ICME_ARATH
ID ICME_ARATH Reviewed; 427 AA.
AC Q94AS5; F4KBA0; Q9LFU2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Isoprenylcysteine alpha-carbonyl methylesterase ICME {ECO:0000303|PubMed:18957507, ECO:0000303|PubMed:20868530};
DE EC=3.1.1.n2 {ECO:0000269|PubMed:16870359, ECO:0000269|PubMed:18957507};
DE AltName: Full=Isoprenylcysteine methylesterase {ECO:0000303|PubMed:18957507, ECO:0000303|PubMed:20868530};
DE AltName: Full=Prenylcysteine methylesterase {ECO:0000303|PubMed:16870359};
DE Short=AtPCME {ECO:0000303|PubMed:16870359};
GN Name=ICME {ECO:0000303|PubMed:18957507, ECO:0000303|PubMed:20868530};
GN Synonyms=PCME {ECO:0000303|PubMed:16870359};
GN OrderedLocusNames=At5g15860 {ECO:0000312|Araport:AT5G15860};
GN ORFNames=F14F8.240 {ECO:0000312|EMBL:CAC01785.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=16870359; DOI=10.1016/j.gene.2006.05.023;
RA Deem A.K., Bultema R.L., Crowell D.N.;
RT "Prenylcysteine methylesterase in Arabidopsis thaliana.";
RL Gene 380:159-166(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=20868530; DOI=10.1186/1471-2229-10-212;
RA Lan P., Li W., Wang H., Ma W.;
RT "Characterization, sub-cellular localization and expression profiling of
RT the isoprenylcysteine methylesterase gene family in Arabidopsis thaliana.";
RL BMC Plant Biol. 10:212-212(2010).
CC -!- FUNCTION: Catalyzes the demethylation of isoprenylcysteine
CC methylesters. In vitro, is specific for N-acetyl-S-farnesyl-L-cysteine
CC methyl ester (AFCme) and has low activity toward N-acetyl-S-geranyl-L-
CC cysteine methyl ester (AGCme). Acts as a positive regulator of ABA
CC signaling. May be involved in the demethylation and inactivation of
CC isoprenylated negative regulators of abscisic acid (ABA) signaling.
CC Carboxyl methylation is a reversible and potentially regulated step in
CC the post-translational modification of prenylated proteins.
CC {ECO:0000269|PubMed:16870359, ECO:0000269|PubMed:18957507,
CC ECO:0000269|PubMed:20868530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl
CC ester + H2O = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine +
CC H(+) + methanol; Xref=Rhea:RHEA:48520, Rhea:RHEA-COMP:12125,
CC Rhea:RHEA-COMP:12126, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:90510, ChEBI:CHEBI:90511; EC=3.1.1.n2;
CC Evidence={ECO:0000269|PubMed:16870359, ECO:0000269|PubMed:18957507};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20868530}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:20868530}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20868530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94AS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AS5-2; Sequence=VSP_041622, VSP_041623;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:20868530}.
CC -!- INDUCTION: By ABA, osmotic stress and salt and heat treatments.
CC {ECO:0000269|PubMed:18957507, ECO:0000269|PubMed:20868530}.
CC -!- MISCELLANEOUS: Plants overexpressing ICME exhibit enhanced ABA
CC inhibition of seed germination and ABA induction of stomatal closure.
CC Plant silencing ICME exhibit a reduced ABA sensitivity in seed
CC germination assays. {ECO:0000269|PubMed:18957507}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Isoprenylcysteine
CC methylesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391144; CAC01785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92217.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92218.1; -; Genomic_DNA.
DR EMBL; AY045829; AAK76503.1; -; mRNA.
DR EMBL; AY091367; AAM14306.1; -; mRNA.
DR PIR; T51415; T51415.
DR RefSeq; NP_197090.2; NM_121591.5. [Q94AS5-1]
DR RefSeq; NP_974786.1; NM_203057.1. [Q94AS5-2]
DR AlphaFoldDB; Q94AS5; -.
DR SMR; Q94AS5; -.
DR BioGRID; 16719; 1.
DR STRING; 3702.AT5G15860.1; -.
DR ESTHER; arath-F14F8.240; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A26; -.
DR iPTMnet; Q94AS5; -.
DR PaxDb; Q94AS5; -.
DR PRIDE; Q94AS5; -.
DR ProteomicsDB; 228761; -. [Q94AS5-1]
DR EnsemblPlants; AT5G15860.1; AT5G15860.1; AT5G15860. [Q94AS5-1]
DR EnsemblPlants; AT5G15860.2; AT5G15860.2; AT5G15860. [Q94AS5-2]
DR GeneID; 831443; -.
DR Gramene; AT5G15860.1; AT5G15860.1; AT5G15860. [Q94AS5-1]
DR Gramene; AT5G15860.2; AT5G15860.2; AT5G15860. [Q94AS5-2]
DR KEGG; ath:AT5G15860; -.
DR Araport; AT5G15860; -.
DR TAIR; locus:2143236; AT5G15860.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_012494_2_4_1; -.
DR InParanoid; Q94AS5; -.
DR OMA; GYRWMTR; -.
DR OrthoDB; 992858at2759; -.
DR PhylomeDB; Q94AS5; -.
DR BioCyc; MetaCyc:AT5G15860-MON; -.
DR PRO; PR:Q94AS5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AS5; baseline and differential.
DR Genevisible; Q94AS5; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0010296; F:prenylcysteine methylesterase activity; IDA:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..427
FT /note="Isoprenylcysteine alpha-carbonyl methylesterase
FT ICME"
FT /id="PRO_0000411668"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /evidence="ECO:0000305"
FT ACT_SITE 336
FT /evidence="ECO:0000305"
FT ACT_SITE 368
FT /evidence="ECO:0000305"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT VAR_SEQ 276..299
FT /note="NLYKLVDHFHNRGLYRSIFLSIME -> LLSFWIPVGFYVLFGLQQLICLSF
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041622"
FT VAR_SEQ 300..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041623"
SQ SEQUENCE 427 AA; 47582 MW; 7B9BC826C4D0DDCA CRC64;
MHSPLQTQQP EQRCWPMTST VSEIEEVLPD EDSDRTTLLN GEPLRRRVSG KSPVDEGPRR
IFRQQSFGRD IGHAAAETYL ITGLSFKLLR YLGVGYRWMT KLLALTCYAM LLMPGFLQVA
YSYFFSKQVR RSIVYGDQPR NRLDLYLPSN NDGLKPVVVF VTGGAWIIGY KAWGSLLGMQ
LAERDIIVAC LDYRNFPQGT ISDMVTDASQ GISFVCNNIS AFGGDPNRIY LMGQSAGAHI
AACALLEQAT KELKGESISW TVSQIKAYFG LSGGYNLYKL VDHFHNRGLY RSIFLSIMEG
EESFEKFSPE VRLKDPVVGK AASLLPPIIL FHGSSDYSIP CDESKTFTDA LQAVGAKAEL
VLYSGKTHTD LFLQDPLRGG KDELFDDIVS VIHAEDNDGL TKDSLAPPRK RLVPELLLKL
AREISPF
