ID H2RUL4_TAKRU Unreviewed; 553 AA.
AC H2RUL4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Cholinesterase {ECO:0000256|ARBA:ARBA00040396};
DE EC=3.1.1.8 {ECO:0000256|ARBA:ARBA00039154};
DE AltName: Full=Acylcholine acylhydrolase {ECO:0000256|ARBA:ARBA00041860};
DE AltName: Full=Butyrylcholine esterase {ECO:0000256|ARBA:ARBA00042339};
DE AltName: Full=Choline esterase II {ECO:0000256|ARBA:ARBA00042391};
DE AltName: Full=Pseudocholinesterase {ECO:0000256|ARBA:ARBA00041941};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000003831.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000003831.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000003831.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000256|ARBA:ARBA00005964}.
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DR AlphaFoldDB; H2RUL4; -.
DR STRING; 31033.ENSTRUP00000082202; -.
DR ESTHER; fugru-BCHEB; BCHE.
DR Ensembl; ENSTRUT00000003851.3; ENSTRUP00000003831.3; ENSTRUG00000001673.3.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157637; -.
DR TreeFam; TF315470; -.
DR Proteomes; UP000005226; Chromosome 11.
DR GO; GO:0004104; F:cholinesterase activity; IEA:InterPro.
DR CDD; cd00312; Esterase_lipase; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR PANTHER; PTHR43918:SF5; CHOLINESTERASE; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022487};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..553
FT /note="Cholinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025571016"
FT DOMAIN 34..549
FT /note="Carboxylesterase type B"
FT /evidence="ECO:0000259|Pfam:PF00135"
FT ACT_SITE 234
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT ACT_SITE 469
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
SQ SEQUENCE 553 AA; 61318 MW; 5BA29B3FF7A72C44 CRC64;
AGKSDLSMVT LSSLNCLLFL SSYLATLFAN KNDLLITTNS GQVHGKILSV LDGEVRAFLG
IPYGRPPVGD LRFRAPEPMD SWQGVKNAAN YANSCFQMPD TKFPGFRGAE MWNPNTPVSE
DCLYLNVWTP RVNNTQAQAS SPLPVMIWIY GGGFTTGTSS LDLYDGRYLT KSENVIVVSM
NYRLSVFGFL SLPNNTNIRG NAALMDQRLA IQWVVDNIAA GLIFIPSITL FGESAGSACV
GFHVLSPGSN VLFQRAVMQS GVPTSPWATL SLEETWRRAI KLGTILECPT SDPAELETCL
QRVNASELII AQYGVLTEDG LGGYPFVPVV DGVFLTDHPQ IMLDNALQKD VLLGLNKDEG
SYFMAYGLPE FELGETLINY QQFKDALKQF LGANSFVSSI IYLHYISMFD SSPGKYRDGL
KNILSDVLFV CPTKEFASSY EGVGGKPFLY YFQHRSSVNP WPEWMGVMHG YEIEFVFGLP
LNPSLGYTEE EVNMSKRFMK YWATFARTGN PGSDGHEWPL YDSGSNYVTL DTAPLEVKKS
LRSYDCTFWS ILN
//
