ID PPAC_HUMAN Reviewed; 158 AA. AC P24666; A8K1L9; B5MCC7; P24667; Q16035; Q16036; Q16725; Q3KQX8; AC Q53RU0; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 173. DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase; DE Short=LMW-PTP; DE Short=LMW-PTPase; DE EC=3.1.3.48; DE AltName: Full=Adipocyte acid phosphatase; DE AltName: Full=Low molecular weight cytosolic acid phosphatase; DE EC=3.1.3.2; DE AltName: Full=Red cell acid phosphatase 1; GN Name=ACP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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; RA Dissing J., Johnsen A.H., Sensabaugh G.F.; RT "Human red cell acid phosphatase (ACP1). The amino acid sequence of RT the two 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 RT two 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; 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 RT red cell-type low-molecular-weight acid phosphotyrosyl phosphatase RT gene, 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 RP AT TYR-132 AND TYR-133, AND MUTAGENESIS OF CYS-13; TYR-132 AND RP TYR-133. 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). 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 RT phosphatase, 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M., RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.; RT "Diversification of transcriptional modulation: large-scale RT identification and characterization of putative alternative promoters RT 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Buerckstuemmer T., 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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., RA Ayoub D., 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. Isoform 3 CC does not possess phosphatase activity. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol + CC phosphate. CC -!- ENZYME REGULATION: Inhibited by sulfhydryl reagents. CC -!- SUBUNIT: Isoform 1 interacts with the SH3 domain of SPTAN1. There CC is no interaction observed for isoforms 2 or 3. Interacts with CC EPHA2; dephosphorylates EPHA2. Interacts with EPHB1. CC {ECO:0000269|PubMed:11971983, ECO:0000269|PubMed:12167657, CC ECO:0000269|PubMed:9499402}. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-717701, EBI-717701; 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, CC 4:1 in allele B and 1:4 in allele C.; CC Name=1; Synonyms=F, A, Alpha, LMPTP-A, HCPTP-A; CC IsoId=P24666-1; Sequence=Displayed; CC Name=2; Synonyms=S, B, Beta, LMPTP-B, HCPTP-B; CC IsoId=P24666-2, P24667-1; CC Sequence=VSP_010087; CC Name=3; Synonyms=C, LMPTP-C; CC IsoId=P24666-3; Sequence=VSP_010088; CC Name=4; CC IsoId=P24666-4; Sequence=VSP_054074, VSP_054075; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: T-lymphocytes express only isoform 2. CC {ECO:0000269|PubMed:9038134}. CC -!- POLYMORPHISM: ACP1 is genetically polymorphic. Three common CC alleles are known in Caucasians: ACP1*A, ACP1*B and ACP1*C. They CC give rise to six different phenotypes. Each allele appears to CC encode two electrophoretically different isozymes, F and S, which CC are produced in allele-specific ratios. The sequence shown is that CC of allele ACP1*B and allele ACP1*C. CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine CC protein 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_001035739.1; NM_001040649.2. [P24666-4] DR RefSeq; NP_004291.1; NM_004300.3. [P24666-1] DR RefSeq; NP_009030.1; NM_007099.3. [P24666-2] DR RefSeq; XP_011508665.1; XM_011510363.1. [P24666-2] DR UniGene; Hs.558296; -. 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; 5PNT; X-ray; 2.20 A; A=2-158. DR PDBsum; 1XWW; -. DR PDBsum; 3N8I; -. DR PDBsum; 4Z99; -. DR PDBsum; 4Z9A; -. DR PDBsum; 4Z9B; -. DR PDBsum; 5PNT; -. DR ProteinModelPortal; P24666; -. DR SMR; P24666; 5-158. DR BioGrid; 106568; 21. DR IntAct; P24666; 7. DR STRING; 9606.ENSP00000272065; -. DR BindingDB; P24666; -. DR ChEMBL; CHEMBL4903; -. DR DrugBank; DB00173; Adenine. DR DEPOD; P24666; -. DR PhosphoSite; P24666; -. DR BioMuta; ACP1; -. DR DMDM; 1709543; -. DR REPRODUCTION-2DPAGE; IPI00218847; -. DR REPRODUCTION-2DPAGE; IPI00219861; -. DR MaxQB; P24666; -. DR PaxDb; P24666; -. DR PRIDE; P24666; -. DR DNASU; 52; -. DR Ensembl; ENST00000272065; ENSP00000272065; ENSG00000143727. [P24666-1] DR Ensembl; ENST00000272067; ENSP00000272067; ENSG00000143727. [P24666-2] DR Ensembl; ENST00000407983; ENSP00000385404; ENSG00000143727. [P24666-4] DR GeneID; 52; -. DR KEGG; hsa:52; -. DR UCSC; uc002qwf.3; human. [P24666-1] DR UCSC; uc002qwg.3; human. [P24666-2] DR CTD; 52; -. DR GeneCards; ACP1; -. DR HGNC; HGNC:122; ACP1. DR HPA; HPA016754; -. DR MIM; 171500; gene. DR neXtProt; NX_P24666; -. DR PharmGKB; PA24446; -. DR eggNOG; KOG3217; Eukaryota. DR eggNOG; COG0394; LUCA. DR GeneTree; ENSGT00500000044891; -. DR HOGENOM; HOG000074091; -. DR HOVERGEN; HBG007540; -. DR InParanoid; P24666; -. DR KO; K14394; -. DR OMA; CEIAPEM; -. DR OrthoDB; EOG7QZGCG; -. DR PhylomeDB; P24666; -. DR TreeFam; TF353727; -. DR BRENDA; 3.1.3.48; 2681. DR SignaLink; P24666; -. DR EvolutionaryTrace; P24666; -. DR GeneWiki; ACP1; -. DR GenomeRNAi; 52; -. DR NextBio; 205; -. DR PRO; PR:P24666; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; P24666; -. DR CleanEx; HS_ACP1; -. 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:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0003993; F:acid phosphatase activity; TAS:ProtInc. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro. DR InterPro; IPR023485; Ptyr_pPase_SF. DR InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml. DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt. DR PANTHER; PTHR11717:SF7; PTHR11717:SF7; 1. 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; Complete proteome; KW Cytoplasm; Direct protein sequencing; Hydrolase; Phosphoprotein; KW Polymorphism; Protein phosphatase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1939112}. FT CHAIN 2 158 Low molecular weight phosphotyrosine FT protein phosphatase. FT /FTId=PRO_0000046558. FT ACT_SITE 13 13 Nucleophile. {ECO:0000250}. FT ACT_SITE 19 19 {ECO:0000250}. FT ACT_SITE 130 130 Proton donor. {ECO:0000250}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000269|PubMed:1939112}. FT MOD_RES 132 132 Phosphotyrosine. FT {ECO:0000269|PubMed:9038134}. FT MOD_RES 133 133 Phosphotyrosine. FT {ECO:0000269|PubMed:9038134}. FT VAR_SEQ 41 74 RVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHV -> VID FT SGAVSDWNVGRSPDPRAVSCLRNHGIHTAHK (in FT isoform 2). {ECO:0000303|PubMed:1304913, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1587862, FT ECO:0000303|Ref.8}. FT /FTId=VSP_010087. FT VAR_SEQ 41 74 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_010088. FT VAR_SEQ 78 112 ITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKA -> VP FT SLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL (in FT isoform 4). FT {ECO:0000303|PubMed:16344560}. FT /FTId=VSP_054074. FT VAR_SEQ 113 158 Missing (in isoform 4). FT {ECO:0000303|PubMed:16344560}. FT /FTId=VSP_054075. FT VARIANT 7 7 K -> N (in dbSNP:rs11691572). FT /FTId=VAR_050526. FT VARIANT 106 106 Q -> R (in allele ACP1*A; FT dbSNP:rs7576247). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_006171. FT VARIANT 137 137 S -> F (in dbSNP:rs35569198). FT /FTId=VAR_050527. FT MUTAGEN 13 13 C->S: Inactive. FT {ECO:0000269|PubMed:9038134}. FT MUTAGEN 132 132 Y->F: Reduced phosphorylation and FT activity. {ECO:0000269|PubMed:9038134}. FT MUTAGEN 133 133 Y->F: Reduced phosphorylation. No effect FT on activity. FT {ECO:0000269|PubMed:9038134}. FT CONFLICT 2 6 AEQAT -> PRRGR (in Ref. 5; AAB27086). FT {ECO:0000305}. FT CONFLICT 2 2 A -> P (in Ref. 10; BP363227). FT {ECO:0000305}. FT CONFLICT 13 20 CLGNICRS -> PARREAAR (in Ref. 5; FT AAB27085). {ECO:0000305}. FT CONFLICT 32 32 T -> W (in Ref. 1; AA sequence and 2; AA FT sequence). {ECO:0000305}. FT STRAND 7 18 {ECO:0000244|PDB:3N8I}. FT HELIX 19 33 {ECO:0000244|PDB:3N8I}. FT HELIX 37 39 {ECO:0000244|PDB:3N8I}. FT STRAND 40 49 {ECO:0000244|PDB:3N8I}. FT TURN 50 53 {ECO:0000244|PDB:3N8I}. FT HELIX 58 66 {ECO:0000244|PDB:3N8I}. FT HELIX 80 85 {ECO:0000244|PDB:3N8I}. FT STRAND 87 93 {ECO:0000244|PDB:3N8I}. FT HELIX 94 104 {ECO:0000244|PDB:3N8I}. FT STRAND 113 116 {ECO:0000244|PDB:3N8I}. FT HELIX 117 120 {ECO:0000244|PDB:3N8I}. FT HELIX 136 155 {ECO:0000244|PDB:3N8I}. SQ SEQUENCE 158 AA; 18042 MW; 46617BD799313EED CRC64; MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH //