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Liver carboxylesterase 1 (EC 3.1.1.1) (Acyl-coenzyme A:cholesterol acyltransferase)

 EST1_RABIT              Reviewed;         565 AA.
P12337; O77540;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 3.
05-DEC-2018, entry version 124.
RecName: Full=Liver carboxylesterase 1;
EC=3.1.1.1;
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase;
Flags: Precursor;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-52, AND FUNCTION.
TISSUE=Liver;
PubMed=9635592;
Potter P.M., Pawlik C.A., Morton C.L., Naeve C.W., Danks M.K.;
"Isolation and partial characterization of a cDNA encoding a rabbit
liver carboxylesterase that activates the prodrug irinotecan (CPT-
11).";
Cancer Res. 58:2646-2651(1998).
[2]
PROTEIN SEQUENCE OF 19-557, AND ACTIVE SITES SER-221 AND HIS-467.
PubMed=3343253;
Korza G., Ozols J.;
"Complete covalent structure of 60-kDa esterase isolated from 2,3,7,8-
tetrachlorodibenzo-p-dioxin-induced rabbit liver microsomes.";
J. Biol. Chem. 263:3486-3495(1988).
[3]
PROTEIN SEQUENCE OF 19-88 AND 558-565.
PubMed=3667634;
Ozols J.;
"Isolation and characterization of a 60-kilodalton glycoprotein
esterase from liver microsomal membranes.";
J. Biol. Chem. 262:15316-15321(1987).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-565 IN COMPLEX WITH
PRODUCT.
PubMed=11967565; DOI=10.1038/nsb790;
Bencharit S., Morton C.L., Howard-Williams E.L., Danks M.K.,
Potter P.M., Redinbo M.R.;
"Structural insights into CPT-11 activation by mammalian
carboxylesterases.";
Nat. Struct. Biol. 9:337-342(2002).
-!- FUNCTION: Involved in the detoxification of xenobiotics and in the
activation of ester and amide prodrugs.
{ECO:0000269|PubMed:9635592}.
-!- CATALYTIC ACTIVITY:
Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol +
H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879,
ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-
ProRule:PRU10039};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11967565}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal
membrane, lumen of endoplasmic reticulum.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF036930; AAC39258.1; -; mRNA.
PIR; A29923; A29923.
RefSeq; NP_001076234.1; NM_001082765.2.
UniGene; Ocu.2266; -.
PDB; 1K4Y; X-ray; 2.50 A; A=23-556.
PDBsum; 1K4Y; -.
ProteinModelPortal; P12337; -.
SMR; P12337; -.
STRING; 9986.ENSOCUP00000005826; -.
BindingDB; P12337; -.
ChEMBL; CHEMBL2623; -.
ESTHER; rabit-1cxes; Carb_B_Chordata.
iPTMnet; P12337; -.
PRIDE; P12337; -.
GeneID; 100009551; -.
KEGG; ocu:100009551; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
KO; K01044; -.
BRENDA; 3.1.1.1; 1749.
SABIO-RK; P12337; -.
EvolutionaryTrace; P12337; -.
PRO; PR:P12337; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Reference proteome; Serine esterase; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:3343253,
ECO:0000269|PubMed:3667634,
ECO:0000269|PubMed:9635592}.
CHAIN 19 565 Liver carboxylesterase 1.
/FTId=PRO_0000008578.
MOTIF 565 565 Prevents secretion from ER.
{ECO:0000255}.
ACT_SITE 221 221 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 353 353 Charge relay system. {ECO:0000250}.
ACT_SITE 467 467 Charge relay system. {ECO:0000250}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3343253}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3343253}.
DISULFID 87 116
DISULFID 273 284
CONFLICT 30 30 H -> K (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 Q -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 175 198 WGFFSTGDEHSRGNWGHLDQVAAL -> GGFGFNIDELFLV
AVN (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 335 336 LA -> YE (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 36 38 {ECO:0000244|PDB:1K4Y}.
STRAND 47 56 {ECO:0000244|PDB:1K4Y}.
HELIX 61 63 {ECO:0000244|PDB:1K4Y}.
STRAND 86 88 {ECO:0000244|PDB:1K4Y}.
HELIX 91 101 {ECO:0000244|PDB:1K4Y}.
STRAND 103 106 {ECO:0000244|PDB:1K4Y}.
STRAND 112 114 {ECO:0000244|PDB:1K4Y}.
STRAND 118 123 {ECO:0000244|PDB:1K4Y}.
STRAND 133 139 {ECO:0000244|PDB:1K4Y}.
TURN 143 145 {ECO:0000244|PDB:1K4Y}.
HELIX 155 161 {ECO:0000244|PDB:1K4Y}.
STRAND 164 168 {ECO:0000244|PDB:1K4Y}.
HELIX 173 177 {ECO:0000244|PDB:1K4Y}.
HELIX 189 204 {ECO:0000244|PDB:1K4Y}.
HELIX 205 208 {ECO:0000244|PDB:1K4Y}.
STRAND 210 220 {ECO:0000244|PDB:1K4Y}.
HELIX 222 232 {ECO:0000244|PDB:1K4Y}.
HELIX 234 236 {ECO:0000244|PDB:1K4Y}.
TURN 237 239 {ECO:0000244|PDB:1K4Y}.
STRAND 241 247 {ECO:0000244|PDB:1K4Y}.
STRAND 253 256 {ECO:0000244|PDB:1K4Y}.
HELIX 261 271 {ECO:0000244|PDB:1K4Y}.
HELIX 278 287 {ECO:0000244|PDB:1K4Y}.
HELIX 290 300 {ECO:0000244|PDB:1K4Y}.
STRAND 324 326 {ECO:0000244|PDB:1K4Y}.
HELIX 331 337 {ECO:0000244|PDB:1K4Y}.
STRAND 345 351 {ECO:0000244|PDB:1K4Y}.
HELIX 376 383 {ECO:0000244|PDB:1K4Y}.
HELIX 385 388 {ECO:0000244|PDB:1K4Y}.
TURN 392 394 {ECO:0000244|PDB:1K4Y}.
HELIX 395 402 {ECO:0000244|PDB:1K4Y}.
HELIX 416 424 {ECO:0000244|PDB:1K4Y}.
HELIX 426 437 {ECO:0000244|PDB:1K4Y}.
TURN 438 440 {ECO:0000244|PDB:1K4Y}.
STRAND 443 448 {ECO:0000244|PDB:1K4Y}.
HELIX 469 474 {ECO:0000244|PDB:1K4Y}.
TURN 475 479 {ECO:0000244|PDB:1K4Y}.
STRAND 480 482 {ECO:0000244|PDB:1K4Y}.
HELIX 486 505 {ECO:0000244|PDB:1K4Y}.
STRAND 525 531 {ECO:0000244|PDB:1K4Y}.
STRAND 533 535 {ECO:0000244|PDB:1K4Y}.
HELIX 540 552 {ECO:0000244|PDB:1K4Y}.
SEQUENCE 565 AA; 62292 MW; 0ACD61400CC81D2F CRC64;
MWLCALALAS LAACTAWGHP SAPPVVDTVH GKVLGKFVSL EGFAQPVAVF LGVPFAKPPL
GSLRFAPPQP AESWSHVKNT TSYPPMCSQD AVSGHMLSEL FTNRKENIPL KFSEDCLYLN
IYTPADLTKR GRLPVMVWIH GGGLMVGGAS TYDGLALSAH ENVVVVTIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALRW VQDNIANFGG DPGSVTIFGE SAGGQSVSIL LLSPLTKNLF
HRAISESGVA LLSSLFRKNT KSLAEKIAIE AGCKTTTSAV MVHCLRQKTE EELMEVTLKM
KFMALDLVGD PKENTAFLTT VIDGVLLPKA PAEILAEKKY NMLPYMVGIN QQEFGWIIPM
QMLGYPLSEG KLDQKTATEL LWKSYPIVNV SKELTPVATE KYLGGTDDPV KKKDLFLDML
ADLLFGVPSV NVARHHRDAG APTYMYEYRY RPSFSSDMRP KTVIGDHGDE IFSVLGAPFL
KEGATEEEIK LSKMVMKYWA NFARNGNPNG EGLPQWPAYD YKEGYLQIGA TTQAAQKLKD
KEVAFWTELW AKEAARPRET EHIEL


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