ICMTB_ARATH
ID ICMTB_ARATH Reviewed; 197 AA.
AC Q93W54; Q9FTA1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase B {ECO:0000303|PubMed:12472689};
DE Short=AtICMTB {ECO:0000303|PubMed:18641086};
DE EC=2.1.1.100 {ECO:0000269|PubMed:12472689};
DE AltName: Full=Isoprenylcysteine carboxylmethyltransferase B {ECO:0000303|PubMed:12472689};
DE AltName: Full=Prenylated protein carboxyl methyltransferase B {ECO:0000303|PubMed:12472689};
DE AltName: Full=Prenylcysteine carboxyl methyltransferase 14 B {ECO:0000303|PubMed:12472689};
DE Short=AtSTE14B {ECO:0000303|PubMed:12472689};
GN Name=ICMTB {ECO:0000303|PubMed:18641086};
GN Synonyms=STE14B {ECO:0000303|PubMed:12472689};
GN OrderedLocusNames=At5g08335 {ECO:0000312|Araport:AT5G08335};
GN ORFNames=F8L15.70 {ECO:0000312|EMBL:CAC08334.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=12472689; DOI=10.1046/j.1365-313x.2002.01463.x;
RA Narasimha Chary S., Bultema R.L., Packard C.E., Crowell D.N.;
RT "Prenylcysteine alpha-carboxyl methyltransferase expression and function in
RT Arabidopsis thaliana.";
RL Plant J. 32:735-747(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18641086; DOI=10.1104/pp.108.120477;
RA Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.;
RT "Functional analysis of Arabidopsis postprenylation CaaX processing enzymes
RT and their function in subcellular protein targeting.";
RL Plant Physiol. 148:119-131(2008).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=18957507; DOI=10.1105/tpc.107.053389;
RA Huizinga D.H., Omosegbon O., Omery B., Crowell D.N.;
RT "Isoprenylcysteine methylation and demethylation regulate abscisic acid
RT signaling in Arabidopsis.";
RL Plant Cell 20:2714-2728(2008).
CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated
CC C-terminal cysteine residues, resulting in the modulation of the
CC function of prenylated proteins. Involved in negative regulation of
CC abscisic acid signaling. Carboxyl methylation is a reversible and
CC potentially regulated step in the post-translational modification of
CC prenylated proteins. {ECO:0000269|PubMed:12472689,
CC ECO:0000269|PubMed:18957507}.
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:12472689};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Probably Zn(2+). {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by farnesylthioacetic acid (FTAA) and N-
CC acetyl-S-trans, trans-farnesyl-l-cysteine (AFC).
CC {ECO:0000269|PubMed:12472689}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.0 uM for AFC as methyl acceptor {ECO:0000269|PubMed:12472689};
CC KM=3.0 uM for AGGC as methyl acceptor {ECO:0000269|PubMed:12472689};
CC Vmax=220 pmol/min/mg enzyme toward AFC as methyl acceptor
CC {ECO:0000269|PubMed:12472689};
CC Vmax=296 pmol/min/mg enzyme toward AGGC as methyl acceptor
CC {ECO:0000269|PubMed:12472689};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18641086}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18641086}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, stems, leaves, roots and
CC siliques. Detected in apices and vascular tissues of leaves and roots,
CC in the stigma and in the filaments and anthers of stamen. Not found in
CC petioles or hypocotyls. {ECO:0000269|PubMed:12472689}.
CC -!- INDUCTION: Not induced by abscisic acid or auxin.
CC {ECO:0000269|PubMed:18957507}.
CC -!- DISRUPTION PHENOTYPE: Plants lacking ICMTA and ICMTB have altered
CC phyllotaxis, fasciated stems and development of axillary flowers.
CC {ECO:0000269|PubMed:18641086}.
CC -!- MISCELLANEOUS: ICMTB is more widely expressed and has a higher
CC catalytic activity than ICMTA. {ECO:0000269|PubMed:18641086}.
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=CAC08334.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL392174; CAC08334.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91285.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69655.1; -; Genomic_DNA.
DR EMBL; AY035028; AAK59533.1; -; mRNA.
DR EMBL; AY059102; AAL15208.1; -; mRNA.
DR RefSeq; NP_001331317.1; NM_001342996.1.
DR RefSeq; NP_568191.1; NM_120917.2.
DR AlphaFoldDB; Q93W54; -.
DR SMR; Q93W54; -.
DR BioGRID; 16009; 2.
DR IntAct; Q93W54; 2.
DR STRING; 3702.AT5G08335.1; -.
DR PaxDb; Q93W54; -.
DR PRIDE; Q93W54; -.
DR ProteomicsDB; 228765; -.
DR EnsemblPlants; AT5G08335.1; AT5G08335.1; AT5G08335.
DR EnsemblPlants; AT5G08335.2; AT5G08335.2; AT5G08335.
DR GeneID; 830731; -.
DR Gramene; AT5G08335.1; AT5G08335.1; AT5G08335.
DR Gramene; AT5G08335.2; AT5G08335.2; AT5G08335.
DR KEGG; ath:AT5G08335; -.
DR Araport; AT5G08335; -.
DR TAIR; locus:505006585; AT5G08335.
DR eggNOG; KOG2628; Eukaryota.
DR HOGENOM; CLU_065200_0_2_1; -.
DR InParanoid; Q93W54; -.
DR OMA; GMVPQVW; -.
DR OrthoDB; 1479599at2759; -.
DR PhylomeDB; Q93W54; -.
DR BioCyc; MetaCyc:AT5G08335-MON; -.
DR BRENDA; 2.1.1.100; 399.
DR SABIO-RK; Q93W54; -.
DR PRO; PR:Q93W54; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93W54; baseline and differential.
DR Genevisible; Q93W54; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:TAIR.
DR GO; GO:0006481; P:C-terminal protein methylation; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; NAS:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
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 Endoplasmic reticulum; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..197
FT /note="Protein-S-isoprenylcysteine O-methyltransferase B"
FT /id="PRO_0000356250"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 116..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 129..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
SQ SEQUENCE 197 AA; 22766 MW; 54EBEBEBADBF97DB CRC64;
MTEIFSDTGF RQLTQMFLAI IFFHTSEYIL AIAIHGASKV TLSSLLISKH YALAMLISVL
EYIAEIVFFP GLKQHWWISN FGLTMIILGE ILRKTAIITA GRSFTHLIKI RREEHHKLVT
EGVYQIMRHP SYSGFLIWSV GTQVMLCNPI SAIAFAVVVW RFFAERIPYE EHYLKQFFGR
QYVEYAQRVP SGVPFVN
