ID   LCMT1_BOVIN             Reviewed;         332 AA.
AC   Q3T0H0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC102399; AAI02400.1; -; mRNA.
DR   RefSeq; NP_001069956.1; NM_001076488.1.
DR   AlphaFoldDB; Q3T0H0; -.
DR   SMR; Q3T0H0; -.
DR   STRING; 9913.ENSBTAP00000037258; -.
DR   PaxDb; Q3T0H0; -.
DR   PRIDE; Q3T0H0; -.
DR   Ensembl; ENSBTAT00000037425; ENSBTAP00000037258; ENSBTAG00000013169.
DR   GeneID; 618021; -.
DR   KEGG; bta:618021; -.
DR   CTD; 51451; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013169; -.
DR   VGNC; VGNC:30812; LCMT1.
DR   eggNOG; KOG2918; Eukaryota.
DR   GeneTree; ENSGT00940000156372; -.
DR   HOGENOM; CLU_031312_0_0_1; -.
DR   InParanoid; Q3T0H0; -.
DR   OMA; IIYEPIR; -.
DR   OrthoDB; 1094856at2759; -.
DR   TreeFam; TF315087; -.
DR   BRENDA; 2.1.1.233; 908.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000013169; Expressed in metanephros cortex and 104 other tissues.
DR   ExpressionAtlas; Q3T0H0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006481; P:C-terminal protein methylation; IBA:GO_Central.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
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_0000226150"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  38009 MW;  011EEDD0274040C3 CRC64;
     MAASLRRPSF TTCSSPTDTD DEGVRGTCED ASICKRFAVS IGYWQDPYIQ HLVRLSKERK
     APEINRGYFA RVHGVSQLTK AFLRKTECNC QILNLGAGMD TTFWMLKDED LLPRKYFEID
     FPMIVTRKLH SIKLKPLLSK PILDLHSEDT LQMDGHMLDS TRYAIIGADL RDIADLEEKL
     KKCNMSTQLP TLLIAECVLV YMTPEQSANL LKWAANSFEA AMFINYEQVN MGDRFGQIMI
     ENLRRRQCDL AGVETCKSLE SQRERLLSSG WESASAIDMM EVYSRLPRAE VIRIEALEFL
     DEMELLEQLM QHYCLCWATK GGSELGLKEI TY