CHLE2_BRALA
ID CHLE2_BRALA Reviewed; 337 AA.
AC Q95001;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Cholinesterase 2;
DE EC=3.1.1.8;
DE Flags: Fragment;
GN Name=CHE2;
OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7740;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9062997;
RX DOI=10.1002/(sici)1097-010x(19970215)277:3<213::aid-jez3>3.0.co;2-r;
RA Sutherland D., McClellan J.S., Milner D., Soong W., Axon N., Sanders M.,
RA Hester A., Kao Y.H., Poczatek T., Routt S., Pezzementi L.;
RT "Two cholinesterase activities and genes are present in amphioxus.";
RL J. Exp. Zool. 277:213-229(1997).
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 -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; U74379; AAB18263.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95001; -.
DR SMR; Q95001; -.
DR MEROPS; S09.980; -.
DR GO; GO:0004104; F:cholinesterase 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 InterPro; IPR000997; Cholinesterase.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Serine esterase.
FT CHAIN <1..>337
FT /note="Cholinesterase 2"
FT /id="PRO_0000070290"
FT ACT_SITE 99
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 153..165
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 337
SQ SEQUENCE 337 AA; 36738 MW; C9DE20A316C71258 CRC64;
QPSPVPVGAT VMVWIYGGGF MSGTASLDVY DGRYIAATQG VIVASMNYRT GAMGFLSLGN
SEAPGNAGLM DQNLALTWIK ENVASFGGDQ SKVSIFGESA GAASVSYHLL SPMSKNLFQR
AIMESASALS PWALLPDAEA HRRGVELAKA VGCSTDSDIE ETIECMRGVP ALTISENEWV
VWGLCQFPFA PVVDGNFIRE HPTVSLQTGN LKQTDVMVGF NNDEGVYFLL YGAPGFSKDT
QSLITRDQYL EGIKMSVMGI NDISVDALSF QYIDWVNFDQ PSMYRDAIDN LSGDYNFICP
ALSFGKAMAS FMGRKTYQYK FVHQASNFPW PKWTGVM