ID ICMT_ORYSJ Reviewed; 191 AA. AC Q7XSR9; A3AX47; Q0JAE6; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 24-JAN-2024, entry version 99. DE RecName: Full=Probable protein-S-isoprenylcysteine O-methyltransferase; DE EC=2.1.1.100; DE AltName: Full=Isoprenylcysteine carboxylmethyltransferase; DE AltName: Full=Prenylated protein carboxyl methyltransferase; DE AltName: Full=Prenylcysteine carboxyl methyltransferase; GN Name=ICMT; OrderedLocusNames=Os04g0602900, LOC_Os04g51380; GN ORFNames=OsJ_015369, OSJNBa0041A02.18; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., RA Li J., Hong G., Xue Y., Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated CC C-terminal cysteine residues. Carboxyl methylation is a reversible and CC potentially regulated step in the post-translational modification of CC prenylated proteins (By similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Divalent metal cations. Probably Zn(2+). {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase CC superfamily. Isoprenylcysteine carboxyl methyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAF15691.1; Type=Erroneous gene model prediction; Evidence={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; AL606638; CAE01825.2; -; Genomic_DNA. DR EMBL; AP008210; BAF15691.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CM000141; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; Q7XSR9; -. DR SMR; Q7XSR9; -. DR STRING; 39947.Q7XSR9; -. DR PaxDb; 39947-Q7XSR9; -. DR HOGENOM; CLU_2744539_0_0_1; -. DR InParanoid; Q7XSR9; -. DR Proteomes; UP000000763; Chromosome 4. DR Proteomes; UP000007752; Chromosome 4. DR Proteomes; UP000059680; Chromosome 4. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.1630; -; 1. DR InterPro; IPR007269; ICMT_MeTrfase. DR InterPro; IPR025770; PPMT_MeTrfase. DR PANTHER; PTHR12714; PROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1. DR PANTHER; PTHR12714:SF9; PROTEIN-S-ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1. DR Pfam; PF04140; ICMT; 1. DR PROSITE; PS51564; SAM_ICMT; 1. DR Genevisible; Q7XSR9; OS. PE 3: Inferred from homology; KW Endoplasmic reticulum; Membrane; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..191 FT /note="Probable protein-S-isoprenylcysteine O- FT methyltransferase" FT /id="PRO_0000356251" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 66..86 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 110..113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q8TMG0" FT BINDING 118 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q8TMG0" FT BINDING 123..126 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q8TMG0" FT BINDING 160 FT /ligand="substrate" 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:Q8TMG0" SQ SEQUENCE 191 AA; 22071 MW; 049589ED58DF63EF CRC64; MAARAQAWLF AAALVIFHGS EYVLAAAFHG RRNVTATSLL ISKQYVLAMS FAMLEHLTEA LLFPELKEYW FVSYVGLVMV IIGEVIRKLA VVTAGRSFTH VIRIHYEDQH KLITHGVYRL MRHPGYSGFL IWAVGTQVML CNPLSTVAFT LVLWRFFSKR IPYEEFFLRQ FFGREYEEYA QKVHSGLPFI E //