ID   MAM4_SCHPO              Reviewed;         236 AA.
AC   P87014;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
DE            EC=2.1.1.100 {ECO:0000269|PubMed:9032282};
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=mam4; ORFNames=SPAC10F6.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Mediates C-terminal methylation of the isoprenylated C-
CC       terminal cysteine in M-factor. {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:0000269|PubMed:9032282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21673;
CC         Evidence={ECO:0000269|PubMed:9032282};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9032282}; Multi-pass
CC       membrane protein {ECO:0000255}.
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; D87749; BAA18999.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA15725.1; -; Genomic_DNA.
DR   PIR; T43237; T43237.
DR   RefSeq; NP_593263.1; NM_001018660.2.
DR   AlphaFoldDB; P87014; -.
DR   SMR; P87014; -.
DR   BioGRID; 279420; 5.
DR   STRING; 284812.P87014; -.
DR   MaxQB; P87014; -.
DR   PaxDb; 4896-SPAC10F6-12c-1; -.
DR   EnsemblFungi; SPAC10F6.12c.1; SPAC10F6.12c.1:pep; SPAC10F6.12c.
DR   GeneID; 2542982; -.
DR   KEGG; spo:SPAC10F6.12c; -.
DR   PomBase; SPAC10F6.12c; mam4.
DR   VEuPathDB; FungiDB:SPAC10F6.12c; -.
DR   eggNOG; KOG2628; Eukaryota.
DR   HOGENOM; CLU_065200_0_2_1; -.
DR   InParanoid; P87014; -.
DR   OMA; FSHHIVD; -.
DR   PhylomeDB; P87014; -.
DR   Reactome; R-SPO-163841; Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation.
DR   PRO; PR:P87014; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IMP:PomBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0019236; P:response to pheromone; 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.
PE   1: Evidence at protein level;
KW   Membrane; Methyltransferase; Pheromone response; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..236
FT                   /note="Protein-S-isoprenylcysteine O-methyltransferase"
FT                   /id="PRO_0000209898"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         155..158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT   BINDING         168..171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT   BINDING         205
FT                   /ligand="substrate"
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:Q8TMG0"
SQ   SEQUENCE   236 AA;  26505 MW;  BE22A8C80BAA16FD CRC64;
     MGNLHTSIAV ASICLTSAFL GCVFGLGFFV WIIYGYSIGG FFAFLSLFHL LEFYITARFQ
     GSQLSWDSFI LNNGKAYWLA MLVGLLECLL SGGKSFAKVI NCLRFPSFLI NFIFSVYQTS
     ALGFLCLGQY LRSSAMVQAG QSFSHIVASK RNKDHLLVTD GIYAYVRHPS YVGFFIWALG
     TQMLLGNFVS TLLFSLVLWK FFSQRITTEE AYLVSFFGDS YEQYRKKVPS GIPLIP
//