PPAC_HUMAN
ID PPAC_HUMAN Reviewed; 158 AA.
AC P24666; A8K1L9; B5MCC7; P24667; Q16035; Q16036; Q16725; Q3KQX8; Q53RU0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase {ECO:0000305};
DE Short=LMW-PTP;
DE Short=LMW-PTPase;
DE EC=3.1.3.48 {ECO:0000305|PubMed:9705307};
DE AltName: Full=Adipocyte acid phosphatase;
DE AltName: Full=Low molecular weight cytosolic acid phosphatase;
DE EC=3.1.3.2 {ECO:0000305|PubMed:10336608, ECO:0000305|PubMed:9038134};
DE AltName: Full=Red cell acid phosphatase 1;
GN Name=ACP1 {ECO:0000312|HGNC:HGNC:122};
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 PROTEIN SEQUENCE (ALLELE B; ISOFORMS 1 AND 2), CLEAVAGE OF INITIATOR
RP METHIONINE, AND ACETYLATION AT ALA-2.
RX PubMed=1939112; DOI=10.1016/s0021-9258(18)54754-2;
RA Dissing J., Johnsen A.H., Sensabaugh G.F.;
RT "Human red cell acid phosphatase (ACP1). The amino acid sequence of the two
RT isozymes Bf and Bs encoded by the ACP1*B allele.";
RL J. Biol. Chem. 266:20619-20625(1991).
RN [2]
RP PROTEIN SEQUENCE (ALLELES A AND C; ISOFORMS 1 AND 2).
RX PubMed=1627603; DOI=10.1016/0167-4838(92)90155-7;
RA Dissing J., Johnsen A.H.;
RT "Human red cell acid phosphatase (ACP1): the primary structure of the two
RT pairs of isozymes encoded by the ACP1*A and ACP1*C alleles.";
RL Biochim. Biophys. Acta 1121:261-268(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=1587862; DOI=10.1016/s0021-9258(19)50097-7;
RA Wo Y.-Y.P., McCormack A.L., Shabonowitz J., Hunt D.F., Davis J.P.,
RA Mitchell G.L., van Etten R.L.;
RT "Sequencing, cloning, and expression of human red cell-type acid
RT phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.";
RL J. Biol. Chem. 267:10856-10865(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8586411; DOI=10.1006/geno.1995.9893;
RA Bryson G.L.M., Massa H., Trask B.J., van Etten R.L.;
RT "Gene structure, sequence, and chromosomal localization of the human red
RT cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene,
RT ACP1.";
RL Genomics 30:133-140(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipocyte;
RX PubMed=1304913; DOI=10.1002/pro.5560010603;
RA Shekels L.L., Smith A.J., van Etten R.L., Bernlohr D.A.;
RT "Identification of the adipocyte acid phosphatase as a PAO-sensitive
RT tyrosyl phosphatase.";
RL Protein Sci. 1:710-721(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP TYR-132 AND TYR-133, MUTAGENESIS OF CYS-13; TYR-132 AND TYR-133, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9038134; DOI=10.1074/jbc.272.9.5371;
RA Tailor P., Gilman J., Williams S., Couture C., Mustelin T.;
RT "Regulation of the low molecular weight phosphotyrosine phosphatase by
RT phosphorylation at tyrosines 131 and 132.";
RL J. Biol. Chem. 272:5371-5374(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3), FUNCTION (ISOFORM 3), CATALYTIC ACTIVITY,
RP AND FUNCTION.
RX PubMed=10336608; DOI=10.1046/j.1432-1327.1999.00353.x;
RA Tailor P., Gilman J., Williams S., Mustelin T.;
RT "A novel isoform of the low molecular weight phosphotyrosine phosphatase,
RT LMPTP-C, arising from alternative mRNA splicing.";
RL Eur. J. Biochem. 262:277-282(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Skeletal muscle;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R.,
RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T.,
RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K.,
RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T.,
RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T.,
RA Sugano S.;
RT "Diversification of transcriptional modulation: large-scale identification
RT and characterization of putative alternative promoters of human genes.";
RL Genome Res. 16:55-65(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-106.
RC TISSUE=Muscle, and Placenta;
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 [14]
RP PROTEIN SEQUENCE OF 42-59, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-158 (ISOFORMS 1/2).
RC TISSUE=Blood;
RX PubMed=8364553; DOI=10.1093/hmg/2.7.1079-a;
RA Sensabaugh G.F., Lazaruk K.A.;
RT "A TaqI site identifies the *A allele at the ACP1 locus.";
RL Hum. Mol. Genet. 2:1079-1079(1993).
RN [16]
RP INTERACTION WITH EPHB1.
RX PubMed=9499402; DOI=10.1101/gad.12.5.667;
RA Stein E., Lane A.A., Cerretti D.P., Schoecklmann H.O., Schroff A.D.,
RA Van Etten R.L., Daniel T.O.;
RT "Eph receptors discriminate specific ligand oligomers to determine
RT alternative signaling complexes, attachment, and assembly responses.";
RL Genes Dev. 12:667-678(1998).
RN [17]
RP INTERACTION WITH EPHA2.
RX PubMed=12167657; DOI=10.1074/jbc.m207127200;
RA Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.;
RT "Regulation of the EphA2 kinase by the low molecular weight tyrosine
RT phosphatase induces transformation.";
RL J. Biol. Chem. 277:39274-39279(2002).
RN [18]
RP INTERACTION WITH SPTAN1.
RX PubMed=11971983; DOI=10.1128/mcb.22.10.3527-3536.2002;
RA Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O.,
RA Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B.,
RA Lecomte M.-C.;
RT "Tyrosine phosphorylation regulates alpha II spectrin cleavage by
RT calpain.";
RL Mol. Cell. Biol. 22:3527-3536(2002).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9705307; DOI=10.1074/jbc.273.34.21714;
RA Zhang M., Stauffacher C.V., Lin D., van Etten R.L.;
RT "Crystal structure of a human low molecular weight phosphotyrosyl
RT phosphatase. Implications for substrate specificity.";
RL J. Biol. Chem. 273:21714-21720(1998).
CC -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC phosphates and natural and synthetic acyl phosphates with differences
CC in substrate specificity between isoform 1 and isoform 2.
CC {ECO:0000269|PubMed:10336608, ECO:0000269|PubMed:9705307}.
CC -!- FUNCTION: [Isoform 3]: Does not possess phosphatase activity.
CC {ECO:0000269|PubMed:10336608}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000305|PubMed:9705307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000305|PubMed:9705307};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000305|PubMed:9705307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000305|PubMed:9705307};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000305|PubMed:10336608, ECO:0000305|PubMed:9705307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000305|PubMed:10336608, ECO:0000305|PubMed:9705307};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000305|PubMed:10336608, ECO:0000305|PubMed:9038134,
CC ECO:0000305|PubMed:9705307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000305|PubMed:10336608, ECO:0000305|PubMed:9038134,
CC ECO:0000305|PubMed:9705307};
CC -!- ACTIVITY REGULATION: Inhibited by sulfhydryl reagents.
CC -!- SUBUNIT: Interacts with EPHA2; dephosphorylates EPHA2. Interacts with
CC EPHB1. {ECO:0000269|PubMed:12167657, ECO:0000269|PubMed:9499402}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with the SH3 domain of SPTAN1. There is
CC no interaction observed for isoforms 2 or 3.
CC {ECO:0000269|PubMed:11971983}.
CC -!- INTERACTION:
CC P24666-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-25910301, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=The ratio of isoform 1 to isoform 2 is 2:1 in allele A, 4:1
CC in allele B and 1:4 in allele C.;
CC Name=1; Synonyms=F, A, Alpha, LMPTP-A {ECO:0000303|PubMed:10336608},
CC HCPTP-A {ECO:0000303|PubMed:9705307};
CC IsoId=P24666-1; Sequence=Displayed;
CC Name=2; Synonyms=S, B, Beta, LMPTP-B {ECO:0000303|PubMed:10336608},
CC HCPTP-B {ECO:0000303|PubMed:9705307};
CC IsoId=P24666-2, P24667-1;
CC Sequence=VSP_010087;
CC Name=3; Synonyms=C, LMPTP-C {ECO:0000303|PubMed:10336608};
CC IsoId=P24666-3; Sequence=VSP_010088;
CC Name=4;
CC IsoId=P24666-4; Sequence=VSP_054074, VSP_054075;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in T-lymphocytes.
CC {ECO:0000269|PubMed:9038134}.
CC -!- PTM: [Isoform 2]: Phosphorylated by LCK (PubMed:9038134,
CC PubMed:10336608). Phosphorylation at Tyr-132 increases its phosphatase
CC activity (PubMed:9038134). {ECO:0000269|PubMed:10336608,
CC ECO:0000269|PubMed:9038134}.
CC -!- PTM: [Isoform 3]: Not phosphorylated. {ECO:0000269|PubMed:10336608}.
CC -!- POLYMORPHISM: ACP1 is genetically polymorphic. Three common alleles are
CC known in Caucasians: ACP1*A, ACP1*B and ACP1*C. They give rise to six
CC different phenotypes. Each allele appears to encode two
CC electrophoretically different isozymes, F and S, which are produced in
CC allele-specific ratios (PubMed:1939112). The sequence shown is that of
CC allele ACP1*B and allele ACP1*C. {ECO:0000269|PubMed:1939112}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; M83653; AAB59354.1; -; mRNA.
DR EMBL; M83654; AAB59355.1; -; mRNA.
DR EMBL; U25849; AAC52067.1; -; Genomic_DNA.
DR EMBL; U25847; AAC52067.1; JOINED; Genomic_DNA.
DR EMBL; U25848; AAC52067.1; JOINED; Genomic_DNA.
DR EMBL; S62884; AAB27085.1; -; mRNA.
DR EMBL; S62885; AAB27086.1; -; mRNA.
DR EMBL; M87545; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT007136; AAP35800.1; -; mRNA.
DR EMBL; AK289934; BAF82623.1; -; mRNA.
DR EMBL; AK291861; BAF84550.1; -; mRNA.
DR EMBL; BP363227; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC079779; AAY14958.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01112.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01116.1; -; Genomic_DNA.
DR EMBL; BC007422; AAH07422.1; -; mRNA.
DR EMBL; BC106011; AAI06012.1; -; mRNA.
DR EMBL; L06508; AAB59628.1; -; Genomic_DNA.
DR CCDS; CCDS1639.1; -. [P24666-1]
DR CCDS; CCDS1640.1; -. [P24666-2]
DR CCDS; CCDS46217.1; -. [P24666-4]
DR PIR; A38148; A38148.
DR PIR; B38148; B38148.
DR RefSeq; NP_004291.1; NM_004300.3. [P24666-1]
DR RefSeq; NP_009030.1; NM_007099.3. [P24666-2]
DR PDB; 1XWW; X-ray; 1.63 A; A=2-158.
DR PDB; 3N8I; X-ray; 1.50 A; A=2-158.
DR PDB; 4Z99; X-ray; 2.30 A; A=1-158.
DR PDB; 4Z9A; X-ray; 2.10 A; A=1-158.
DR PDB; 4Z9B; X-ray; 2.41 A; A=1-158.
DR PDB; 5JNR; X-ray; 2.00 A; A=1-158.
DR PDB; 5JNS; X-ray; 1.80 A; A=1-158.
DR PDB; 5JNT; X-ray; 1.45 A; A=1-158.
DR PDB; 5KQG; X-ray; 1.50 A; A=1-158.
DR PDB; 5KQL; X-ray; 1.45 A; A=1-158.
DR PDB; 5KQM; X-ray; 1.91 A; A=1-158.
DR PDB; 5KQP; X-ray; 2.05 A; A=1-158.
DR PDB; 5PNT; X-ray; 2.20 A; A=2-158.
DR PDB; 6Y2V; X-ray; 2.00 A; A=1-158.
DR PDB; 6Y2W; X-ray; 1.77 A; A=2-158.
DR PDB; 7KH8; X-ray; 1.30 A; A/B=5-158.
DR PDBsum; 1XWW; -.
DR PDBsum; 3N8I; -.
DR PDBsum; 4Z99; -.
DR PDBsum; 4Z9A; -.
DR PDBsum; 4Z9B; -.
DR PDBsum; 5JNR; -.
DR PDBsum; 5JNS; -.
DR PDBsum; 5JNT; -.
DR PDBsum; 5KQG; -.
DR PDBsum; 5KQL; -.
DR PDBsum; 5KQM; -.
DR PDBsum; 5KQP; -.
DR PDBsum; 5PNT; -.
DR PDBsum; 6Y2V; -.
DR PDBsum; 6Y2W; -.
DR PDBsum; 7KH8; -.
DR AlphaFoldDB; P24666; -.
DR BMRB; P24666; -.
DR SMR; P24666; -.
DR BioGRID; 106568; 100.
DR IntAct; P24666; 22.
DR MINT; P24666; -.
DR BindingDB; P24666; -.
DR ChEMBL; CHEMBL4903; -.
DR DrugBank; DB04214; 4-Nitrophenyl Phosphate.
DR DrugBank; DB00173; Adenine.
DR DEPOD; ACP1; -.
DR iPTMnet; P24666; -.
DR MetOSite; P24666; -.
DR PhosphoSitePlus; P24666; -.
DR SwissPalm; P24666; -.
DR BioMuta; ACP1; -.
DR DMDM; 1709543; -.
DR REPRODUCTION-2DPAGE; IPI00218847; -.
DR REPRODUCTION-2DPAGE; IPI00219861; -.
DR EPD; P24666; -.
DR jPOST; P24666; -.
DR MassIVE; P24666; -.
DR MaxQB; P24666; -.
DR PaxDb; P24666; -.
DR PeptideAtlas; P24666; -.
DR PRIDE; P24666; -.
DR ProteomicsDB; 54220; -. [P24666-1]
DR ProteomicsDB; 54221; -. [P24666-2]
DR ProteomicsDB; 54222; -. [P24666-3]
DR ProteomicsDB; 6027; -.
DR Antibodypedia; 12168; 403 antibodies from 34 providers.
DR DNASU; 52; -.
DR Ensembl; ENST00000272065.10; ENSP00000272065.5; ENSG00000143727.16. [P24666-1]
DR Ensembl; ENST00000272067.10; ENSP00000272067.6; ENSG00000143727.16. [P24666-2]
DR Ensembl; ENST00000407983.7; ENSP00000385404.3; ENSG00000143727.16. [P24666-4]
DR GeneID; 52; -.
DR KEGG; hsa:52; -.
DR MANE-Select; ENST00000272065.10; ENSP00000272065.5; NM_004300.4; NP_004291.1.
DR UCSC; uc002qwd.3; human. [P24666-1]
DR CTD; 52; -.
DR DisGeNET; 52; -.
DR GeneCards; ACP1; -.
DR HGNC; HGNC:122; ACP1.
DR HPA; ENSG00000143727; Low tissue specificity.
DR MIM; 171500; gene.
DR neXtProt; NX_P24666; -.
DR OpenTargets; ENSG00000143727; -.
DR PharmGKB; PA24446; -.
DR VEuPathDB; HostDB:ENSG00000143727; -.
DR GeneTree; ENSGT00940000158351; -.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; P24666; -.
DR OMA; YQQVTRF; -.
DR PhylomeDB; P24666; -.
DR TreeFam; TF353727; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P24666; -.
DR SignaLink; P24666; -.
DR SIGNOR; P24666; -.
DR BioGRID-ORCS; 52; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; ACP1; human.
DR EvolutionaryTrace; P24666; -.
DR GeneWiki; ACP1; -.
DR GenomeRNAi; 52; -.
DR Pharos; P24666; Tchem.
DR PRO; PR:P24666; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P24666; protein.
DR Bgee; ENSG00000143727; Expressed in sperm and 200 other tissues.
DR ExpressionAtlas; P24666; baseline and differential.
DR Genevisible; P24666; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR PRINTS; PR00720; MAMMALPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1939112"
FT CHAIN 2..158
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase"
FT /id="PRO_0000046558"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 19
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1939112"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9038134"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9038134"
FT VAR_SEQ 41..74
FT /note="RVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHV -> VIDSGAVSDWNVGR
FT SPDPRAVSCLRNHGIHTAHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1304913,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1587862, ECO:0000303|Ref.8"
FT /id="VSP_010087"
FT VAR_SEQ 41..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_010088"
FT VAR_SEQ 78..112
FT /note="ITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKA -> VPSLDLKLCVLCF
FT SGSLTAVLFLTGTWAGPQTQEL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16344560"
FT /id="VSP_054074"
FT VAR_SEQ 113..158
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16344560"
FT /id="VSP_054075"
FT VARIANT 7
FT /note="K -> N (in dbSNP:rs11691572)"
FT /id="VAR_050526"
FT VARIANT 106
FT /note="Q -> R (in allele ACP1*A; dbSNP:rs79716074)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_006171"
FT VARIANT 137
FT /note="S -> F (in dbSNP:rs35569198)"
FT /id="VAR_050527"
FT MUTAGEN 13
FT /note="C->S: Inactive."
FT /evidence="ECO:0000269|PubMed:9038134"
FT MUTAGEN 132
FT /note="Y->F: Reduced phosphorylation and activity."
FT /evidence="ECO:0000269|PubMed:9038134"
FT MUTAGEN 133
FT /note="Y->F: Reduced phosphorylation. No effect on
FT activity."
FT /evidence="ECO:0000269|PubMed:9038134"
FT CONFLICT 2..6
FT /note="AEQAT -> PRRGR (in Ref. 5; AAB27086)"
FT /evidence="ECO:0000305"
FT CONFLICT 2
FT /note="A -> P (in Ref. 10; BP363227)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..20
FT /note="CLGNICRS -> PARREAAR (in Ref. 5; AAB27085)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="T -> W (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..18
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:7KH8"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:7KH8"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:7KH8"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:7KH8"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:7KH8"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:7KH8"
SQ SEQUENCE 158 AA; 18042 MW; 46617BD799313EED CRC64;
MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG
QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY
DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH
