EST5A_DROMI
ID EST5A_DROMI Reviewed; 555 AA.
AC O16168;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Esterase-5A;
DE Short=Est-5A;
DE EC=3.1.1.1;
DE AltName: Full=Carboxylic-ester hydrolase 5A;
DE Short=Carboxylesterase-5A;
DE Flags: Precursor;
GN Name=Est-5A; Synonyms=Est5A;
OS Drosophila miranda (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7229;
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}.
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DR EMBL; AF016108; AAB70219.1; -; Genomic_DNA.
DR AlphaFoldDB; O16168; -.
DR SMR; O16168; -.
DR ESTHER; dromi-est5a; Carb_B_Arthropoda.
DR MEROPS; S09.947; -.
DR FlyBase; FBgn0021338; Dmir\Est-5A.
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..555
FT /note="Esterase-5A"
FT /id="PRO_0000008552"
FT ACT_SITE 210
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..106
FT /evidence="ECO:0000250"
FT DISULFID 262..274
FT /evidence="ECO:0000250"
FT DISULFID 518..539
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 62282 MW; E8EACEA4AE379630 CRC64;
MHLVRWLICL IQLWIQLGAA GSVTLLDPLL IEIPNGKLRG RDNGHYYSYE AIPYAEPPTG
ELRFEVPKPY KQQWTNTFDA TQPPVLCMQW NQFINGTNKL LGVEDCLTVS VYRPKNSSRN
NFPVVANLHG GAFMFGGPSQ YGHENIMREG SVILVTIGYR LGPLGFVSTG DADLSGNFGL
KDQRLALLWI KQNIASFGGE PENILVVGHS AGGASVHLQM LREDFSKVAK AAISFSGNAL
DPWVIQQGLR GRTFELGRIV GCGQASDSVT LKKCLKSKPA SEIVSAVQSF LVFSYVPFTP
FGPAIESPDA PEAFITQHPI DIIKSGKFAQ VPWAVTYTTE DGGYNAALLL EKQASSGREL
ILDLNDRWFD WAPYLLFYRD SMTTIKDMDD YSRKLRQEYL GDRRFSVESY WDVQRMFTDL
LFKNSVTVSV DLHRKYGKSP VYAFVYDNPA EVGVGQILSG RNDVYFGTVH GDDVFLIFNV
SFVPANRRPD EQIISRNFIK MLEYFALSTN DTMAYGDCVF QNNVGSKHMQ LLSITRDGCE
NKQLNCFIQR CLIFF