ID I3L2Q8_HUMAN Unreviewed; 119 AA. AC I3L2Q8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 22-FEB-2023, entry version 57. DE RecName: Full=[phosphatase 2A protein]-leucine-carboxy methyltransferase {ECO:0000256|ARBA:ARBA00012834}; DE EC=2.1.1.233 {ECO:0000256|ARBA:ARBA00012834}; DE AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000256|ARBA:ARBA00032526}; DE Flags: Fragment; GN Name=LCMT1 {ECO:0000313|Ensembl:ENSP00000459851.1}; 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:ENSP00000459851.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000459851.1, 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:0007829|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:ENSP00000459851.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2022) 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 AlphaFoldDB; I3L2Q8; -. DR SMR; I3L2Q8; -. DR MaxQB; I3L2Q8; -. DR PeptideAtlas; I3L2Q8; -. DR ProteomicsDB; 47014; -. DR Antibodypedia; 26192; 263 antibodies from 21 providers. DR Ensembl; ENST00000570981.1; ENSP00000459851.1; ENSG00000205629.12. DR UCSC; uc059shf.1; human. DR HGNC; HGNC:17557; LCMT1. DR VEuPathDB; HostDB:ENSG00000205629; -. DR GeneTree; ENSGT00940000156372; -. DR HOGENOM; CLU_2066711_0_0_1; -. DR OMA; IIYEPIR; -. DR ChiTaRS; LCMT1; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000205629; Expressed in middle temporal gyrus and 202 other tissues. DR ExpressionAtlas; I3L2Q8; baseline and differential. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:InterPro. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR016651; PPM1. DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR13600; LEUCINE CARBOXYL METHYLTRANSFERASE; 1. DR PANTHER; PTHR13600:SF33; LEUCINE CARBOXYL METHYLTRANSFERASE 1; 1. DR Pfam; PF04072; LCM; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:I3L2Q8, KW ECO:0007829|MaxQB:I3L2Q8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000459851.1" SQ SEQUENCE 119 AA; 13740 MW; AC002C4D181F7599 CRC64; SSCDADDEGV RGTCEDASLC KRFAVSIGYW HDPYIQHFVR LSKERKAPEI NRGYFARVHG VSQLIKAFLR KTECHCQIVN LGAGMDTTFW RLKDEDLLPS KYFEVDFPMI VTRKLHSIK //