PPAP_HUMAN
ID PPAP_HUMAN Reviewed; 386 AA.
AC P15309; D3DNC6; Q5FBY0; Q96KY0; Q96QK9; Q96QM0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Prostatic acid phosphatase {ECO:0000305};
DE Short=PAP;
DE EC=3.1.3.2 {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:15280042, ECO:0000269|PubMed:9584846};
DE AltName: Full=5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q8CE08};
DE AltName: Full=Acid phosphatase 3 {ECO:0000312|HGNC:HGNC:125};
DE AltName: Full=Ecto-5'-nucleotidase;
DE AltName: Full=Protein tyrosine phosphatase ACP3 {ECO:0000305|PubMed:20498373};
DE EC=3.1.3.48 {ECO:0000269|PubMed:20498373};
DE AltName: Full=Thiamine monophosphatase;
DE Short=TMPase;
DE Contains:
DE RecName: Full=PAPf39;
DE Flags: Precursor;
GN Name=ACP3 {ECO:0000312|HGNC:HGNC:125}; Synonyms=ACPP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1375464; DOI=10.1016/s0006-291x(05)80048-8;
RA Sharief F.S., Li S.S.-L.;
RT "Structure of human prostatic acid phosphatase gene.";
RL Biochem. Biophys. Res. Commun. 184:1468-1476(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, DISULFIDE
RP BONDS, AND ACTIVE SITE.
RX PubMed=1989985; DOI=10.1016/s0021-9258(18)52245-6;
RA van Etten R.L., Davidson R., Stevis P.E., Macarthur H., Moore D.L.;
RT "Covalent structure, disulfide bonding, and identification of reactive
RT surface and active site residues of human prostatic acid phosphatase.";
RL J. Biol. Chem. 266:2313-2319(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2712834; DOI=10.1016/0006-291x(89)91623-9;
RA Sharief F.S., Lee H., Leuderman M.M., Lundwall A., Deaven L.L., Lee C.-L.,
RA Li S.S.-L.;
RT "Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein
RT sequence homology with lysosomal acid phosphatase.";
RL Biochem. Biophys. Res. Commun. 160:79-86(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Prostate;
RX PubMed=2842184; DOI=10.1016/0014-5793(88)80037-1;
RA Vihko P., Virkkunen P., Henttu P., Roiko K., Solin T., Huhtala M.L.;
RT "Molecular cloning and sequence analysis of cDNA encoding human prostatic
RT acid phosphatase.";
RL FEBS Lett. 236:275-281(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=2395659; DOI=10.1093/nar/18.16.4928;
RA Tailor P.G., Govindan M.V., Patel P.C.;
RT "Nucleotide sequence of human prostatic acid phosphatase determined from a
RT full-length cDNA clone.";
RL Nucleic Acids Res. 18:4928-4928(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7951074;
RA Sharief F.S., Li S.S.-L.;
RT "Nucleotide sequence of human prostatic acid phosphatase ACPP gene,
RT including seven Alu repeats.";
RL Biochem. Mol. Biol. Int. 33:561-565(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S.,
RA Furuya T., Saito T.;
RT "Acid phosphatase prostate mRNA,nirs splice variant1.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ASN-15; VAL-124; ARG-226; HIS-330 AND ALA-360.
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=3674882; DOI=10.1016/0003-9861(87)90361-4;
RA Risley J.M., Van Etten R.L.;
RT "Structures of the carbohydrate moieties of human prostatic acid
RT phosphatase elucidated by H1 nuclear magnetic resonance spectroscopy.";
RL Arch. Biochem. Biophys. 258:404-412(1987).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF TRP-206.
RX PubMed=9584846;
RA Zhang Z., Ostanin K., Van Etten R.L.;
RT "Covalent modification and site-directed mutagenesis of an active site
RT tryptophan of human prostatic acid phosphatase.";
RL Acta Biochim. Pol. 44:659-672(1997).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10506173; DOI=10.1074/jbc.274.41.29172;
RA Hiroyama M., Takenawa T.;
RT "Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that
RT is involved in the regulation of mitochondrial lipid biosynthesis.";
RL J. Biol. Chem. 274:29172-29180(1999).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15280042; DOI=10.1016/j.febslet.2004.06.083;
RA Tanaka M., Kishi Y., Takanezawa Y., Kakehi Y., Aoki J., Arai H.;
RT "Prostatic acid phosphatase degrades lysophosphatidic acid in seminal
RT plasma.";
RL FEBS Lett. 571:197-204(2004).
RN [16]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17638863; DOI=10.1158/0008-5472.can-07-1651;
RA Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M.,
RA Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J.,
RA Hirvikoski P.P., Vihko P.T.;
RT "Prostatic acid phosphatase is not a prostate specific target.";
RL Cancer Res. 67:6549-6554(2007).
RN [17]
RP PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY OF PAPF39, AND
RP FUNCTION IN HIV INFECTION (MICROBIAL INFECTION).
RX PubMed=18083097; DOI=10.1016/j.cell.2007.10.014;
RA Munch J., Rucker E., Standker L., Adermann K., Goffinet C., Schindler M.,
RA Wildum S., Chinnadurai R., Rajan D., Specht A., Gimenez-Gallego G.,
RA Sanchez P.C., Fowler D.M., Koulov A., Kelly J.W., Mothes W., Grivel J.C.,
RA Margolis L., Keppler O.T., Forssmann W.G., Kirchhoff F.;
RT "Semen-derived amyloid fibrils drastically enhance HIV infection.";
RL Cell 131:1059-1071(2007).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [19]
RP PROTEOLYTIC PROCESSING, AND FUNTION IN XMRV INFECTION (MICROBIAL
RP INFECTION).
RX PubMed=19403677; DOI=10.1128/jvi.00268-09;
RA Hong S., Klein E.A., Das Gupta J., Hanke K., Weight C.J., Nguyen C.,
RA Gaughan C., Kim K.A., Bannert N., Kirchhoff F., Munch J., Silverman R.H.;
RT "Fibrils of prostatic acid phosphatase fragments boost infections with XMRV
RT (xenotropic murine leukemia virus-related virus), a human retrovirus
RT associated with prostate cancer.";
RL J. Virol. 83:6995-7003(2009).
RN [20]
RP FUNCTION, AND DEGRADATION OF SEVI AMYLOID FIBRILS (MICROBIAL INFECTION).
RX PubMed=19451623; DOI=10.1073/pnas.0811827106;
RA Hauber I., Hohenberg H., Holstermann B., Hunstein W., Hauber J.;
RT "The main green tea polyphenol epigallocatechin-3-gallate counteracts
RT semen-mediated enhancement of HIV infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9033-9038(2009).
RN [21]
RP FUNCTION (MICROBIAL INFECTION), AND INHIBITION OF SEVI ACTIVITY.
RX PubMed=19897482; DOI=10.1074/jbc.m109.066167;
RA Roan N.R., Sowinski S., Munch J., Kirchhoff F., Greene W.C.;
RT "Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer
RT of viral infection).";
RL J. Biol. Chem. 285:1861-1869(2010).
RN [22]
RP FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY (ISOFORM 2), AND SUBCELLULAR
RP LOCATION (ISOFORM 2).
RX PubMed=20498373; DOI=10.1074/jbc.m109.098301;
RA Chuang T.D., Chen S.J., Lin F.F., Veeramani S., Kumar S., Batra S.K.,
RA Tu Y., Lin M.F.;
RT "Human prostatic acid phosphatase, an authentic tyrosine phosphatase,
RT dephosphorylates ErbB-2 and regulates prostate cancer cell growth.";
RL J. Biol. Chem. 285:23598-23606(2010).
RN [23]
RP TISSUE SPECIFICITY.
RX PubMed=21487525;
RA Graddis T.J., McMahan C.J., Tamman J., Page K.J., Trager J.B.;
RT "Prostatic acid phosphatase expression in human tissues.";
RL Int. J. Clin. Exp. Pathol. 4:295-306(2011).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH
RP N-PROPYL-L-TARTRAMATE.
RX PubMed=9804805; DOI=10.1074/jbc.273.46.30406;
RA Lacount M.W., Handy G., Lebioda L.;
RT "Structural origins of L(+)-tartrate inhibition of human prostatic acid
RT phosphatase.";
RL J. Biol. Chem. 273:30406-30409(1998).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 33-374, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-94 AND ASN-220.
RX PubMed=10639192;
RX DOI=10.1002/(sici)1097-0045(20000215)42:3<211::aid-pros7>3.0.co;2-u;
RA Jakob C.G., Lewinski K., Kuciel R., Ostrowski W., Lebioda L.;
RT "Crystal structure of human prostatic acid phosphatase.";
RL Prostate 42:211-218(2000).
RN [26] {ECO:0007744|PDB:1ND5, ECO:0007744|PDB:1ND6}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-386 IN COMPLEX WITH A PHOSPHATE
RP ION AND INHIBITOR ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID, DISULFIDE BONDS,
RP AND GLYCOSYLATION AT ASN-220 AND ASN-333.
RX PubMed=12525165; DOI=10.1021/bi0265067;
RA Ortlund E., LaCount M.W., Lebioda L.;
RT "Crystal structures of human prostatic acid phosphatase in complex with a
RT phosphate ion and alpha-benzylaminobenzylphosphonic acid update the
RT mechanistic picture and offer new insights into inhibitor design.";
RL Biochemistry 42:383-389(2003).
RN [27]
RP STRUCTURE BY NMR OF 248-286.
RX PubMed=19995078; DOI=10.1021/ja908170s;
RA Nanga R.P., Brender J.R., Vivekanandan S., Popovych N., Ramamoorthy A.;
RT "NMR structure in a membrane environment reveals putative amyloidogenic
RT regions of the SEVI precursor peptide PAP(248-286).";
RL J. Am. Chem. Soc. 131:17972-17979(2009).
CC -!- FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a
CC diverse number of substrates under acidic conditions (pH 4-6) including
CC alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated
CC proteins (PubMed:10506173, PubMed:15280042, PubMed:20498373,
CC PubMed:9584846). Has lipid phosphatase activity and inactivates
CC lysophosphatidic acid in seminal plasma (PubMed:10506173,
CC PubMed:15280042). {ECO:0000269|PubMed:10506173,
CC ECO:0000269|PubMed:15280042, ECO:0000269|PubMed:20498373,
CC ECO:0000269|PubMed:9584846}.
CC -!- FUNCTION: [Isoform 2]: Tyrosine phosphatase that acts as a tumor
CC suppressor of prostate cancer through dephosphorylation of ERBB2 and
CC deactivation of MAPK-mediated signaling (PubMed:20498373). In addition
CC to its tyrosine phosphatase activity has ecto-5'-nucleotidase activity
CC in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP
CC which acts as a pain suppressor (By similarity).
CC {ECO:0000250|UniProtKB:Q8CE08, ECO:0000269|PubMed:20498373}.
CC -!- FUNCTION: [PAPf39]: (Microbial infection) Forms amyloid beta-sheet
CC fibrils in semen. These fibrils, termed SEVI (semen-derived enhancer of
CC viral infection) capture HIV virions, attach them to target cells and
CC enhance infection (PubMed:18083097, PubMed:19451623, PubMed:19897482).
CC SEVI amyloid fibrils are degraded by polyphenol epigallocatechin-3-
CC gallate (EGCG), a constituent of green tea (PubMed:19451623). Target
CC cell attachment and enhancement of HIV infection is inhibited by surfen
CC (PubMed:19897482). Also similarly boosts XMRV (xenotropic murine
CC leukemia virus-related virus) infection (PubMed:19403677).
CC {ECO:0000269|PubMed:18083097, ECO:0000269|PubMed:19403677,
CC ECO:0000269|PubMed:19451623, ECO:0000269|PubMed:19897482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:15280042,
CC ECO:0000269|PubMed:9584846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000269|PubMed:10506173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000305|PubMed:10506173};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q8CE08};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:20498373};
CC -!- ACTIVITY REGULATION: Phosphatase activity inhibited by L(+)-tartrate,
CC and by its derivative, alpha-benzylaminobenzylphosphonic acid.
CC {ECO:0000269|PubMed:9584846}.
CC -!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
CC activity. {ECO:0000250|UniProtKB:P20646}.
CC -!- INTERACTION:
CC P15309; P15309: ACP3; NbExp=4; IntAct=EBI-1222012, EBI-1222012;
CC P15309; P04626: ERBB2; NbExp=2; IntAct=EBI-1222012, EBI-641062;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000305|PubMed:17638863}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:20498373}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863,
CC ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:20498373}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:20498373}. Note=Appears to shuttle between
CC the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at
CC cell membrane and in intracellular vesicles (PubMed:17638863).
CC Colocalizes with LAMP2 on the lysosome membrane (PubMed:17897319).
CC {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Secreted PAP, sPAP;
CC IsoId=P15309-1; Sequence=Displayed;
CC Name=2; Synonyms=TMPase, TM-PAP {ECO:0000303|PubMed:17638863}, cellular
CC PAP, cPAP, cPAcP {ECO:0000303|PubMed:20498373};
CC IsoId=P15309-2; Sequence=VSP_036023;
CC Name=3;
CC IsoId=P15309-3; Sequence=VSP_053360;
CC -!- TISSUE SPECIFICITY: Highly expressed in the prostate, restricted to
CC glandular and ductal epithelial cells. Also expressed in bladder,
CC kidney, pancreas, lung, cervix, testis and ovary. Weak expression in a
CC subset of pancreatic islet cells, squamous epithelia, the pilosebaceous
CC unit, colonic neuroendocrine cells and skin adnexal structures. Low
CC expression in prostate carcinoma cells and tissues.
CC {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:21487525}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed. Expressed in the
CC sarcolemma of skeletal muscle. {ECO:0000269|PubMed:17638863}.
CC -!- PTM: N-glycosylated. High mannose content, partially sialylated and
CC fucosylated biantennary complex. Also fucosylated with partially
CC sialylated triantennary complex oligosaccharides.
CC {ECO:0000269|PubMed:10639192, ECO:0000269|PubMed:12525165}.
CC -!- PTM: Proteolytically cleaved in seminal fluid to produce several
CC peptides. Peptide PAPf39, the most prominent, forms amyloid beta-sheet
CC fibrils, SEVI (semen-derived enhancer of viral infection).
CC {ECO:0000269|PubMed:18083097}.
CC -!- MISCELLANEOUS: Has been used as a diagnostic tool for staging
CC metastatic prostatic cancer.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; M97589; AAA60021.1; -; Genomic_DNA.
DR EMBL; M97580; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97581; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97582; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97583; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97584; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97585; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97586; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97587; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M97588; AAA60021.1; JOINED; Genomic_DNA.
DR EMBL; M34840; AAA69694.1; -; mRNA.
DR EMBL; M24902; AAA60022.1; -; mRNA.
DR EMBL; X52174; CAA36422.1; -; mRNA.
DR EMBL; X53605; CAA37673.1; -; mRNA.
DR EMBL; U07097; AAB60640.1; -; Genomic_DNA.
DR EMBL; U07083; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07085; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07086; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07088; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07091; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07092; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07093; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; U07095; AAB60640.1; JOINED; Genomic_DNA.
DR EMBL; AB102888; BAD89417.1; -; mRNA.
DR EMBL; AK300540; BAG62248.1; -; mRNA.
DR EMBL; AC020633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79203.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79205.1; -; Genomic_DNA.
DR EMBL; BC007460; AAH07460.1; -; mRNA.
DR EMBL; BC008493; AAH08493.1; -; mRNA.
DR EMBL; BC016344; AAH16344.1; -; mRNA.
DR CCDS; CCDS3073.1; -. [P15309-1]
DR CCDS; CCDS46916.1; -. [P15309-2]
DR CCDS; CCDS77818.1; -. [P15309-3]
DR PIR; JH0610; JH0610.
DR RefSeq; NP_001090.2; NM_001099.4. [P15309-1]
DR RefSeq; NP_001127666.1; NM_001134194.1. [P15309-2]
DR RefSeq; NP_001278966.1; NM_001292037.1. [P15309-3]
DR PDB; 1CVI; X-ray; 3.20 A; A/B/C/D=33-374.
DR PDB; 1ND5; X-ray; 2.90 A; A/B/C/D=33-386.
DR PDB; 1ND6; X-ray; 2.40 A; A/B/C/D=33-386.
DR PDB; 2HPA; X-ray; 2.90 A; A/B/C/D=33-374.
DR PDB; 2L3H; NMR; -; A=248-286.
DR PDB; 2L77; NMR; -; A=248-286.
DR PDB; 2L79; NMR; -; A=248-286.
DR PDB; 2MG0; NMR; -; A=262-270.
DR PDB; 3PPD; X-ray; 1.50 A; A=260-265.
DR PDBsum; 1CVI; -.
DR PDBsum; 1ND5; -.
DR PDBsum; 1ND6; -.
DR PDBsum; 2HPA; -.
DR PDBsum; 2L3H; -.
DR PDBsum; 2L77; -.
DR PDBsum; 2L79; -.
DR PDBsum; 2MG0; -.
DR PDBsum; 3PPD; -.
DR AlphaFoldDB; P15309; -.
DR BMRB; P15309; -.
DR SMR; P15309; -.
DR BioGRID; 106571; 175.
DR ComplexPortal; CPX-120; Prostatic acid phosphatase complex.
DR IntAct; P15309; 22.
DR MINT; P15309; -.
DR STRING; 9606.ENSP00000323036; -.
DR BindingDB; P15309; -.
DR ChEMBL; CHEMBL2633; -.
DR DrugBank; DB03390; (2R,3R)-2,3-Dihydroxy-4-oxo-4-(propylamino)butanoic acid.
DR DrugBank; DB03577; Alpha-Benzyl-Aminobenzyl-Phosphonic Acid.
DR DrugBank; DB06688; Sipuleucel-T.
DR DrugCentral; P15309; -.
DR SwissLipids; SLP:000001295; -. [P15309-1]
DR DEPOD; ACPP; -.
DR GlyConnect; 2001; 6 N-Linked glycans (2 sites).
DR GlyGen; P15309; 3 sites, 20 N-linked glycans (2 sites).
DR iPTMnet; P15309; -.
DR PhosphoSitePlus; P15309; -.
DR BioMuta; ACPP; -.
DR DMDM; 130730; -.
DR EPD; P15309; -.
DR jPOST; P15309; -.
DR MassIVE; P15309; -.
DR MaxQB; P15309; -.
DR PaxDb; P15309; -.
DR PeptideAtlas; P15309; -.
DR PRIDE; P15309; -.
DR ProteomicsDB; 53126; -. [P15309-1]
DR ProteomicsDB; 53127; -. [P15309-2]
DR ProteomicsDB; 62789; -.
DR Antibodypedia; 1343; 962 antibodies from 43 providers.
DR DNASU; 55; -.
DR Ensembl; ENST00000336375.10; ENSP00000337471.5; ENSG00000014257.16. [P15309-1]
DR Ensembl; ENST00000351273.11; ENSP00000323036.8; ENSG00000014257.16. [P15309-2]
DR Ensembl; ENST00000475741.5; ENSP00000417744.1; ENSG00000014257.16. [P15309-3]
DR GeneID; 55; -.
DR KEGG; hsa:55; -.
DR MANE-Select; ENST00000336375.10; ENSP00000337471.5; NM_001099.5; NP_001090.2.
DR UCSC; uc003eon.4; human. [P15309-1]
DR CTD; 55; -.
DR DisGeNET; 55; -.
DR GeneCards; ACP3; -.
DR HGNC; HGNC:125; ACP3.
DR HPA; ENSG00000014257; Tissue enriched (prostate).
DR MIM; 171790; gene.
DR neXtProt; NX_P15309; -.
DR OpenTargets; ENSG00000014257; -.
DR VEuPathDB; HostDB:ENSG00000014257; -.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000160450; -.
DR HOGENOM; CLU_030431_1_1_1; -.
DR InParanoid; P15309; -.
DR OMA; GMKQHYE; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; P15309; -.
DR TreeFam; TF312893; -.
DR BRENDA; 3.1.3.2; 2681.
DR PathwayCommons; P15309; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P15309; -.
DR SignaLink; P15309; -.
DR BioGRID-ORCS; 55; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; ACPP; human.
DR EvolutionaryTrace; P15309; -.
DR GeneWiki; Prostatic_acid_phosphatase; -.
DR GenomeRNAi; 55; -.
DR Pharos; P15309; Tchem.
DR PRO; PR:P15309; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P15309; protein.
DR Bgee; ENSG00000014257; Expressed in prostate gland and 132 other tissues.
DR ExpressionAtlas; P15309; baseline and differential.
DR Genevisible; P15309; HS.
DR GO; GO:1904097; C:acid phosphatase complex; IPI:ComplexPortal.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1904144; C:phosphatidylinositol phosphate phosphatase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0012506; C:vesicle membrane; ISS:CAFA.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042131; F:thiamine phosphate phosphatase activity; ISS:CAFA.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:Ensembl.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:Ensembl.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; ISS:CAFA.
DR CDD; cd07061; HP_HAP_like; 1.
DR DisProt; DP00628; -.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amyloid; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid metabolism; Lysosome; Membrane; Nucleus; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:10639192"
FT CHAIN 33..386
FT /note="Prostatic acid phosphatase"
FT /id="PRO_0000023963"
FT PEPTIDE 248..286
FT /note="PAPf39"
FT /evidence="ECO:0000269|PubMed:18083097"
FT /id="PRO_0000411250"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:1989985"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:1989985"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9804805"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9804805"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9804805"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9804805"
FT SITE 49
FT /note="Important for substrate specificity"
FT SITE 138
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 144
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 206
FT /note="Required for structural stability"
FT /evidence="ECO:0000269|PubMed:9584846"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10639192"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10639192,
FT ECO:0000269|PubMed:12525165"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12525165"
FT DISULFID 161..372
FT /evidence="ECO:0000269|PubMed:12525165,
FT ECO:0000269|PubMed:1989985"
FT DISULFID 215..313
FT /evidence="ECO:0000269|PubMed:1989985"
FT DISULFID 347..351
FT /evidence="ECO:0000269|PubMed:12525165,
FT ECO:0000269|PubMed:1989985"
FT VAR_SEQ 153..185
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_053360"
FT VAR_SEQ 380..386
FT /note="GTEDSTD -> VLKVIFAVAFCLISAVLMVLLFIHIRRGLCWQRESYGNI
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036023"
FT VARIANT 15
FT /note="S -> N (in dbSNP:rs17850347)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047960"
FT VARIANT 124
FT /note="F -> V (in dbSNP:rs17856254)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047961"
FT VARIANT 226
FT /note="W -> R (in dbSNP:rs17856253)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047962"
FT VARIANT 330
FT /note="Y -> H (in dbSNP:rs17851392)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047963"
FT VARIANT 360
FT /note="V -> A (in dbSNP:rs17850198)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047964"
FT MUTAGEN 206
FT /note="W->F: Greatly reduced enzyme activity, marked
FT decrease in structural stability, and increased binding of
FT the inhibitor, L(+)-tartrate."
FT /evidence="ECO:0000269|PubMed:9584846"
FT MUTAGEN 206
FT /note="W->L: Reduced enzyme activity, marked decrease in
FT structural stability, and increased binding of the
FT inhibitor, L(+)-tartrate."
FT /evidence="ECO:0000269|PubMed:9584846"
FT CONFLICT 15..24
FT /note="SLGFLFLLFF -> AFASCFCFFC (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT CONFLICT 15..24
FT /note="SLGFLFLLFF -> ALASCFCFFC (in Ref. 3; AAA60022 and 4;
FT CAA36422)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="D -> H (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..73
FT /note="GFGQLTQL -> RIWPTHPA (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..73
FT /note="GFGQLTQL -> WIWPTHPA (in Ref. 4; CAA36422)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="E -> D (in Ref. 3; AAA60022)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> R (in Ref. 3; AAA60022)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> E (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="P -> R (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="P -> A (in Ref. 4; CAA36422)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="C -> S (in Ref. 3; AAA60022)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> T (in Ref. 3; AAA60022)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="C -> V (in Ref. 3; AAA60022)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> N (in Ref. 5; CAA37673)"
FT /evidence="ECO:0000305"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:1ND6"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1CVI"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1ND5"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:1ND6"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1CVI"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1ND5"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1ND6"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1ND6"
SQ 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