ICML2_ARATH
ID ICML2_ARATH Reviewed; 422 AA.
AC Q1PET6; A0MEU1; B3H6W3; Q9M899;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2 {ECO:0000303|PubMed:20868530};
DE EC=3.1.1.n2 {ECO:0000250|UniProtKB:Q94AS5};
DE AltName: Full=Isoprenylcysteine methylesterase-like protein 2 {ECO:0000303|PubMed:20868530};
GN Name=ICMEL2 {ECO:0000303|PubMed:20868530};
GN OrderedLocusNames=At3g02410 {ECO:0000312|Araport:AT3G02410};
GN ORFNames=F16B3.4 {ECO:0000312|EMBL:AAF32448.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 methylesters
CC (By similarity). May act as a negative regulator of ABA signaling
CC (PubMed:20868530). {ECO:0000250|UniProtKB:Q94AS5,
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:0000250|UniProtKB:Q94AS5};
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=Q1PET6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1PET6-2; Sequence=VSP_041625, VSP_041626;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in flowers and siliques.
CC {ECO:0000269|PubMed:20868530}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to abscissic acid (ABA) but
CC slightly decreased sensitivity to salt and osmotic stresses during seed
CC germination. {ECO:0000269|PubMed:20868530}.
CC -!- MISCELLANEOUS: Plants silencing ICMEL2 show enhanced ABA inhibition of
CC seed germination. {ECO:0000269|PubMed:20868530}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Isoprenylcysteine
CC methylesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF32448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABK28542.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC021640; AAF32448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73804.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73805.1; -; Genomic_DNA.
DR EMBL; DQ446631; ABE65914.1; -; mRNA.
DR EMBL; DQ653064; ABK28542.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001118556.1; NM_001125084.1. [Q1PET6-2]
DR RefSeq; NP_186890.2; NM_111108.4. [Q1PET6-1]
DR AlphaFoldDB; Q1PET6; -.
DR SMR; Q1PET6; -.
DR BioGRID; 6524; 23.
DR IntAct; Q1PET6; 23.
DR STRING; 3702.AT3G02410.1; -.
DR ESTHER; arath-F16B3.4; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A62; -.
DR PaxDb; Q1PET6; -.
DR PRIDE; Q1PET6; -.
DR ProteomicsDB; 228763; -. [Q1PET6-1]
DR EnsemblPlants; AT3G02410.1; AT3G02410.1; AT3G02410. [Q1PET6-1]
DR EnsemblPlants; AT3G02410.2; AT3G02410.2; AT3G02410. [Q1PET6-2]
DR GeneID; 821191; -.
DR Gramene; AT3G02410.1; AT3G02410.1; AT3G02410. [Q1PET6-1]
DR Gramene; AT3G02410.2; AT3G02410.2; AT3G02410. [Q1PET6-2]
DR KEGG; ath:AT3G02410; -.
DR Araport; AT3G02410; -.
DR TAIR; locus:2076979; AT3G02410.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; Q1PET6; -.
DR OMA; CESIASF; -.
DR PhylomeDB; Q1PET6; -.
DR PRO; PR:Q1PET6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PET6; baseline and differential.
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:0010296; F:prenylcysteine methylesterase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..422
FT /note="Probable isoprenylcysteine alpha-carbonyl
FT methylesterase ICMEL2"
FT /id="PRO_0000411670"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /evidence="ECO:0000305"
FT ACT_SITE 331
FT /evidence="ECO:0000305"
FT ACT_SITE 363
FT /evidence="ECO:0000305"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041625"
FT VAR_SEQ 70..89
FT /note="AAETYLITRLSFNLLGYLGV -> MQLPRRISLLDLASTFLDIS (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041626"
SQ SEQUENCE 422 AA; 47010 MW; 17400548BB60F784 CRC64;
MQLSPERCRP MSENREAWSA NSEEMELLHG SNRLSSPEHV RRRVSGNSSE DGSPRICRQQ
SFGRDIGHAA AETYLITRLS FNLLGYLGVG YRWITRLLAL ACYAMLLMPG FLQVAYLYFF
SSQVRRSIVY GGHPRNRLDL YIPPTSDGLK PVVVFVTGGA WIIGYKAWGS LLGLQLAERD
IIVACLDYRN FPQGTISDMV SDAAQGISFV CNNISAFGGD PNRIYLMGQS AGAHISSCAL
FEQAIKESRG ESISWSVSQI KAYFGLSGGY NLFNLVEHFH NRGLYRSIFL SIMEGEESFK
QFSPEVRLKD LNVRKAAALL PHIILFHGSA DYSIPPEASK TFTDALQAAE VKAELVMYKG
KTHTDLFLQD PLRGGKDELF DHIVSMIHAD DSDALRNDAV APPRKRLVPE FLLKLAGRVS
PF
