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EST3_PONAB
ID   EST3_PONAB              Reviewed;         569 AA.
AC   Q5RCL7; Q5RFG4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Carboxylesterase 3;
DE            EC=3.1.1.1;
DE   AltName: Full=Liver carboxylesterase 31 homolog;
DE   Flags: Precursor;
GN   Name=CES3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC       activation of ester and amide prodrugs. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857194; CAH89493.1; -; mRNA.
DR   EMBL; CR858253; CAH90490.1; -; mRNA.
DR   RefSeq; NP_001125256.1; NM_001131784.1.
DR   RefSeq; NP_001128738.1; NM_001135266.1.
DR   AlphaFoldDB; Q5RCL7; -.
DR   SMR; Q5RCL7; -.
DR   STRING; 9601.ENSPPYP00000008401; -.
DR   ESTHER; ponab-est3; Carb_B_Chordata.
DR   GeneID; 100172153; -.
DR   GeneID; 100189629; -.
DR   KEGG; pon:100172153; -.
DR   CTD; 23491; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   InParanoid; Q5RCL7; -.
DR   Proteomes; UP000001595; 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   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Reference proteome; Serine esterase; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..569
FT                   /note="Carboxylesterase 3"
FT                   /id="PRO_0000305192"
FT   MOTIF           566..569
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        227
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        458
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..290
FT                   /evidence="ECO:0000250"
FT   CONFLICT        333
FT                   /note="H -> R (in Ref. 1; CAH89493)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="C -> F (in Ref. 1; CAH89493)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="V -> F (in Ref. 1; CAH89493)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="E -> G (in Ref. 1; CAH89493)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="W -> R (in Ref. 1; CAH90490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="H -> Q (in Ref. 1; CAH89493)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   569 AA;  62439 MW;  2720B9C19D028373 CRC64;
     MRLHRLRARL NAVAFGLLLL LVHGQGPEIV QPEVDTTLGR VRGRQVGVKG TDRLVNVFLG
     IPFAQPPLGP DRFSAPHPAQ PWEGVRDASA APPMCLQDVE SMNNSRFVLN GKQQIFSVSE
     DCLVLNIYSP AEATAGAGRP VMVWVHGGAL ITGAATSYDG SALAAYGDVV VVTVQYRLGV
     LGFFSTGDEH APGNQGFLDV VAALRWVQGN ITPFGGDLNC VTVFGGSAGG SIVSGLVLSP
     MAAGLFHRAI TQSGVITTPG IIESHPWPLA QKITNTLACS SSSPAEMVQC LRQKEGEELV
     LSKKLKSTIY PLTVDGTVFP KSPKELLKEK PFHSVPFLMG VNNHEFSWLI PRGWGLLDTM
     EQMSREDMLA ISTPVLTSLD VPPEMMPTVI DEYLGSNSDA QAKCLAFQEF MGDVFINVPT
     VSFSRYLRDS GSPVFFYEFQ HRPSSFAKIK PAWVKADHAA EGAFVFGGPF LMDESSRLAF
     PEATEEEKQL SLTMMAQWTH FARTGDPNSK GLPPWPRFNQ AEQYLEINPV PRAGQKFRET
     RMQFWSETLP SKIQQWHQKQ KNRKAQEDL
 
 
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