MAM4_SCHPO
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 03-AUG-2022, entry version 137.
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; 4896.SPAC10F6.12c.1; -.
DR MaxQB; P87014; -.
DR PaxDb; P87014; -.
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; SAFHWGE; -.
DR PhylomeDB; P87014; -.
DR Reactome; R-SPO-163841; Gamma carboxylation, hypusine formation 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IMP:PomBase.
DR GO; GO:0006481; P:C-terminal protein methylation; IBA:GO_Central.
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 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 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
