ICMT_DICDI
ID ICMT_DICDI Reviewed; 237 AA.
AC Q558K8; Q86AM7; Q8T623;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
DE EC=2.1.1.100 {ECO:0000250|UniProtKB:D6WJ77};
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-1; Synonyms=icmA; ORFNames=DDB_G0272799;
GN and
GN Name=icmt-2; Synonyms=icmA; ORFNames=DDB_G0273995;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17699599; DOI=10.1091/mbc.e06-11-1006;
RA Chen Y., McQuade K.J., Guan X.-J., Thomason P.A., Wert M.S., Stock J.B.,
RA Cox E.C.;
RT "Isoprenylcysteine carboxy methylation is essential for development in
RT Dictyostelium discoideum.";
RL Mol. Biol. Cell 18:4106-4118(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Methylates the C-terminal cysteine residues of small GTPases
CC and the heterotrimeric G protein gamma subunit in response to cAMP. The
CC methylation is required for intercellular signaling and regulation of
CC cAMP waves propagation. It also seems to induce the activity of car1, a
CC G protein-coupled receptor which senses extracellular cAMP during the
CC aggregation phase of development. {ECO:0000269|PubMed:17699599}.
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:D6WJ77};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60725}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Induced by starvation and expressed throughout
CC development, with a peak at 8 hours after starvation.
CC {ECO:0000269|PubMed:17699599}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both icmt-1 and icmt-2 do not
CC propagate cAMP waves in a sustained manner and fail to aggregate,
CC affecting differentiation and development.
CC {ECO:0000269|PubMed:17699599}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. Isoprenylcysteine carboxyl methyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AF487784; AAL99548.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70431.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL71037.2; -; Genomic_DNA.
DR RefSeq; XP_644356.1; XM_639264.1.
DR RefSeq; XP_645058.2; XM_639966.2.
DR AlphaFoldDB; Q558K8; -.
DR SMR; Q558K8; -.
DR STRING; 44689.DDB0185114; -.
DR PaxDb; Q558K8; -.
DR EnsemblProtists; EAL70431; EAL70431; DDB_G0273995.
DR EnsemblProtists; EAL71037; EAL71037; DDB_G0272799.
DR GeneID; 8618733; -.
DR GeneID; 8619243; -.
DR KEGG; ddi:DDB_G0272799; -.
DR KEGG; ddi:DDB_G0273995; -.
DR dictyBase; DDB_G0272799; icmA-1.
DR dictyBase; DDB_G0273995; icmA-2.
DR eggNOG; KOG2628; Eukaryota.
DR HOGENOM; CLU_065200_0_2_1; -.
DR InParanoid; Q558K8; -.
DR OMA; SAFHWGE; -.
DR PhylomeDB; Q558K8; -.
DR Reactome; R-DDI-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:Q558K8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0006481; P:C-terminal protein methylation; IDA:dictyBase.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:dictyBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:dictyBase.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:dictyBase.
DR GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:dictyBase.
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..237
FT /note="Protein-S-isoprenylcysteine O-methyltransferase"
FT /id="PRO_0000328175"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 156..159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 169..172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
SQ SEQUENCE 237 AA; 27379 MW; 3F6961685B01C5DE CRC64;
MDQSEIVKLN KIKAKSAWLK KGAARSSAIS CGLGIGIGFG IALFIFSQTL RGFGIYLAGL
CTFHMWEYIW VTMYHPDKLS SKSFLLNHSP QFNMALLISF IEFWIEWYFF PSLKTFSLWW
VGAICMVFGQ IVRSVAMDTA GSNFTHLVQE EKRDDHVLVT NGIYQYMRHP SYFGWFVWSV
STQVILMNPI SIIGFGWASW SFFSQRIENE EDYLIQFFGK SYKDYKKSVW SGIPGIH
