ICML1_ARATH
ID ICML1_ARATH Reviewed; 476 AA.
AC Q8VYP9; C0Z2P7; Q9C556;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1 {ECO:0000303|PubMed:20868530};
DE EC=3.1.1.n2 {ECO:0000250|UniProtKB:Q94AS5};
DE AltName: Full=Isoprenylcysteine methylesterase-like protein 1 {ECO:0000303|PubMed:20868530};
GN Name=ICMEL1 {ECO:0000303|PubMed:20868530};
GN OrderedLocusNames=At1g26120 {ECO:0000312|Araport:AT1G26120};
GN ORFNames=F14G11.9 {ECO:0000312|EMBL:AAG50528.1},
GN F28B23.20 {ECO:0000312|EMBL:AAG50668.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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 be involved in the regulation of ABA signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q94AS5}.
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=Q8VYP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYP9-2; Sequence=VSP_041624;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:20868530}.
CC -!- INDUCTION: Down-regulated by heat treatment.
CC {ECO:0000269|PubMed:20868530}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Isoprenylcysteine
CC methylesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50528.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC079829; AAG50668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC084221; AAG50528.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30651.1; -; Genomic_DNA.
DR EMBL; AY070374; AAL49871.1; -; mRNA.
DR EMBL; AY091332; AAM14271.1; -; mRNA.
DR EMBL; AK318861; BAH56976.1; -; mRNA.
DR PIR; C86387; C86387.
DR RefSeq; NP_173937.2; NM_102377.4. [Q8VYP9-1]
DR AlphaFoldDB; Q8VYP9; -.
DR SMR; Q8VYP9; -.
DR STRING; 3702.AT1G26120.1; -.
DR ESTHER; arath-ICML1; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A21; -.
DR iPTMnet; Q8VYP9; -.
DR PaxDb; Q8VYP9; -.
DR PRIDE; Q8VYP9; -.
DR ProteomicsDB; 228762; -. [Q8VYP9-1]
DR EnsemblPlants; AT1G26120.1; AT1G26120.1; AT1G26120. [Q8VYP9-1]
DR GeneID; 839153; -.
DR Gramene; AT1G26120.1; AT1G26120.1; AT1G26120. [Q8VYP9-1]
DR KEGG; ath:AT1G26120; -.
DR Araport; AT1G26120; -.
DR TAIR; locus:2011415; AT1G26120.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_012494_2_4_1; -.
DR InParanoid; Q8VYP9; -.
DR OMA; GKDDMFE; -.
DR PhylomeDB; Q8VYP9; -.
DR PRO; PR:Q8VYP9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYP9; 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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 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..476
FT /note="Probable isoprenylcysteine alpha-carbonyl
FT methylesterase ICMEL1"
FT /id="PRO_0000411669"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 92..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /evidence="ECO:0000305"
FT ACT_SITE 388
FT /evidence="ECO:0000305"
FT ACT_SITE 420
FT /evidence="ECO:0000305"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 285..287
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT VAR_SEQ 327..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041624"
SQ SEQUENCE 476 AA; 52719 MW; 410B5D403A4AD32B CRC64;
MPSQILQISH HLPPKSSPST EMMFKSLIYD DPSTTLLSRF GDDHHTISST VKPLLSRSSS
YNGTAMKTSS SSSAGGFTGW YQNRRRRSNS DNCLSAFSDD TNGTADGGNN SGDRQTTIGQ
EVGHAAAETF LLTRLCLKLL SYLGVGYRWI TRFMALGCYA FLLMPGFIQV GYYYFFSPYV
RRSIVYGDQP RNRLDLYLPK NSTGPKPVVA FVTGGAWIIG YKAWGSLLGQ QLSERDIIVA
CIDYRNFPQG SISDMVKDAS SGISFVCNHI AEYGGDPDRI YLMGQSAGAH IAACTIVEQV
IKESGEGDSV SWSSSQINAY FGLSGGYNLL NLVDHFHSRG LYRSIFLSIM EGEESLRQFS
PELVVQNPNL KHIIARLPPF ILFHGTDDYS IPSDASKSFA ETLQRLGAKA KVILYEGKTH
TDLFLQDPMR GGIDEMFEDI VTVVLGDDQE AIGKSVDRRR LVPEFMLKLA HWVSPF
