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Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein-leucine O-methyltransferase) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1)

 LCMT1_HUMAN             Reviewed;         334 AA.
Q9UIC8; A6NL89; A8K770; Q53FC5; Q96CI5; Q9H6I9; Q9NTG4; Q9Y378;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
05-DEC-2018, entry version 156.
RecName: Full=Leucine carboxyl methyltransferase 1;
EC=2.1.1.233 {ECO:0000269|PubMed:10600115, ECO:0000269|PubMed:21206058};
AltName: Full=Protein-leucine O-methyltransferase;
AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
Name=LCMT1; Synonyms=LCMT; ORFNames=CGI-68;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10600115; DOI=10.1021/bi991646a;
De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E.,
Merlevede W., Goris J.;
"Purification of porcine brain protein phosphatase 2A leucine carboxyl
methyltransferase and cloning of the human homologue.";
Biochemistry 38:16539-16547(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skeletal muscle, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, 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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-334 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
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).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-334 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE, AND CATALYTIC ACTIVITY.
PubMed=21206058; DOI=10.1107/S0907444910042204;
Tsai M.L., Cronin N., Djordjevic S.;
"The structure of human leucine carboxyl methyltransferase 1 that
regulates protein phosphatase PP2A.";
Acta Crystallogr. D 67:14-24(2011).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) ALONE AND IN COMPLEX WITH
PPP2CA.
PubMed=21292165; DOI=10.1016/j.molcel.2010.12.030;
Stanevich V., Jiang L., Satyshur K.A., Li Y., Jeffrey P.D., Li Z.,
Menden P., Semmelhack M.F., Xing Y.;
"The structural basis for tight control of PP2A methylation and
function by LCMT-1.";
Mol. Cell 41:331-342(2011).
-!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
residue of protein phosphatase 2A catalytic subunits to form
alpha-leucine ester residues. {ECO:0000269|PubMed:10600115}.
-!- CATALYTIC ACTIVITY:
Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-
adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-
leucine methyl ester + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:48544, Rhea:RHEA-COMP:12134, Rhea:RHEA-
COMP:12135, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=2.1.1.233;
Evidence={ECO:0000269|PubMed:10600115,
ECO:0000269|PubMed:21206058};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.1 uM for PP2AD {ECO:0000269|PubMed:10600115};
KM=1.3 uM for AdoMet {ECO:0000269|PubMed:10600115};
-!- INTERACTION:
P51116:FXR2; NbExp=2; IntAct=EBI-747632, EBI-740459;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UIC8-1; Sequence=Displayed;
Name=2;
IsoId=Q9UIC8-2; Sequence=VSP_017428;
Name=3;
IsoId=Q9UIC8-3; Sequence=VSP_041416;
-!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT
family. {ECO:0000305}.
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EMBL; AF037601; AAF18267.1; -; mRNA.
EMBL; AF151826; AAD34063.1; -; mRNA.
EMBL; AK025884; BAB15270.1; -; mRNA.
EMBL; AK223364; BAD97084.1; -; mRNA.
EMBL; AK291885; BAF84574.1; -; mRNA.
EMBL; AK314409; BAG37031.1; -; mRNA.
EMBL; AC008741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001214; AAH01214.1; -; mRNA.
EMBL; BC014217; AAH14217.1; -; mRNA.
EMBL; AL137283; CAB70677.1; -; mRNA.
CCDS; CCDS45445.1; -. [Q9UIC8-1]
CCDS; CCDS45446.1; -. [Q9UIC8-3]
PIR; T46352; T46352.
RefSeq; NP_001027563.1; NM_001032391.1. [Q9UIC8-3]
RefSeq; NP_057393.2; NM_016309.2. [Q9UIC8-1]
RefSeq; XP_011544166.1; XM_011545864.1. [Q9UIC8-2]
UniGene; Hs.337730; -.
PDB; 3IEI; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-334.
PDB; 3O7W; X-ray; 2.00 A; A=23-232, A=259-334.
PDB; 3P71; X-ray; 2.70 A; T=1-334.
PDBsum; 3IEI; -.
PDBsum; 3O7W; -.
PDBsum; 3P71; -.
ProteinModelPortal; Q9UIC8; -.
SMR; Q9UIC8; -.
BioGrid; 119549; 10.
IntAct; Q9UIC8; 4.
MINT; Q9UIC8; -.
STRING; 9606.ENSP00000382021; -.
DrugBank; DB00149; L-Leucine.
iPTMnet; Q9UIC8; -.
PhosphoSitePlus; Q9UIC8; -.
BioMuta; LCMT1; -.
DMDM; 12643251; -.
EPD; Q9UIC8; -.
PaxDb; Q9UIC8; -.
PeptideAtlas; Q9UIC8; -.
PRIDE; Q9UIC8; -.
ProteomicsDB; 84491; -.
ProteomicsDB; 84492; -. [Q9UIC8-2]
ProteomicsDB; 84493; -. [Q9UIC8-3]
DNASU; 51451; -.
Ensembl; ENST00000380966; ENSP00000370353; ENSG00000205629. [Q9UIC8-3]
Ensembl; ENST00000399069; ENSP00000382021; ENSG00000205629. [Q9UIC8-1]
GeneID; 51451; -.
KEGG; hsa:51451; -.
UCSC; uc002dnx.2; human. [Q9UIC8-1]
CTD; 51451; -.
DisGeNET; 51451; -.
EuPathDB; HostDB:ENSG00000205629.11; -.
GeneCards; LCMT1; -.
H-InvDB; HIX0017913; -.
H-InvDB; HIX0022158; -.
HGNC; HGNC:17557; LCMT1.
HPA; HPA041559; -.
HPA; HPA043530; -.
MIM; 610286; gene.
neXtProt; NX_Q9UIC8; -.
OpenTargets; ENSG00000205629; -.
PharmGKB; PA134928443; -.
eggNOG; KOG2918; Eukaryota.
eggNOG; ENOG410YB9K; LUCA.
GeneTree; ENSGT00940000156372; -.
HOVERGEN; HBG052313; -.
InParanoid; Q9UIC8; -.
KO; K18203; -.
OMA; CKRFATS; -.
OrthoDB; EOG091G0CW2; -.
PhylomeDB; Q9UIC8; -.
TreeFam; TF315087; -.
BioCyc; MetaCyc:MONOMER-16510; -.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
SABIO-RK; Q9UIC8; -.
ChiTaRS; LCMT1; human.
EvolutionaryTrace; Q9UIC8; -.
GeneWiki; Leucine_carboxyl_methyltransferase_1; -.
GenomeRNAi; 51451; -.
PRO; PR:Q9UIC8; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205629; Expressed in 225 organ(s), highest expression level in testis.
CleanEx; HS_LCMT1; -.
ExpressionAtlas; Q9UIC8; baseline and differential.
Genevisible; Q9UIC8; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003880; F:protein C-terminal carboxyl O-methyltransferase activity; IDA:MGI.
GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:ProtInc.
GO; GO:0006481; P:C-terminal protein methylation; IDA:MGI.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0031333; P:negative regulation of protein complex assembly; IMP:MGI.
GO; GO:0006479; P:protein methylation; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:MGI.
InterPro; IPR016651; PPM1.
InterPro; IPR040212; PPM1/2.
InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR13600; PTHR13600; 1.
Pfam; PF04072; LCM; 1.
PIRSF; PIRSF016305; LCM_mtfrase; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 334 Leucine carboxyl methyltransferase 1.
/FTId=PRO_0000204422.
REGION 171 172 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
BINDING 37 37 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
BINDING 73 73 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
BINDING 98 98 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
BINDING 122 122 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
BINDING 198 198 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3O7W,
ECO:0000269|PubMed:21206058}.
VAR_SEQ 1 37 MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCK ->
MLPCARELPSAAPDSTLLLTAQHWVANLFILATLIGWTVRS
FFLGRMETCCSHLGLRSGR (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_017428.
VAR_SEQ 136 190 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_041416.
CONFLICT 49 49 P -> S (in Ref. 4; BAD97084).
{ECO:0000305}.
CONFLICT 114 114 L -> P (in Ref. 3; BAB15270).
{ECO:0000305}.
CONFLICT 248 249 RQ -> PS (in Ref. 2; AAD34063).
{ECO:0000305}.
CONFLICT 251 251 D -> E (in Ref. 1; AAF18267).
{ECO:0000305}.
CONFLICT 301 301 F -> L (in Ref. 3; BAB15270).
{ECO:0000305}.
CONFLICT 306 307 EL -> DV (in Ref. 1; AAF18267).
{ECO:0000305}.
CONFLICT 312 313 MR -> NA (in Ref. 1; AAF18267).
{ECO:0000305}.
HELIX 28 43 {ECO:0000244|PDB:3IEI}.
HELIX 51 53 {ECO:0000244|PDB:3IEI}.
HELIX 64 87 {ECO:0000244|PDB:3IEI}.
TURN 88 90 {ECO:0000244|PDB:3IEI}.
STRAND 92 97 {ECO:0000244|PDB:3IEI}.
HELIX 104 110 {ECO:0000244|PDB:3IEI}.
STRAND 116 122 {ECO:0000244|PDB:3IEI}.
HELIX 124 136 {ECO:0000244|PDB:3IEI}.
HELIX 138 147 {ECO:0000244|PDB:3IEI}.
STRAND 148 152 {ECO:0000244|PDB:3IEI}.
STRAND 159 161 {ECO:0000244|PDB:3IEI}.
STRAND 163 169 {ECO:0000244|PDB:3IEI}.
HELIX 175 184 {ECO:0000244|PDB:3IEI}.
STRAND 193 199 {ECO:0000244|PDB:3IEI}.
HELIX 201 203 {ECO:0000244|PDB:3IEI}.
HELIX 206 219 {ECO:0000244|PDB:3IEI}.
STRAND 221 230 {ECO:0000244|PDB:3IEI}.
HELIX 236 246 {ECO:0000244|PDB:3IEI}.
TURN 247 249 {ECO:0000244|PDB:3IEI}.
HELIX 255 259 {ECO:0000244|PDB:3IEI}.
HELIX 261 269 {ECO:0000244|PDB:3IEI}.
TURN 270 272 {ECO:0000244|PDB:3IEI}.
STRAND 274 280 {ECO:0000244|PDB:3IEI}.
HELIX 281 286 {ECO:0000244|PDB:3IEI}.
HELIX 290 299 {ECO:0000244|PDB:3IEI}.
HELIX 305 312 {ECO:0000244|PDB:3IEI}.
STRAND 315 323 {ECO:0000244|PDB:3IEI}.
TURN 325 328 {ECO:0000244|PDB:3IEI}.
HELIX 329 331 {ECO:0000244|PDB:3IEI}.
SEQUENCE 334 AA; 38379 MW; C8D200118E6F353D CRC64;
MATRQRESSI TSCCSTSSCD ADDEGVRGTC EDASLCKRFA VSIGYWHDPY IQHFVRLSKE
RKAPEINRGY FARVHGVSQL IKAFLRKTEC HCQIVNLGAG MDTTFWRLKD EDLLPSKYFE
VDFPMIVTRK LHSIKCKPPL SSPILELHSE DTLQMDGHIL DSKRYAVIGA DLRDLSELEE
KLKKCNMNTQ LPTLLIAECV LVYMTPEQSA NLLKWAANSF ERAMFINYEQ VNMGDRFGQI
MIENLRRRQC DLAGVETCKS LESQKERLLS NGWETASAVD MMELYNRLPR AEVSRIESLE
FLDEMELLEQ LMRHYCLCWA TKGGNELGLK EITY


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