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 27-MAR-2024, entry version 234. 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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7UW6; X-ray; 1.50 A; A=2-158. 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 PDBsum; 7UW6; -. DR AlphaFoldDB; P24666; -. DR BMRB; P24666; -. DR SMR; P24666; -. DR BioGRID; 106568; 111. DR IntAct; P24666; 24. DR MINT; P24666; -. DR STRING; 9606.ENSP00000272067; -. DR BindingDB; P24666; -. DR ChEMBL; CHEMBL4903; -. DR DrugBank; DB04214; 4-Nitrophenyl Phosphate. DR DrugBank; DB00173; Adenine. DR DEPOD; ACP1; -. DR GlyGen; P24666; 1 site, 1 O-linked glycan (1 site). 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 PeptideAtlas; P24666; -. DR ProteomicsDB; 54220; -. [P24666-1] DR ProteomicsDB; 54221; -. [P24666-2] DR ProteomicsDB; 54222; -. [P24666-3] DR ProteomicsDB; 6027; -. DR Pumba; P24666; -. DR Antibodypedia; 12168; 438 antibodies from 34 providers. DR DNASU; 52; -. DR Ensembl; ENST00000272065.10; ENSP00000272065.5; ENSG00000143727.16. [P24666-1] DR Ensembl; ENST00000272067.11; 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 AGR; HGNC:122; -. 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; QGEWHVE; -. DR OrthoDB; 5470890at2759; -. 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 1166 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 202 other cell types or tissues. DR ExpressionAtlas; P24666; baseline and differential. 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 CDD; cd16343; LMWPTP; 1. DR Gene3D; 3.40.50.2300; -; 1. 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 PANTHER; PTHR11717:SF35; LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11717; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1. DR Pfam; PF01451; LMWPc; 1. DR PRINTS; PR00719; LMWPTPASE. DR PRINTS; PR00720; MAMMALPTPASE. DR SMART; SM00226; LMWPc; 1. DR SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1. DR Genevisible; P24666; HS. 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 //