ID A0A072U334_MEDTR Unreviewed; 472 AA.
AC A0A072U334;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=protein-S-isoprenylcysteine alpha-carbonyl methylesterase {ECO:0000256|ARBA:ARBA00038928};
DE EC=3.1.1.n2 {ECO:0000256|ARBA:ARBA00038928};
GN Name=25501513 {ECO:0000313|EnsemblPlants:KEH20235};
GN OrderedLocusNames=MTR_8g070000 {ECO:0000313|EMBL:KEH20235.1};
GN ORFNames=MtrunA17_Chr8g0368801 {ECO:0000313|EMBL:RHN41696.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH20235.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH20235.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH20235.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH20235,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH20235.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH20235.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH20235,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH20235}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH20235};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN41696.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN41696.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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:0000256|ARBA:ARBA00035789};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Isoprenylcysteine
CC methylesterase family. {ECO:0000256|ARBA:ARBA00038028}.
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; CM001224; KEH20235.1; -; Genomic_DNA.
DR EMBL; PSQE01000008; RHN41696.1; -; Genomic_DNA.
DR RefSeq; XP_013446208.1; XM_013590754.1.
DR AlphaFoldDB; A0A072U334; -.
DR STRING; 3880.A0A072U334; -.
DR EnsemblPlants; KEH20235; KEH20235; MTR_8g070000.
DR GeneID; 25501513; -.
DR Gramene; KEH20235; KEH20235; MTR_8g070000.
DR KEGG; mtr:25501513; -.
DR OrthoDB; 1651930at2759; -.
DR Proteomes; UP000002051; Chromosome 8.
DR Proteomes; UP000265566; Chromosome 8.
DR ExpressionAtlas; A0A072U334; differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0010296; F:prenylcysteine methylesterase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR049492; BD-FAE-like_dom.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF36; ALPHA BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF20434; BD-FAE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:RHN41696.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 187..396
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51698 MW; F07F3B98A560026C CRC64;
MPSQILPITN FQPPKKPLFS SSSSSSSAST MLLKDIDDPL TSLLISSSFK DNNNAIMSVK
PLLSKASSFN NSIGSGGGGG VSCFYQKRRR RAASDDSLSC VSNGSSERSS FGRDVRHVAS
ETFLVTRLAL KMLTYLGVGY KWITQFLALG CYALLLLPGF IQVGYQYFFS SQIHRSIVYG
DKPRNRLDLF LPKNSDGPKP VVAFITGGAW IIGYKAWGSL LGQQLSERDI IVACIDYRNF
PQATISDMID DASQGISFIC NNIAEYGGDP NRIYLMGQSA GAHIAACTMV EQAIKEAGEG
ESTSWSLSQI KAYFGLSGGY NLFNLVDHFH SRGLYRSLFL SIMEGEESLR RFSPEVMVQD
PNFGNAVSLL PPIVLFHGTG DYSIPSDQSV SFADTLKRFG VKAESILYEG KTHTDVFLQD
PMRGGDDDMF DDLVAYIHAG DAEALSRDAT APPRKRLVPE FMLKLAHTVS PF
//