EST5C_DROPE
ID EST5C_DROPE Reviewed; 545 AA.
AC O16171;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Esterase-5C;
DE Short=Est-5C;
DE EC=3.1.1.1;
DE AltName: Full=Carboxylic-ester hydrolase 5C;
DE Short=Carboxylesterase-5C;
DE Flags: Precursor;
GN Name=Est-5C; Synonyms=Est5C;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9475741; DOI=10.1093/genetics/148.1.305;
RA King L.M.;
RT "The role of gene conversion in determining sequence variation and
RT divergence in the Est-5 gene family in Drosophila pseudoobscura.";
RL Genetics 148:305-315(1998).
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: Secreted.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF016110; AAB70222.1; -; Genomic_DNA.
DR AlphaFoldDB; O16171; -.
DR SMR; O16171; -.
DR STRING; 7234.FBpp0189268; -.
DR ESTHER; drope-est5c; Carb_B_Arthropoda.
DR MEROPS; S09.947; -.
DR eggNOG; KOG1516; Eukaryota.
DR GO; GO:0005576; C:extracellular region; 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 InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..545
FT /note="Esterase-5C"
FT /id="PRO_0000008559"
FT ACT_SITE 207
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..103
FT /evidence="ECO:0000250"
FT DISULFID 259..271
FT /evidence="ECO:0000250"
FT DISULFID 515..536
FT /evidence="ECO:0000255"
SQ SEQUENCE 545 AA; 60921 MW; 56AC03A500E15B92 CRC64;
MLAARLIILL SFYWLSASAI DPADPLFVDL PHGKIRGRDN GFYYSYESLP YAEPPVGELR
FEAPQPYKQQ WTDTFDATQP PVTCMQWNQF IFGDNKLAGV EDCLTVSIYK PKNTSQSSFP
VVAHMHGGAF MFGEARQNGH ENMMREGKLI LVKISYRLGP LGFASTGDAG LSGNFGLKDQ
RLALLWIKQN IASFGGEPEN IIVVGHSAGG ASVHLQMLRE DFAQVAKAGI SFGGNAMDPW
VIHQSARGRT FELGRIVGCG QASDSTELKN CLKSKPAGEI VSAVHSFLVF AYVPFAPFGP
VVESPDAPEA FISQHPVDII KSGKFAQVPW AVTYNTEDGG YNAAVLLEKQ ASSGRELIFD
LNDHWFDWAP YLLFYRDSMT TIKDMDDYSR KLRQEYLGDR RFSVESYWDL QRLFTDILYK
NATELALDLY RKHGKSPVYA FVYDNPANTG IGQFFSKRTD VHFGTVHGDE YFLIFENLAR
GPEMRSDEEI ISRNFLNMIN DFVVSGNGTM TFGNCVLQDN VGSNKFQLLS ITKNGCENLQ
LESFP