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Q93W54 (ICMTB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-S-isoprenylcysteine O-methyltransferase B

Short name=AtICMTB
EC=2.1.1.100
Alternative name(s):
Isoprenylcysteine carboxylmethyltransferase B
Prenylated protein carboxyl methyltransferase B
Prenylcysteine carboxyl methyltransferase B
Gene names
Name:ICMTB
Synonyms:STE14B
Ordered Locus Names:At5g08335
ORF Names:F8L15.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues, resulting in the modulation of the function of prenylated proteins. Involved in negative regulation of abscisic acid signaling. Carboxyl methylation is a reversible and potentially regulated step in the post-translational modification of prenylated proteins. Ref.1 Ref.6

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.

Cofactor

Divalent cations. Probably zinc By similarity.

Enzyme regulation

Inhibited by farnesylthioacetic acid (FTAA) and N-acetyl-S-trans, trans-farnesyl-l-cysteine (AFC).

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.5.

Tissue specificity

Expressed in flowers, stems, leaves, roots and siliques. Detected in apices and vascular tissues of leaves and roots, in the stigma and in the filaments and anthers of stamen. Not found in petioles or hypocotyls. Ref.1

Induction

Not induced by abscisic acid or auxin. Ref.6

Disruption phenotype

Plants lacking ICMTA and ICMTB have altered phyllotaxis, fasciated stems and development of axillary flowers. Ref.5

Miscellaneous

ICMTB is more widely expressed and has a higher catalytic activity than ICMTA.

Sequence similarities

Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=5.0 µM for AFC as methyl acceptor Ref.1

KM=3.0 µM for AGGC as methyl acceptor

Vmax=220 pmol/min/mg enzyme toward AFC as methyl acceptor

Vmax=296 pmol/min/mg enzyme toward AGGC as methyl acceptor

Sequence caution

The sequence CAC08334.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Protein-S-isoprenylcysteine O-methyltransferase B
PRO_0000356250

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane52 – 7221Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane140 – 16021Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q93W54 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 54EBEBEBADBF97DB

FASTA19722,766
        10         20         30         40         50         60 
MTEIFSDTGF RQLTQMFLAI IFFHTSEYIL AIAIHGASKV TLSSLLISKH YALAMLISVL 

        70         80         90        100        110        120 
EYIAEIVFFP GLKQHWWISN FGLTMIILGE ILRKTAIITA GRSFTHLIKI RREEHHKLVT 

       130        140        150        160        170        180 
EGVYQIMRHP SYSGFLIWSV GTQVMLCNPI SAIAFAVVVW RFFAERIPYE EHYLKQFFGR 

       190 
QYVEYAQRVP SGVPFVN 

« Hide

References

« Hide 'large scale' references
[1]"Prenylcysteine alpha-carboxyl methyltransferase expression and function in Arabidopsis thaliana."
Narasimha Chary S., Bultema R.L., Packard C.E., Crowell D.N.
Plant J. 32:735-747(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting."
Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.
Plant Physiol. 148:119-131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[6]"Isoprenylcysteine methylation and demethylation regulate abscisic acid signaling in Arabidopsis."
Huizinga D.H., Omosegbon O., Omery B., Crowell D.N.
Plant Cell 20:2714-2728(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL392174 Genomic DNA. Translation: CAC08334.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91285.1.
AY035028 mRNA. Translation: AAK59533.1.
AY059102 mRNA. Translation: AAL15208.1.
RefSeqNP_568191.1. NM_120917.1.
UniGeneAt.19166.

3D structure databases

ProteinModelPortalQ93W54.
SMRQ93W54. Positions 72-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16009. 2 interactions.
IntActQ93W54. 2 interactions.
STRING3702.AT5G08335.1-P.

Proteomic databases

PaxDbQ93W54.
PRIDEQ93W54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G08335.1; AT5G08335.1; AT5G08335.
GeneID830731.
KEGGath:AT5G08335.

Organism-specific databases

TAIRAT5G08335.

Phylogenomic databases

eggNOGCOG2020.
HOGENOMHOG000213961.
InParanoidQ93W54.
KOK00587.
OMAMLISVLE.
PhylomeDBQ93W54.
ProtClustDBCLSN2686135.

Enzyme and pathway databases

BioCycARA:AT5G08335-MONOMER.
MetaCyc:AT5G08335-MONOMER.
SABIO-RKQ93W54.

Gene expression databases

GenevestigatorQ93W54.

Family and domain databases

InterProIPR007269. ICMT_MeTrfase.
IPR025770. PPMT_MeTrfase.
[Graphical view]
PfamPF04140. ICMT. 1 hit.
[Graphical view]
PROSITEPS51564. SAM_ICMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameICMTB_ARATH
AccessionPrimary (citable) accession number: Q93W54
Secondary accession number(s): Q9FTA1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names