ID A0A067FS18_CITSI Unreviewed; 454 AA.
AC A0A067FS18;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=protein-S-isoprenylcysteine alpha-carbonyl methylesterase {ECO:0000256|ARBA:ARBA00038928};
DE EC=3.1.1.n2 {ECO:0000256|ARBA:ARBA00038928};
GN ORFNames=CISIN_1g011866mg {ECO:0000313|EMBL:KDO70138.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO70138.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO70138.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK784891; KDO70138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067FS18; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..378
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT REGION 59..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 49841 MW; A6190EB3561FC4C8 CRC64;
MPSQILPVTH HHRGTEAAAM LIKAEIERDD PTTSLLISSE YEDVEKAITS IKPVLSRTSS
YNNNNITSPN DSPGLGNCYQ QRRRRSASDN SLSSLSGSNG SGAASSAGGS RRHSFSKDVG
RAAAETFLVT RLSFKLLRYL GVGYRWIVRF LALGCYSLLL LPGFIQVGCH YFFSSQVRRG
IVYGDQPRNR LDLYFPKSSD GPKPVVAFIT GGAWIIGYKA WGSLLGQQLS ERDIIVACID
YRNFPQGTIK DMVKDASQGI SFVCNNISEY GGDPDRIYLM GQSAGAHIAA CTLLEQAIKE
TGEGESTTWS VSQIRAYFGL SGGIMDGEES LRQYSPEVLV QDPNTRHAVS LLPPIILFHG
TADYSIPADA SKNFANTLQR VGVRAESILY EGKTHTDLFL QDPMRGGKDD MFEDIVAIIH
ADDQEARAKD AVAPPRRRLV PEFMLKLARS ISPF
//
