EST2_RABIT
ID EST2_RABIT Reviewed; 532 AA.
AC P14943;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Cocaine esterase {ECO:0000250|UniProtKB:O00748};
DE EC=3.1.1.84 {ECO:0000250|UniProtKB:O00748};
DE AltName: Full=Liver carboxylesterase 2;
DE EC=3.1.1.1;
GN Name=CES2; Synonyms=ICE;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Liver;
RX PubMed=2745458; DOI=10.1016/s0021-9258(18)63890-6;
RA Ozols J.;
RT "Isolation, properties, and the complete amino acid sequence of a second
RT form of 60-kDa glycoprotein esterase. Orientation of the 60-kDa proteins in
RT the microsomal membrane.";
RL J. Biol. Chem. 264:12533-12545(1989).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Converts monoacylglycerides to
CC free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and
CC prostaglandins (By similarity). {ECO:0000250|UniProtKB:O00748}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cocaine + H2O = benzoate + ecgonine methyl ester + H(+);
CC Xref=Rhea:RHEA:27506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; EC=3.1.1.84;
CC Evidence={ECO:0000250|UniProtKB:O00748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:O00748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000250|UniProtKB:O00748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) +
CC prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230,
CC ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O00748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297;
CC Evidence={ECO:0000250|UniProtKB:O00748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+)
CC + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:90233; Evidence={ECO:0000250|UniProtKB:O00748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301;
CC Evidence={ECO:0000250|UniProtKB:O00748};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:O00748}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR PIR; A34329; A34329.
DR AlphaFoldDB; P14943; -.
DR SMR; P14943; -.
DR STRING; 9986.ENSOCUP00000012531; -.
DR ESTHER; rabit-2cxes; Carb_B_Chordata.
DR MEROPS; S09.956; -.
DR PRIDE; P14943; -.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; P14943; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Lipid metabolism; Pyrrolidone carboxylic acid;
KW Reference proteome; Serine esterase.
FT CHAIN 1..532
FT /note="Cocaine esterase"
FT /id="PRO_0000070278"
FT MOTIF 529..532
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 201
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2745458"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 69..96
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 253..264
FT /evidence="ECO:0000250|UniProtKB:P23141"
SQ SEQUENCE 532 AA; 59059 MW; C57DDD76A13A9C52 CRC64;
QDSASPIRNT HTGQVRGSLV HVEGTDAGVH TFLGIPFAKP PLGPLRFAPP EPAEAWSGVR
DGTSLPAMCL QNLAIMDQDV LLLHFTPPSI PMSEDCLYLN IYSPAHAREG SDLPVMVWIH
GGGLTMGMAS MYDGSALAAF EDVVVVTIQY RLGVLGFFST GDQHATGNHG YLDQVAALRW
VQKNIAHFGG NPGRVTIFGE SAGGTSVSSH VLSPMSQGLF HGAIMESLVA LLPGLITSSS
EVVSTVVANL SRCGQVDSET LVRCLRAKSE EEMLAITQVF MLIPGVVDGV FLPRHPEELL
ALADFQPVPS IIGINNDEYG WIIPKLLLAI DPQEERDRQA MREIMHQATK QLMLPPALGD
LLMDEYMGSN EDPKHLMAQF QEMMADAMFV MPALRVAHLQ RSHAPTYFYE FQHRPSFTKD
LRPPHVRADH GDEVVFVFRS HLFGSKVPLT EEEELLSRRV MKYWANFARN RNPNGEGLAH
WPLFDLDQRY LQLNMQPAVG QALKARRLQF WTHTLPQRVQ ELRGTEQKHT EL
