ICMT_XENLA
ID ICMT_XENLA Reviewed; 288 AA.
AC O12947;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
DE EC=2.1.1.100 {ECO:0000305|PubMed:9032282};
DE AltName: Full=Farnesyl cysteine carboxyl methyltransferase;
DE Short=FCMT;
DE AltName: Full=Isoprenylcysteine carboxylmethyltransferase;
DE AltName: Full=Prenylated protein carboxyl methyltransferase;
DE Short=PPMT;
DE AltName: Full=Prenylcysteine carboxyl methyltransferase;
DE Short=pcCMT;
GN Name=icmt;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Ovary;
RX PubMed=9032282; DOI=10.1128/mcb.17.3.1543;
RA Imai Y., Davey J., Kawagishi-Kobayashi M., Yamamoto M.;
RT "Genes encoding farnesyl cysteine carboxyl methyltransferase in
RT Schizosaccharomyces pombe and Xenopus laevis.";
RL Mol. Cell. Biol. 17:1543-1551(1997).
CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated
CC C-terminal cysteine residues. {ECO:0000269|PubMed:9032282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-
CC adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-
CC cysteine methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90510,
CC ChEBI:CHEBI:90511; EC=2.1.1.100;
CC Evidence={ECO:0000305|PubMed:9032282};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60725}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O60725}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. Isoprenylcysteine carboxyl methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00897}.
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DR EMBL; D87750; BAA19000.1; -; mRNA.
DR RefSeq; NP_001081219.1; NM_001087750.1.
DR AlphaFoldDB; O12947; -.
DR SMR; O12947; -.
DR GeneID; 397717; -.
DR KEGG; xla:397717; -.
DR CTD; 397717; -.
DR Xenbase; XB-GENE-6068654; icmt.S.
DR OMA; GMVPQVW; -.
DR OrthoDB; 1479599at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 397717; Expressed in blastula and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR025770; PPMT_MeTrfase.
DR Pfam; PF04140; ICMT; 1.
DR PROSITE; PS51564; SAM_ICMT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Protein-S-isoprenylcysteine O-methyltransferase"
FT /id="PRO_0000209897"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..45
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..158
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 201..204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 214..217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
SQ SEQUENCE 288 AA; 32432 MW; 7F32D5A7BC1B522B CRC64;
MAGARLLQEG RVSIVSFTLG ASVISLPLLT SSFTEQTLLA AAPGRIALVF FIAALNGLLL
LLYKAQLYQV AIRASFLGFA FGCGLLLSIT QSPWKPFGWY VCSLSFFHYS EYLVTAMNNP
RSLSIDSFLL NHSLEYTLAA LSSWVEFTIE TTIYPDLKQI TWLSVIGLIM VLFGEVLRKC
AMLTAGSNFN HIVQNEKSDS HTLVTSGVYS WFRHPSYVGW FYWSIGTQVL LCNPLCLVGY
TLASWRFFSE RIEEEEFSLI HFFGENYLEY KKKVPTGLPF IKGVKMEP
