ID U3IYS1_ANAPP Unreviewed; 626 AA.
AC U3IYS1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU361235};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361235};
GN Name=BCHE {ECO:0000313|Ensembl:ENSAPLP00000012397.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000012397.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000012397.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000012397.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Esterase with broad substrate specificity. Contributes to the
CC inactivation of the neurotransmitter acetylcholine. Can degrade
CC neurotoxic organophosphate esters. {ECO:0000256|ARBA:ARBA00037444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00036543};
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers.
CC {ECO:0000256|ARBA:ARBA00038819}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000256|ARBA:ARBA00005964, ECO:0000256|RuleBase:RU361235}.
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DR AlphaFoldDB; U3IYS1; -.
DR STRING; 8840.ENSAPLP00000012397; -.
DR ESTHER; anapl-BCHE; BCHE.
DR Ensembl; ENSAPLT00000013135.2; ENSAPLP00000012397.2; ENSAPLG00000012607.2.
DR GeneTree; ENSGT00940000157023; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR Proteomes; UP000016666; Chromosome 9.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0003990; F:acetylcholinesterase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR CDD; cd00312; Esterase_lipase; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR014788; AChE_tetra.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR PANTHER; PTHR43918:SF5; CHOLINESTERASE; 1.
DR Pfam; PF08674; AChE_tetra; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361235};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 54..573
FT /note="Carboxylesterase type B"
FT /evidence="ECO:0000259|Pfam:PF00135"
FT DOMAIN 588..622
FT /note="Acetylcholinesterase tetramerisation"
FT /evidence="ECO:0000259|Pfam:PF08674"
FT ACT_SITE 249
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT ACT_SITE 489
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
SQ SEQUENCE 626 AA; 70985 MW; 11DA25DED1B902E1 CRC64;
MGSPERRGKT WKVIREGQQG PGIMIWVNGT NIHTRFLMWL LLLYMFIRKV VPEDNIITTK
NGRVRGTNLQ VLGGTVTAFL GIPYGKPPIG RLRFQKPEPH EKWSDVWDAT KHANSCYQVI
DTTFPGFPGS EMWNPKTNLS EDCLYLNVWT PSPRPKNATV MVWIYGGGFE SGSTSLPVYD
GKFLARVERV IVVSMNYRTG ALGFLALPGN QEVPGNAGLF DQRLALQWVQ ENIAAFGGNP
KSVTIFGESA GSASVSYHIL SPKSHPLFTR AIMQSGSANA PWAAITASEA RNRTVALAKQ
LHCPTSNETE LILCLQDKDP KDILENEVYV TKYAPLLQIY FCPTVDGDFL LDMPETLIEN
GIFKQTQILV GVNKDEGSSF LAYGVPGFSK DSDSLINKTE FEAALTLSFP EASQLAIESI
IFQYTDWENE QNPEHYRDAM DDVIGDYNII CPVMEFTKKF AQLGHNAFFY FFEHRSSKLP
WPEWMGVMHG YEIEFVFGLP LERRVNYTKA EEILSRSMLR YWASFAKTGN PNGTLINGTR
WPVFTSAEQK YLTLNTDASE VLTKLRSQQC RFWNTFFPKV LEMTGNIDEA EREWKAGFHR
WNNYMSDWKN QFNDYTSKKE RCAGSN
//
