ID I3L2Q8_HUMAN Unreviewed; 119 AA. AC I3L2Q8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-OCT-2020, entry version 47. DE RecName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000256|ARBA:ARBA00018956}; DE EC=2.1.1.233 {ECO:0000256|ARBA:ARBA00012834}; DE Flags: Fragment; GN Name=LCMT1 {ECO:0000313|Ensembl:ENSP00000459851}; 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 {ECO:0000313|Ensembl:ENSP00000459851, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000459851, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000213|PubMed:21269460} 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., Burckstummer 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 [3] {ECO:0000313|Ensembl:ENSP00000459851} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine CC residue of protein phosphatase 2A catalytic subunits to form alpha- CC leucine ester residues. {ECO:0000256|ARBA:ARBA00003455}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L- CC methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA- CC COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; CC EC=2.1.1.233; Evidence={ECO:0000256|ARBA:ARBA00000724}; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family. CC {ECO:0000256|ARBA:ARBA00010703}. 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; AC008741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MaxQB; I3L2Q8; -. DR PeptideAtlas; I3L2Q8; -. DR PRIDE; I3L2Q8; -. DR ProteomicsDB; 47014; -. DR Antibodypedia; 26192; 229 antibodies. DR Ensembl; ENST00000570981; ENSP00000459851; ENSG00000205629. DR UCSC; uc059shf.1; human. DR EuPathDB; HostDB:ENSG00000205629.11; -. DR HGNC; HGNC:17557; LCMT1. DR OpenTargets; ENSG00000205629; -. DR GeneTree; ENSGT00940000156372; -. DR HOGENOM; CLU_2066711_0_0_1; -. DR ChiTaRS; LCMT1; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000205629; Expressed in testis and 237 other tissues. DR ExpressionAtlas; I3L2Q8; baseline and differential. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR InterPro; IPR016651; PPM1. DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR13600; PTHR13600; 1. DR Pfam; PF04072; LCM; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0000213|EPD:I3L2Q8, KW ECO:0000213|MaxQB:I3L2Q8, ECO:0000213|PeptideAtlas:I3L2Q8, KW ECO:0000213|ProteomicsDB:I3L2Q8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000459851" SQ SEQUENCE 119 AA; 13740 MW; AC002C4D181F7599 CRC64; SSCDADDEGV RGTCEDASLC KRFAVSIGYW HDPYIQHFVR LSKERKAPEI NRGYFARVHG VSQLIKAFLR KTECHCQIVN LGAGMDTTFW RLKDEDLLPS KYFEVDFPMI VTRKLHSIK //