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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
 
 
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