ICMT_RAT
ID ICMT_RAT Reviewed; 284 AA.
AC Q9WVM4; G3V7G5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
DE EC=2.1.1.100 {ECO:0000250|UniProtKB:O60725};
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 {ECO:0000312|RGD:621618};
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] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL81231.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAD42926.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-284.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RA Otaki J.M., Firestein S.;
RT "Molecular cloning of farnesyl cysteine carboxyl methyltransferase gene
RT from rat olfactory bulb.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated
CC C-terminal cysteine residues. {ECO:0000250|UniProtKB:O60725}.
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:0000250|UniProtKB:O60725};
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:0000305}.
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DR EMBL; AC135674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473968; EDL81231.1; -; Genomic_DNA.
DR EMBL; AF075595; AAD42926.1; -; mRNA.
DR RefSeq; NP_579844.2; NM_133310.2.
DR AlphaFoldDB; Q9WVM4; -.
DR SMR; Q9WVM4; -.
DR STRING; 10116.ENSRNOP00000014625; -.
DR BindingDB; Q9WVM4; -.
DR ChEMBL; CHEMBL2298; -.
DR PhosphoSitePlus; Q9WVM4; -.
DR PaxDb; Q9WVM4; -.
DR PRIDE; Q9WVM4; -.
DR Ensembl; ENSRNOT00000014625; ENSRNOP00000014625; ENSRNOG00000010953.
DR GeneID; 170818; -.
DR KEGG; rno:170818; -.
DR UCSC; RGD:621618; rat.
DR CTD; 23463; -.
DR RGD; 621618; Icmt.
DR eggNOG; KOG2628; Eukaryota.
DR GeneTree; ENSGT00390000017394; -.
DR HOGENOM; CLU_065200_0_1_1; -.
DR InParanoid; Q9WVM4; -.
DR OMA; GMVPQVW; -.
DR OrthoDB; 1479599at2759; -.
DR PhylomeDB; Q9WVM4; -.
DR TreeFam; TF313769; -.
DR Reactome; R-RNO-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR Reactome; R-RNO-9648002; RAS processing.
DR SABIO-RK; Q9WVM4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000010953; Expressed in testis and 18 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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:0016020; C:membrane; IDA:RGD.
DR GO; GO:0008140; F:cAMP response element binding protein binding; ISO:RGD.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IMP:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0006481; P:C-terminal protein methylation; IMP:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0006479; P:protein methylation; ISO:RGD.
DR GO; GO:2000772; P:regulation of cellular senescence; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IMP:RGD.
DR GO; GO:0046499; P:S-adenosylmethioninamine metabolic process; IMP:RGD.
DR GO; GO:0031929; P:TOR signaling; ISO:RGD.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR025770; PPMT_MeTrfase.
DR Pfam; PF04140; ICMT; 1.
DR PROSITE; PS51564; SAM_ICMT; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..284
FT /note="Protein-S-isoprenylcysteine O-methyltransferase"
FT /id="PRO_0000209896"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..41
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..92
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..154
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 197..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 210..213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
SQ SEQUENCE 284 AA; 31812 MW; DCAB6EA1D6EE0827 CRC64;
MAGCAARVPP GSEARLSLAT FLLGASVLAL PLLTRAGLQG RTGLALYVAG LNALLLLLYR
PPRYQIAIRA CFLGFVFGCG VLLSFSQSSW NHFGWYVCSL SLFHYSEYLV TAVNNPKSLS
LDSFLLNHSL EYTVAALSSW IEFTLENIFW PELKQITWLS AAGLLMVIFG ECLRKVAMFT
AGSNFNHVVQ SEKSDTHTLV TSGVYAWCRH PSYVGWFYWS IGTQVMLCNP ICGVVYALTV
WRFFRDRTEE EEISLIHFFG EEYLDYKKRV PTGLPFIKGV KVGL
