ESTJ_TRICA
ID ESTJ_TRICA Reviewed; 588 AA.
AC D6WMZ8; D7US45;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Juvenile hormone esterase {ECO:0000303|PubMed:20522120};
DE Short=JHE {ECO:0000303|PubMed:20522120};
DE EC=3.1.1.59 {ECO:0000269|PubMed:20522120};
DE Flags: Precursor;
GN Name=Tcjhe {ECO:0000303|PubMed:20522120};
GN ORFNames=TcasGA2_TC013193 {ECO:0000312|EMBL:EFA03259.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000312|EMBL:EFA03259.2};
RN [1] {ECO:0000312|EMBL:BAJ10675.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=20522120; DOI=10.1111/j.1365-2583.2010.01019.x;
RA Tsubota T., Minakuchi C., Nakakura T., Shinoda T., Shiotsuki T.;
RT "Molecular characterization of a gene encoding juvenile hormone esterase in
RT the red flour beetle, Tribolium castaneum.";
RL Insect Mol. Biol. 19:527-535(2010).
RN [2] {ECO:0000312|EMBL:EFA03259.2, ECO:0000312|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000312|EMBL:EFA03259.2,
RC ECO:0000312|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [3] {ECO:0000312|EMBL:EFA03259.2, ECO:0000312|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000312|EMBL:EFA03259.2,
RC ECO:0000312|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
CC -!- FUNCTION: May function as a juvenile hormone (JH)-specific degradation
CC enzyme in vivo decreasing JH activity. Hydrolyzes JH III in vitro.
CC Hydrolyzes effectively also methyl hepthylthioacetothioate (HEPTAT), a
CC synthetic substrate. Of the general esterase substrates, it has
CC preference for 2-naphthyl acetate (2-NA) and shows a weak activity for
CC 1-NA and 4-nitrophenylacetate (4-NPA). {ECO:0000269|PubMed:20522120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + juvenile hormone III = H(+) + juvenile hormone III
CC carboxylate + methanol; Xref=Rhea:RHEA:46912, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:27493,
CC ChEBI:CHEBI:83274; EC=3.1.1.59;
CC Evidence={ECO:0000269|PubMed:20522120};
CC -!- ACTIVITY REGULATION: Inhibited by 3-octylthio-1,1,1-trifluoro-2-
CC propanone (OTFP), a specific inhibitor of juvenile hormone esterase
CC (JHE), but not by diisopropyl fluorophosphate (DFP), a serine enzyme
CC inhibitor. {ECO:0000269|PubMed:20522120}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=657 nM for juvenile hormone (JH) III
CC {ECO:0000269|PubMed:20522120};
CC Note=kcat is 0.164 sec(-1) for JH III. {ECO:0000269|PubMed:20522120};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20522120}.
CC -!- DEVELOPMENTAL STAGE: Low expression in first to third larval instars,
CC but substantially higher expression levels detected at the beginning of
CC the sixth (penultimate) instars. Strongly expressed in seventh (final)
CC instar larvae. High levels of expression are detected on the final day
CC of pupal development in both males and females. On the seventh day of
CC adult life, the levels in females are greater than those in males by a
CC factor of more than three. {ECO:0000269|PubMed:20522120}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000255|RuleBase:RU361235}.
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DR EMBL; AB542179; BAJ10675.1; -; mRNA.
DR EMBL; AB542180; BAJ10676.1; -; mRNA.
DR EMBL; AB542181; BAJ10677.1; -; mRNA.
DR EMBL; AB542182; BAJ10678.1; -; mRNA.
DR EMBL; AB542183; BAJ10679.1; -; mRNA.
DR EMBL; KQ971343; EFA03259.2; -; Genomic_DNA.
DR RefSeq; NP_001180223.1; NM_001193294.1.
DR RefSeq; XP_015835613.1; XM_015980127.1.
DR RefSeq; XP_015835614.1; XM_015980128.1.
DR RefSeq; XP_015835615.1; XM_015980129.1.
DR RefSeq; XP_015835616.1; XM_015980130.1.
DR AlphaFoldDB; D6WMZ8; -.
DR SMR; D6WMZ8; -.
DR ESTHER; trica-d7us45; Juvenile_hormone_esterase.
DR EnsemblMetazoa; TC013193_001; TC013193_001; TC013193.
DR GeneID; 658208; -.
DR KEGG; tca:658208; -.
DR CTD; 658208; -.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_006586_13_2_1; -.
DR InParanoid; D6WMZ8; -.
DR OrthoDB; 754103at2759; -.
DR BRENDA; 3.1.1.59; 6437.
DR Proteomes; UP000007266; Linkage group 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004453; F:juvenile-hormone 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Serine esterase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..588
FT /note="Juvenile hormone esterase"
FT /evidence="ECO:0000255"
FT /id="PRO_5007230847"
FT ACT_SITE 214
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 479
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 91..109
FT /evidence="ECO:0000250|UniProtKB:P12337"
FT DISULFID 268..281
FT /evidence="ECO:0000250|UniProtKB:P12337"
FT CONFLICT 6
FT /note="N -> T (in Ref. 1; BAJ10675/BAJ10676/BAJ10677/
FT BAJ10678/BAJ10679)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="I -> N (in Ref. 1; BAJ10675/BAJ10676/BAJ10677/
FT BAJ10678/BAJ10679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 65853 MW; 95B3C92C23C41AFE CRC64;
MKFPKNLFLV LFYTSWKFCD VCAYTPSHPL VYTKYGSVIG SVEYSRNSRA YMSFKGIPFA
KPPVGDLRFK APEPPEPWNF SINGTKDAPF CIQKNYFFSN PKVEGSEDCL YLNVYVPKTE
GSQLLPVMVF IHWGGFFAGR GSSDYIGPEY IMDKDVILVT FNYRLGVFGF LSTLDDNAPG
NFGLKDQVMA LKFVHENIEC FGGDNNRVTI FGQSAGSGSV NLHLISPASR GLFQQAISQS
GAALDLWARP LNALQPNVTA ALAAFTGCSA HIGSSKDIVD CLRKIEATKL AETADNFKYF
SIEPLTPYSM VTEKQTDANP NPFLVQDPLE SLKAGAFMKI PWMVGSVQDE GILRAAPLIR
QPETLQTLNS NFEKLITQML FLQFSAGANA SSLLKNMTDF YLGGKSLIDV NNPKSVQGFI
NLYGDRAFHY GIYQTVILQL RKGHKPIWMY NFNYKGQYSY GDKFAATDKN VNFTWGVSHC
DDLLYLFKSP GLFANLQKDN DILMSKTMVS FWTNFAIYGN PDPHQNLNWN SLNFEKPEGV
KVADLNIMHI TGNHETGKIA FDVEKSQILD RIAFWAKQSL LENFPDFG
