ID   LCMT1_RAT               Reviewed;         332 AA.
AC   Q6P4Z6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Leucine carboxyl methyltransferase 1;
DE            EC=2.1.1.233;
DE   AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
GN   Name=Lcmt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000305}.
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DR   EMBL; BC063186; AAH63186.1; -; mRNA.
DR   RefSeq; NP_955437.1; NM_199405.2.
DR   AlphaFoldDB; Q6P4Z6; -.
DR   SMR; Q6P4Z6; -.
DR   STRING; 10116.ENSRNOP00000019640; -.
DR   PhosphoSitePlus; Q6P4Z6; -.
DR   jPOST; Q6P4Z6; -.
DR   PaxDb; Q6P4Z6; -.
DR   GeneID; 361643; -.
DR   KEGG; rno:361643; -.
DR   UCSC; RGD:735118; rat.
DR   CTD; 51451; -.
DR   RGD; 735118; Lcmt1.
DR   eggNOG; KOG2918; Eukaryota.
DR   InParanoid; Q6P4Z6; -.
DR   OrthoDB; 1094856at2759; -.
DR   PhylomeDB; Q6P4Z6; -.
DR   BRENDA; 2.1.1.233; 5301.
DR   Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   PRO; PR:Q6P4Z6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0003880; F:protein C-terminal carboxyl O-methyltransferase activity; ISO:RGD.
DR   GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008276; F:protein methyltransferase activity; ISO:RGD.
DR   GO; GO:0006481; P:C-terminal protein methylation; ISO:RGD.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR   GO; GO:0006479; P:protein methylation; ISO:RGD.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR   GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISO:RGD.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016651; PPM1.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13600; PTHR13600; 1.
DR   Pfam; PF04072; LCM; 1.
DR   PIRSF; PIRSF016305; LCM_mtfrase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..332
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226151"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  38330 MW;  1190662A8B869337 CRC64;
     MATGSRESSF SSCASSCDFD DEGVRGTCED ASLCKRFAVS IGHWHDPYIE HLVRQSKERK
     APEINRGYFA RVHGVSQLIK AFLRKTECRC QILNLGAGMD TTFWKLKDEG LLPNKYFEVD
     FPMIVTRKLH TIKNKPLLFR PIMELHPEDT LQIDSHMLDS KRYAIIGADL RDLSELEEKL
     KKCNMNTQLP TLLITECVLV YMTPEQSANL LKWAARSFET AMFINYEQVN MDDRFGQIMI
     ENLRRRQCDL AGVETCKSLE SQKERLLLNG WETASAVNMM ELYSGLPRAE VNRIESLEFL
     DEMELLEQLM RHYCLCWATR GGQELGLKEI TY