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Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Adipocyte acid phosphatase) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) (Red cell acid phosphatase 1)

 PPAC_HUMAN              Reviewed;         158 AA.
P24666; A8K1L9; B5MCC7; P24667; Q16035; Q16036; Q16725; Q3KQX8;
Q53RU0;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 192.
RecName: Full=Low molecular weight phosphotyrosine protein phosphatase;
Short=LMW-PTP;
Short=LMW-PTPase;
EC=3.1.3.48;
AltName: Full=Adipocyte acid phosphatase;
AltName: Full=Low molecular weight cytosolic acid phosphatase;
EC=3.1.3.2;
AltName: Full=Red cell acid phosphatase 1;
Name=ACP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE (ALLELE B; ISOFORMS 1 AND 2), CLEAVAGE OF INITIATOR
METHIONINE, AND ACETYLATION AT ALA-2.
PubMed=1939112;
Dissing J., Johnsen A.H., Sensabaugh G.F.;
"Human red cell acid phosphatase (ACP1). The amino acid sequence of
the two isozymes Bf and Bs encoded by the ACP1*B allele.";
J. Biol. Chem. 266:20619-20625(1991).
[2]
PROTEIN SEQUENCE (ALLELES A AND C; ISOFORMS 1 AND 2).
PubMed=1627603; DOI=10.1016/0167-4838(92)90155-7;
Dissing J., Johnsen A.H.;
"Human red cell acid phosphatase (ACP1): the primary structure of the
two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles.";
Biochim. Biophys. Acta 1121:261-268(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=1587862;
Wo Y.-Y.P., McCormack A.L., Shabonowitz J., Hunt D.F., Davis J.P.,
Mitchell G.L., van Etten R.L.;
"Sequencing, cloning, and expression of human red cell-type acid
phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.";
J. Biol. Chem. 267:10856-10865(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8586411; DOI=10.1006/geno.1995.9893;
Bryson G.L.M., Massa H., Trask B.J., van Etten R.L.;
"Gene structure, sequence, and chromosomal localization of the human
red cell-type low-molecular-weight acid phosphotyrosyl phosphatase
gene, ACP1.";
Genomics 30:133-140(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adipocyte;
PubMed=1304913; DOI=10.1002/pro.5560010603;
Shekels L.L., Smith A.J., van Etten R.L., Bernlohr D.A.;
"Identification of the adipocyte acid phosphatase as a PAO-sensitive
tyrosyl phosphatase.";
Protein Sci. 1:710-721(1992).
[6]
NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION
AT TYR-132 AND TYR-133, AND MUTAGENESIS OF CYS-13; TYR-132 AND
TYR-133.
PubMed=9038134; DOI=10.1074/jbc.272.9.5371;
Tailor P., Gilman J., Williams S., Couture C., Mustelin T.;
"Regulation of the low molecular weight phosphotyrosine phosphatase by
phosphorylation at tyrosines 131 and 132.";
J. Biol. Chem. 272:5371-5374(1997).
[7]
NUCLEOTIDE SEQUENCE (ISOFORM 3).
PubMed=10336608; DOI=10.1046/j.1432-1327.1999.00353.x;
Tailor P., Gilman J., Williams S., Mustelin T.;
"A novel isoform of the low molecular weight phosphotyrosine
phosphatase, LMPTP-C, arising from alternative mRNA splicing.";
Eur. J. Biochem. 262:277-282(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hippocampus, and Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=16344560; DOI=10.1101/gr.4039406;
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
"Diversification of transcriptional modulation: large-scale
identification and characterization of putative alternative promoters
of human genes.";
Genome Res. 16:55-65(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ARG-106.
TISSUE=Muscle, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PROTEIN SEQUENCE OF 42-59, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-158 (ISOFORMS 1/2).
TISSUE=Blood;
PubMed=8364553; DOI=10.1093/hmg/2.7.1079-a;
Sensabaugh G.F., Lazaruk K.A.;
"A TaqI site identifies the *A allele at the ACP1 locus.";
Hum. Mol. Genet. 2:1079-1079(1993).
[16]
INTERACTION WITH EPHB1.
PubMed=9499402; DOI=10.1101/gad.12.5.667;
Stein E., Lane A.A., Cerretti D.P., Schoecklmann H.O., Schroff A.D.,
Van Etten R.L., Daniel T.O.;
"Eph receptors discriminate specific ligand oligomers to determine
alternative signaling complexes, attachment, and assembly responses.";
Genes Dev. 12:667-678(1998).
[17]
INTERACTION WITH EPHA2.
PubMed=12167657; DOI=10.1074/jbc.M207127200;
Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.;
"Regulation of the EphA2 kinase by the low molecular weight tyrosine
phosphatase induces transformation.";
J. Biol. Chem. 277:39274-39279(2002).
[18]
INTERACTION WITH SPTAN1.
PubMed=11971983; DOI=10.1128/MCB.22.10.3527-3536.2002;
Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O.,
Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B.,
Lecomte M.-C.;
"Tyrosine phosphorylation regulates alpha II spectrin cleavage by
calpain.";
Mol. Cell. Biol. 22:3527-3536(2002).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=9705307; DOI=10.1074/jbc.273.34.21714;
Zhang M., Stauffacher C.V., Lin D., van Etten R.L.;
"Crystal structure of a human low molecular weight phosphotyrosyl
phosphatase. Implications for substrate specificity.";
J. Biol. Chem. 273:21714-21720(1998).
-!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
phosphates and natural and synthetic acyl phosphates. Isoform 3
does not possess phosphatase activity.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate.
-!- ENZYME REGULATION: Inhibited by sulfhydryl reagents.
-!- SUBUNIT: Isoform 1 interacts with the SH3 domain of SPTAN1. There
is no interaction observed for isoforms 2 or 3. Interacts with
EPHA2; dephosphorylates EPHA2. Interacts with EPHB1.
{ECO:0000269|PubMed:11971983, ECO:0000269|PubMed:12167657,
ECO:0000269|PubMed:9499402}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=The ratio of isoform 1 to isoform 2 is 2:1 in allele A,
4:1 in allele B and 1:4 in allele C.;
Name=1; Synonyms=F, A, Alpha, LMPTP-A, HCPTP-A;
IsoId=P24666-1; Sequence=Displayed;
Name=2; Synonyms=S, B, Beta, LMPTP-B, HCPTP-B;
IsoId=P24666-2, P24667-1;
Sequence=VSP_010087;
Name=3; Synonyms=C, LMPTP-C;
IsoId=P24666-3; Sequence=VSP_010088;
Name=4;
IsoId=P24666-4; Sequence=VSP_054074, VSP_054075;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: T-lymphocytes express only isoform 2.
{ECO:0000269|PubMed:9038134}.
-!- POLYMORPHISM: ACP1 is genetically polymorphic. Three common
alleles are known in Caucasians: ACP1*A, ACP1*B and ACP1*C. They
give rise to six different phenotypes. Each allele appears to
encode two electrophoretically different isozymes, F and S, which
are produced in allele-specific ratios (PubMed:1939112). The
sequence shown is that of allele ACP1*B and allele ACP1*C.
{ECO:0000269|PubMed:1939112}.
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. {ECO:0000305}.
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EMBL; M83653; AAB59354.1; -; mRNA.
EMBL; M83654; AAB59355.1; -; mRNA.
EMBL; U25849; AAC52067.1; -; Genomic_DNA.
EMBL; U25847; AAC52067.1; JOINED; Genomic_DNA.
EMBL; U25848; AAC52067.1; JOINED; Genomic_DNA.
EMBL; S62884; AAB27085.1; -; mRNA.
EMBL; S62885; AAB27086.1; -; mRNA.
EMBL; M87545; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BT007136; AAP35800.1; -; mRNA.
EMBL; AK289934; BAF82623.1; -; mRNA.
EMBL; AK291861; BAF84550.1; -; mRNA.
EMBL; BP363227; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC079779; AAY14958.1; -; Genomic_DNA.
EMBL; CH471053; EAX01112.1; -; Genomic_DNA.
EMBL; CH471053; EAX01116.1; -; Genomic_DNA.
EMBL; BC007422; AAH07422.1; -; mRNA.
EMBL; BC106011; AAI06012.1; -; mRNA.
EMBL; L06508; AAB59628.1; -; Genomic_DNA.
CCDS; CCDS1639.1; -. [P24666-1]
CCDS; CCDS1640.1; -. [P24666-2]
CCDS; CCDS46217.1; -. [P24666-4]
PIR; A38148; A38148.
PIR; B38148; B38148.
RefSeq; NP_004291.1; NM_004300.3. [P24666-1]
RefSeq; NP_009030.1; NM_007099.3. [P24666-2]
UniGene; Hs.558296; -.
PDB; 1XWW; X-ray; 1.63 A; A=2-158.
PDB; 3N8I; X-ray; 1.50 A; A=2-158.
PDB; 4Z99; X-ray; 2.30 A; A=1-158.
PDB; 4Z9A; X-ray; 2.10 A; A=1-158.
PDB; 4Z9B; X-ray; 2.41 A; A=1-158.
PDB; 5JNR; X-ray; 2.00 A; A=1-158.
PDB; 5JNS; X-ray; 1.80 A; A=1-158.
PDB; 5JNT; X-ray; 1.45 A; A=1-158.
PDB; 5KQG; X-ray; 1.50 A; A=1-158.
PDB; 5KQL; X-ray; 1.45 A; A=1-158.
PDB; 5KQM; X-ray; 1.91 A; A=1-158.
PDB; 5KQP; X-ray; 2.05 A; A=1-158.
PDB; 5PNT; X-ray; 2.20 A; A=2-158.
PDBsum; 1XWW; -.
PDBsum; 3N8I; -.
PDBsum; 4Z99; -.
PDBsum; 4Z9A; -.
PDBsum; 4Z9B; -.
PDBsum; 5JNR; -.
PDBsum; 5JNS; -.
PDBsum; 5JNT; -.
PDBsum; 5KQG; -.
PDBsum; 5KQL; -.
PDBsum; 5KQM; -.
PDBsum; 5KQP; -.
PDBsum; 5PNT; -.
ProteinModelPortal; P24666; -.
SMR; P24666; -.
BioGrid; 106568; 39.
IntAct; P24666; 16.
STRING; 9606.ENSP00000272065; -.
BindingDB; P24666; -.
ChEMBL; CHEMBL4903; -.
DrugBank; DB04214; 4-Nitrophenyl Phosphate.
DrugBank; DB00173; Adenine.
DEPOD; P24666; -.
iPTMnet; P24666; -.
PhosphoSitePlus; P24666; -.
SwissPalm; P24666; -.
BioMuta; ACP1; -.
DMDM; 1709543; -.
REPRODUCTION-2DPAGE; IPI00218847; -.
REPRODUCTION-2DPAGE; IPI00219861; -.
EPD; P24666; -.
MaxQB; P24666; -.
PaxDb; P24666; -.
PeptideAtlas; P24666; -.
PRIDE; P24666; -.
DNASU; 52; -.
Ensembl; ENST00000272065; ENSP00000272065; ENSG00000143727. [P24666-1]
Ensembl; ENST00000272067; ENSP00000272067; ENSG00000143727. [P24666-2]
Ensembl; ENST00000407983; ENSP00000385404; ENSG00000143727. [P24666-4]
GeneID; 52; -.
KEGG; hsa:52; -.
UCSC; uc002qwd.3; human. [P24666-1]
CTD; 52; -.
DisGeNET; 52; -.
EuPathDB; HostDB:ENSG00000143727.15; -.
GeneCards; ACP1; -.
HGNC; HGNC:122; ACP1.
HPA; HPA016754; -.
MIM; 171500; gene.
neXtProt; NX_P24666; -.
OpenTargets; ENSG00000143727; -.
PharmGKB; PA24446; -.
eggNOG; KOG3217; Eukaryota.
eggNOG; COG0394; LUCA.
GeneTree; ENSGT00500000044891; -.
HOGENOM; HOG000074091; -.
HOVERGEN; HBG007540; -.
InParanoid; P24666; -.
KO; K14394; -.
OMA; AGTGSWH; -.
OrthoDB; EOG091G0P0O; -.
PhylomeDB; P24666; -.
TreeFam; TF353727; -.
BRENDA; 3.1.3.48; 2681.
SignaLink; P24666; -.
SIGNOR; P24666; -.
EvolutionaryTrace; P24666; -.
GeneWiki; ACP1; -.
GenomeRNAi; 52; -.
PRO; PR:P24666; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143727; -.
CleanEx; HS_ACP1; -.
ExpressionAtlas; P24666; baseline and differential.
Genevisible; P24666; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0003993; F:acid phosphatase activity; TAS:ProtInc.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
InterPro; IPR023485; Ptyr_pPase_SF.
InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
Pfam; PF01451; LMWPc; 1.
PRINTS; PR00719; LMWPTPASE.
PRINTS; PR00720; MAMMALPTPASE.
SMART; SM00226; LMWPc; 1.
SUPFAM; SSF52788; SSF52788; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Hydrolase; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1939112}.
CHAIN 2 158 Low molecular weight phosphotyrosine
protein phosphatase.
/FTId=PRO_0000046558.
ACT_SITE 13 13 Nucleophile. {ECO:0000250}.
ACT_SITE 19 19 {ECO:0000250}.
ACT_SITE 130 130 Proton donor. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:1939112}.
MOD_RES 132 132 Phosphotyrosine.
{ECO:0000269|PubMed:9038134}.
MOD_RES 133 133 Phosphotyrosine.
{ECO:0000269|PubMed:9038134}.
VAR_SEQ 41 74 RVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHV -> VID
SGAVSDWNVGRSPDPRAVSCLRNHGIHTAHK (in
isoform 2). {ECO:0000303|PubMed:1304913,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1587862,
ECO:0000303|Ref.8}.
/FTId=VSP_010087.
VAR_SEQ 41 74 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_010088.
VAR_SEQ 78 112 ITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKA -> VP
SLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL (in
isoform 4).
{ECO:0000303|PubMed:16344560}.
/FTId=VSP_054074.
VAR_SEQ 113 158 Missing (in isoform 4).
{ECO:0000303|PubMed:16344560}.
/FTId=VSP_054075.
VARIANT 7 7 K -> N (in dbSNP:rs11691572).
/FTId=VAR_050526.
VARIANT 106 106 Q -> R (in allele ACP1*A;
dbSNP:rs79716074).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_006171.
VARIANT 137 137 S -> F (in dbSNP:rs35569198).
/FTId=VAR_050527.
MUTAGEN 13 13 C->S: Inactive.
{ECO:0000269|PubMed:9038134}.
MUTAGEN 132 132 Y->F: Reduced phosphorylation and
activity. {ECO:0000269|PubMed:9038134}.
MUTAGEN 133 133 Y->F: Reduced phosphorylation. No effect
on activity.
{ECO:0000269|PubMed:9038134}.
CONFLICT 2 6 AEQAT -> PRRGR (in Ref. 5; AAB27086).
{ECO:0000305}.
CONFLICT 2 2 A -> P (in Ref. 10; BP363227).
{ECO:0000305}.
CONFLICT 13 20 CLGNICRS -> PARREAAR (in Ref. 5;
AAB27085). {ECO:0000305}.
CONFLICT 32 32 T -> W (in Ref. 1; AA sequence and 2; AA
sequence). {ECO:0000305}.
STRAND 7 18 {ECO:0000244|PDB:5KQL}.
HELIX 19 33 {ECO:0000244|PDB:5KQL}.
HELIX 37 39 {ECO:0000244|PDB:5KQL}.
STRAND 40 49 {ECO:0000244|PDB:5KQL}.
TURN 50 53 {ECO:0000244|PDB:5KQL}.
HELIX 58 66 {ECO:0000244|PDB:5KQL}.
HELIX 80 85 {ECO:0000244|PDB:5KQL}.
STRAND 87 93 {ECO:0000244|PDB:5KQL}.
HELIX 94 104 {ECO:0000244|PDB:5KQL}.
STRAND 113 116 {ECO:0000244|PDB:5KQL}.
HELIX 117 120 {ECO:0000244|PDB:5KQL}.
HELIX 136 155 {ECO:0000244|PDB:5KQL}.
SEQUENCE 158 AA; 18042 MW; 46617BD799313EED CRC64;
MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG
QSCMKRHGIP MSHVARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY
DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH


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