0000255}. Lysosome
membrane {ECO:0000269|PubMed:17638863,
ECO:0000269|PubMed:17897319}; 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 (PubMed:17897319).
{ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Secreted PAP, sPAP;
IsoId=P15309-1; Sequence=Displayed;
Name=2; Synonyms=TMPase, TM-PAP, cellular PAP, cPAP;
IsoId=P15309-2; Sequence=VSP_036023;
Name=3;
IsoId=P15309-3; Sequence=VSP_053360;
-!- TISSUE SPECIFICITY: Highly expressed in the prostate, restricted
to glandular and ductal epithelial cells. Also expressed in
bladder, kidney, pancreas, lung, cervix, testis and ovary. Weak
expression in a subset of pancreatic islet cells, squamous
epithelia, the pilosebaceous unit, colonic neuroendocrine cells
and skin adnexal structures. Isoform 2 also expressed in the
sarcolemma of skeletal muscle. Levels of this cellular isoform
decreased in prostate cancer. {ECO:0000269|PubMed:17638863,
ECO:0000269|PubMed:21487525}.
-!- PTM: N-glycosylated. High mannose content, partially sialylated
and fucosylated biantennary complex. Also fucosylated with
partially sialylated triantennary complex oligosaccharides.
{ECO:0000269|PubMed:10639192, ECO:0000269|PubMed:12525165}.
-!- PTM: Proteolytically cleaved in seminal fluid to produce several
peptides. Peptide PAPf39, the most prominent, forms amyloid beta-
sheet fibrils, SEVI (semen-derived enhancer of viral infection)
which entrap HIV virions, attach them to target cells and enhance
infection. SEVI amyloid fibrils are degraded by polyphenol
epigallocatechin-3-gallate (EGCG), a constituent of green tea.
Target cell attachment and enhancement of HIV infection is
inhibited by surfen. Also similarly boosts XMRV (xenotropic murine
leukemia virus-related virus) infection.
{ECO:0000269|PubMed:18083097, ECO:0000269|PubMed:19403677}.
-!- MISCELLANEOUS: Used as a diagnostic tool for staging metastatic
prostatic cancer.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family.
{ECO:0000305}.
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EMBL; M97589; AAA60021.1; -; Genomic_DNA.
EMBL; M97580; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97581; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97582; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97583; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97584; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97585; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97586; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97587; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M97588; AAA60021.1; JOINED; Genomic_DNA.
EMBL; M34840; AAA69694.1; -; mRNA.
EMBL; M24902; AAA60022.1; -; mRNA.
EMBL; X52174; CAA36422.1; -; mRNA.
EMBL; X53605; CAA37673.1; -; mRNA.
EMBL; U07097; AAB60640.1; -; Genomic_DNA.
EMBL; U07083; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07085; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07086; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07088; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07091; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07092; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07093; AAB60640.1; JOINED; Genomic_DNA.
EMBL; U07095; AAB60640.1; JOINED; Genomic_DNA.
EMBL; AB102888; BAD89417.1; -; mRNA.
EMBL; AK300540; BAG62248.1; -; mRNA.
EMBL; AC020633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79203.1; -; Genomic_DNA.
EMBL; CH471052; EAW79205.1; -; Genomic_DNA.
EMBL; BC007460; AAH07460.1; -; mRNA.
EMBL; BC008493; AAH08493.1; -; mRNA.
EMBL; BC016344; AAH16344.1; -; mRNA.
CCDS; CCDS3073.1; -. [P15309-1]
CCDS; CCDS46916.1; -. [P15309-2]
CCDS; CCDS77818.1; -. [P15309-3]
PIR; JH0610; JH0610.
RefSeq; NP_001090.2; NM_001099.4. [P15309-1]
RefSeq; NP_001127666.1; NM_001134194.1. [P15309-2]
RefSeq; NP_001278966.1; NM_001292037.1. [P15309-3]
UniGene; Hs.433060; -.
PDB; 1CVI; X-ray; 3.20 A; A/B/C/D=33-374.
PDB; 1ND5; X-ray; 2.90 A; A/B/C/D=33-386.
PDB; 1ND6; X-ray; 2.40 A; A/B/C/D=33-386.
PDB; 2HPA; X-ray; 2.90 A; A/B/C/D=33-374.
PDB; 2L3H; NMR; -; A=248-286.
PDB; 2L77; NMR; -; A=248-286.
PDB; 2L79; NMR; -; A=248-286.
PDB; 2MG0; NMR; -; A=262-270.
PDB; 3PPD; X-ray; 1.50 A; A=260-265.
PDBsum; 1CVI; -.
PDBsum; 1ND5; -.
PDBsum; 1ND6; -.
PDBsum; 2HPA; -.
PDBsum; 2L3H; -.
PDBsum; 2L77; -.
PDBsum; 2L79; -.
PDBsum; 2MG0; -.
PDBsum; 3PPD; -.
DisProt; DP00628; -.
ProteinModelPortal; P15309; -.
SMR; P15309; -.
BioGrid; 106571; 26.
IntAct; P15309; 3.
MINT; MINT-6780778; -.
STRING; 9606.ENSP00000323036; -.
BindingDB; P15309; -.
ChEMBL; CHEMBL2633; -.
DrugBank; DB03577; Alpha-Benzyl-Aminobenzyl-Phosphonic Acid.
DrugBank; DB03390; N-Propyl-Tartramic Acid.
DrugBank; DB06688; Sipuleucel-T.
SwissLipids; SLP:000001295; -. [P15309-1]
DEPOD; P15309; -.
iPTMnet; P15309; -.
PhosphoSitePlus; P15309; -.
BioMuta; ACPP; -.
DMDM; 130730; -.
EPD; P15309; -.
MaxQB; P15309; -.
PaxDb; P15309; -.
PeptideAtlas; P15309; -.
PRIDE; P15309; -.
DNASU; 55; -.
Ensembl; ENST00000336375; ENSP00000337471; ENSG00000014257. [P15309-1]
Ensembl; ENST00000351273; ENSP00000323036; ENSG00000014257. [P15309-2]
Ensembl; ENST00000475741; ENSP00000417744; ENSG00000014257. [P15309-3]
GeneID; 55; -.
KEGG; hsa:55; -.
UCSC; uc003eon.4; human. [P15309-1]
CTD; 55; -.
DisGeNET; 55; -.
GeneCards; ACPP; -.
HGNC; HGNC:125; ACPP.
HPA; CAB000071; -.
HPA; HPA004335; -.
HPA; HPA063916; -.
MIM; 171790; gene.
neXtProt; NX_P15309; -.
OpenTargets; ENSG00000014257; -.
PharmGKB; PA24449; -.
eggNOG; KOG3720; Eukaryota.
eggNOG; ENOG410ZVBQ; LUCA.
GeneTree; ENSGT00530000062956; -.
HOGENOM; HOG000231439; -.
HOVERGEN; HBG002203; -.
InParanoid; P15309; -.
KO; K19283; -.
OMA; YGIHKQK; -.
OrthoDB; EOG091G09FA; -.
PhylomeDB; P15309; -.
TreeFam; TF312893; -.
BRENDA; 3.1.3.2; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P15309; -.
ChiTaRS; ACPP; human.
EvolutionaryTrace; P15309; -.
GeneWiki; Prostatic_acid_phosphatase; -.
GenomeRNAi; 55; -.
PMAP-CutDB; P15309; -.
PRO; PR:P15309; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000014257; -.
CleanEx; HS_ACPP; -.
ExpressionAtlas; P15309; baseline and differential.
Genevisible; P15309; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB.
GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
GO; GO:0003993; F:acid phosphatase activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IDA:UniProtKB.
GO; GO:0016791; F:phosphatase activity; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0042131; F:thiamine phosphate phosphatase activity; ISS:UniProtKB.
GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009117; P:nucleotide metabolic process; IEA:Ensembl.
GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
GO; GO:0006144; P:purine nucleobase metabolic process; IEA:Ensembl.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
GO; GO:0006772; P:thiamine metabolic process; ISS: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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amyloid; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Membrane; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 32
CHAIN 33 386 Prostatic acid phosphatase.
/FTId=PRO_0000023963.
PEPTIDE 248 286 PAPf39.
/FTId=PRO_0000411250.
ACT_SITE 44 44 Nucleophile.
{ECO:0000269|PubMed:1989985}.
ACT_SITE 290 290 Proton donor.
{ECO:0000305|PubMed:1989985}.
BINDING 43 43 Substrate.
BINDING 47 47 Substrate.
BINDING 111 111 Substrate.
BINDING 289 289 Substrate.
SITE 49 49 Important for substrate specificity.
SITE 138 138 Required for homodimerization.
{ECO:0000250}.
SITE 144 144 Required for homodimerization.
{ECO:0000250}.
SITE 206 206 Required for structural stability.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10639192}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10639192,
ECO:0000269|PubMed:12525165}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12525165}.
DISULFID 161 372
DISULFID 215 313
DISULFID 347 351
VAR_SEQ 153 185 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.7}.
/FTId=VSP_053360.
VAR_SEQ 380 386 GTEDSTD -> VLKVIFAVAFCLISAVLMVLLFIHIRRGLC
WQRESYGNI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036023.
VARIANT 15 15 S -> N (in dbSNP:rs17850347).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047960.
VARIANT 124 124 F -> V (in dbSNP:rs17856254).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047961.
VARIANT 226 226 W -> R (in dbSNP:rs17856253).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047962.
VARIANT 330 330 Y -> H (in dbSNP:rs17851392).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047963.
VARIANT 360 360 V -> A (in dbSNP:rs17850198).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047964.
MUTAGEN 206 206 W->F: Greatly reduced enzyme activity,
marked decrease in structural stability,
and increased binding of the inhibitor,
L(+)-tartrate.
{ECO:0000269|PubMed:9584846}.
MUTAGEN 206 206 W->L: Reduced enzyme activity, marked
decrease in structural stability, and
increased binding of the inhibitor, L(+)-
tartrate. {ECO:0000269|PubMed:9584846}.
CONFLICT 15 24 SLGFLFLLFF -> AFASCFCFFC (in Ref. 5;
CAA37673). {ECO:0000305}.
CONFLICT 15 24 SLGFLFLLFF -> ALASCFCFFC (in Ref. 3;
AAA60022 and 4; CAA36422). {ECO:0000305}.
CONFLICT 46 46 D -> H (in Ref. 5; CAA37673).
{ECO:0000305}.
CONFLICT 66 73 GFGQLTQL -> RIWPTHPA (in Ref. 5;
CAA37673). {ECO:0000305}.
CONFLICT 66 73 GFGQLTQL -> WIWPTHPA (in Ref. 4;
CAA36422). {ECO:0000305}.
CONFLICT 95 95 E -> D (in Ref. 3; AAA60022).
{ECO:0000305}.
CONFLICT 116 116 A -> R (in Ref. 3; AAA60022).
{ECO:0000305}.
CONFLICT 139 139 Q -> E (in Ref. 5; CAA37673).
{ECO:0000305}.
CONFLICT 157 157 P -> R (in Ref. 5; CAA37673).
{ECO:0000305}.
CONFLICT 212 212 P -> A (in Ref. 4; CAA36422).
{ECO:0000305}.
CONFLICT 215 215 C -> S (in Ref. 3; AAA60022).
{ECO:0000305}.
CONFLICT 294 294 S -> T (in Ref. 3; AAA60022).
{ECO:0000305}.
CONFLICT 372 372 C -> V (in Ref. 3; AAA60022).
{ECO:0000305}.
CONFLICT 383 383 D -> N (in Ref. 5; CAA37673).
{ECO:0000305}.
STRAND 34 43 {ECO:0000244|PDB:1ND6}.
HELIX 60 62 {ECO:0000244|PDB:1ND6}.
HELIX 72 88 {ECO:0000244|PDB:1ND6}.
TURN 89 93 {ECO:0000244|PDB:1ND6}.
HELIX 99 101 {ECO:0000244|PDB:1ND6}.
STRAND 102 108 {ECO:0000244|PDB:1ND6}.
HELIX 110 123 {ECO:0000244|PDB:1ND6}.
HELIX 128 130 {ECO:0000244|PDB:1ND6}.
STRAND 134 136 {ECO:0000244|PDB:1CVI}.
STRAND 144 146 {ECO:0000244|PDB:1ND6}.
HELIX 148 150 {ECO:0000244|PDB:1ND6}.
STRAND 152 155 {ECO:0000244|PDB:1ND6}.
HELIX 162 173 {ECO:0000244|PDB:1ND6}.
HELIX 175 181 {ECO:0000244|PDB:1ND6}.
HELIX 182 184 {ECO:0000244|PDB:1ND6}.
HELIX 185 195 {ECO:0000244|PDB:1ND6}.
HELIX 202 208 {ECO:0000244|PDB:1ND6}.
HELIX 210 218 {ECO:0000244|PDB:1ND6}.
HELIX 229 247 {ECO:0000244|PDB:1ND6}.
STRAND 248 251 {ECO:0000244|PDB:1ND6}.
HELIX 252 258 {ECO:0000244|PDB:1ND6}.
HELIX 261 276 {ECO:0000244|PDB:1ND6}.
STRAND 277 279 {ECO:0000244|PDB:1ND5}.
STRAND 282 288 {ECO:0000244|PDB:1ND6}.
HELIX 290 299 {ECO:0000244|PDB:1ND6}.
STRAND 313 321 {ECO:0000244|PDB:1ND6}.
STRAND 324 332 {ECO:0000244|PDB:1ND6}.
STRAND 335 337 {ECO:0000244|PDB:1CVI}.
STRAND 340 342 {ECO:0000244|PDB:1ND5}.
STRAND 349 352 {ECO:0000244|PDB:1ND6}.
HELIX 353 360 {ECO:0000244|PDB:1ND6}.
HELIX 361 363 {ECO:0000244|PDB:1ND6}.
HELIX 368 371 {ECO:0000244|PDB:1ND6}.
SEQUENCE 386 AA; 44566 MW; EF81E11DFAECADEA CRC64;
MRAAPLLLAR AASLSLGFLF LLFFWLDRSV LAKELKFVTL VFRHGDRSPI DTFPTDPIKE
SSWPQGFGQL TQLGMEQHYE LGEYIRKRYR KFLNESYKHE QVYIRSTDVD RTLMSAMTNL
AALFPPEGVS IWNPILLWQP IPVHTVPLSE DQLLYLPFRN CPRFQELESE TLKSEEFQKR
LHPYKDFIAT LGKLSGLHGQ DLFGIWSKVY DPLYCESVHN FTLPSWATED TMTKLRELSE
LSLLSLYGIH KQKEKSRLQG GVLVNEILNH MKRATQIPSY KKLIMYSAHD TTVSGLQMAL
DVYNGLLPPY ASCHLTELYF EKGEYFVEMY YRNETQHEPY PLMLPGCSPS CPLERFAELV
GPVIPQDWST ECMTTNSHQG TEDSTD


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