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Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase) (Prenylated protein carboxyl methyltransferase) (PPMT) (Prenylcysteine carboxyl methyltransferase) (pcCMT)

 ICMT_HUMAN              Reviewed;         284 AA.
O60725; Q6FHT0;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
EC=2.1.1.100;
AltName: Full=Isoprenylcysteine carboxylmethyltransferase;
AltName: Full=Prenylated protein carboxyl methyltransferase;
Short=PPMT;
AltName: Full=Prenylcysteine carboxyl methyltransferase;
Short=pcCMT;
Name=ICMT; Synonyms=PCCMT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Myeloid;
PubMed=9614111; DOI=10.1074/jbc.273.24.15030;
Dai Q., Choy E., Chiu V., Romano J., Slivka S.R., Steitz S.A.,
Michaelis S., Philips M.R.;
"Mammalian prenylcysteine carboxyl methyltransferase is in the
endoplasmic reticulum.";
J. Biol. Chem. 273:15030-15034(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=10649571; DOI=10.1038/72101;
Lin X., Antalffy B., Kang D., Orr H.T., Zoghbi H.Y.;
"Polyglutamine expansion down-regulates specific neuronal genes before
pathologic changes in SCA1.";
Nat. Neurosci. 3:157-163(2000).
[7]
SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
PubMed=19158273; DOI=10.1128/MCB.01719-08;
Wright L.P., Court H., Mor A., Ahearn I.M., Casey P.J., Philips M.R.;
"Topology of mammalian isoprenylcysteine carboxyl methyltransferase
determined in live cells with a fluorescent probe.";
Mol. Cell. Biol. 29:1826-1833(2009).
-!- FUNCTION: Catalyzes the post-translational methylation of
isoprenylated C-terminal cysteine residues.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein C-terminal
S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-
terminal S-farnesyl-L-cysteine methyl ester. {ECO:0000255|PROSITE-
ProRule:PRU00897}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Divalent metal cations. Probably Zn(2+). {ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:19158273}; Multi-pass membrane protein
{ECO:0000269|PubMed:19158273}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher
levels in the cerebellum and putamen than in other brain regions.
Abundant expression seen in the Purkinje cells and pontine
neurons. {ECO:0000269|PubMed:10649571}.
-!- SIMILARITY: Belongs to the class VI-like SAM-binding
methyltransferase superfamily. Isoprenylcysteine carboxyl
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00897}.
-----------------------------------------------------------------------
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EMBL; AF064084; AAC16554.1; -; mRNA.
EMBL; CR541671; CAG46472.1; -; mRNA.
EMBL; CR541711; CAG46512.1; -; mRNA.
EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471130; EAW71522.1; -; Genomic_DNA.
EMBL; BC028168; AAH28168.1; -; mRNA.
CCDS; CCDS61.1; -.
RefSeq; NP_036537.1; NM_012405.3.
UniGene; Hs.515688; -.
ProteinModelPortal; O60725; -.
SMR; O60725; -.
BioGrid; 117026; 15.
IntAct; O60725; 13.
MINT; O60725; -.
STRING; 9606.ENSP00000343552; -.
BindingDB; O60725; -.
ChEMBL; CHEMBL4699; -.
iPTMnet; O60725; -.
PhosphoSitePlus; O60725; -.
BioMuta; ICMT; -.
EPD; O60725; -.
PaxDb; O60725; -.
PeptideAtlas; O60725; -.
PRIDE; O60725; -.
ProteomicsDB; 49571; -.
DNASU; 23463; -.
Ensembl; ENST00000343813; ENSP00000343552; ENSG00000116237.
GeneID; 23463; -.
KEGG; hsa:23463; -.
UCSC; uc001amk.4; human.
CTD; 23463; -.
DisGeNET; 23463; -.
EuPathDB; HostDB:ENSG00000116237.15; -.
GeneCards; ICMT; -.
HGNC; HGNC:5350; ICMT.
HPA; HPA032024; -.
HPA; HPA032025; -.
MIM; 605851; gene.
neXtProt; NX_O60725; -.
OpenTargets; ENSG00000116237; -.
PharmGKB; PA29598; -.
eggNOG; KOG2628; Eukaryota.
eggNOG; COG2020; LUCA.
GeneTree; ENSGT00390000017394; -.
HOGENOM; HOG000213961; -.
HOVERGEN; HBG019034; -.
InParanoid; O60725; -.
KO; K00587; -.
OMA; FHFLEFW; -.
OrthoDB; EOG091G0HSB; -.
PhylomeDB; O60725; -.
TreeFam; TF313769; -.
Reactome; R-HSA-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
SABIO-RK; O60725; -.
GeneWiki; ICMT; -.
GenomeRNAi; 23463; -.
PRO; PR:O60725; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116237; Expressed in 235 organ(s), highest expression level in adrenal tissue.
CleanEx; HS_ICMT; -.
ExpressionAtlas; O60725; baseline and differential.
Genevisible; O60725; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0003880; F:protein C-terminal carboxyl O-methyltransferase activity; TAS:ProtInc.
GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; TAS:Reactome.
GO; GO:0006481; P:C-terminal protein methylation; TAS:ProtInc.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006612; P:protein targeting to membrane; TAS:ProtInc.
InterPro; IPR007269; ICMT_MeTrfase.
InterPro; IPR025770; PPMT_MeTrfase.
Pfam; PF04140; ICMT; 1.
PROSITE; PS51564; SAM_ICMT; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Membrane; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 284 Protein-S-isoprenylcysteine O-
methyltransferase.
/FTId=PRO_0000209894.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 33 Helical. {ECO:0000255}.
TOPO_DOM 34 41 Lumenal. {ECO:0000255}.
TRANSMEM 42 59 Helical. {ECO:0000255}.
TOPO_DOM 60 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 87 Helical. {ECO:0000255}.
TOPO_DOM 88 92 Lumenal. {ECO:0000255}.
TRANSMEM 93 112 Helical. {ECO:0000255}.
TOPO_DOM 113 131 Cytoplasmic. {ECO:0000255}.
TRANSMEM 132 149 Helical. {ECO:0000255}.
TOPO_DOM 150 154 Lumenal. {ECO:0000255}.
TRANSMEM 155 174 Helical. {ECO:0000255}.
TOPO_DOM 175 212 Cytoplasmic. {ECO:0000255}.
TRANSMEM 213 228 Helical. {ECO:0000255}.
TOPO_DOM 229 229 Lumenal. {ECO:0000255}.
TRANSMEM 230 244 Helical. {ECO:0000255}.
TOPO_DOM 245 284 Cytoplasmic. {ECO:0000255}.
SEQUENCE 284 AA; 31938 MW; C86741B13ACA611C CRC64;
MAGCAARAPP GSEARLSLAT FLLGASVLAL PLLTRAGLQG RTGLALYVAG LNALLLLLYR
PPRYQIAIRA CFLGFVFGCG TLLSFSQSSW SHFGWYMCSL SLFHYSEYLV TAVNNPKSLS
LDSFLLNHSL EYTVAALSSW LEFTLENIFW PELKQITWLS VTGLLMVVFG ECLRKAAMFT
AGSNFNHVVQ NEKSDTHTLV TSGVYAWFRH PSYVGWFYWS IGTQVMLCNP ICGVSYALTV
WRFFRDRTEE EEISLIHFFG EEYLEYKKRV PTGLPFIKGV KVDL


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