TREA_DROME
ID TREA_DROME Reviewed; 596 AA.
AC Q9W2M2; Q0E903; Q0E904; Q7YWL2; Q961P0; Q9W2M1; Q9W2M3;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Trehalase {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000250|UniProtKB:O43280};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=Treh; ORFNames=CG9364;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-451, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:O43280};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C; Synonyms=F;
CC IsoId=Q9W2M2-1; Sequence=Displayed;
CC Name=A; Synonyms=D;
CC IsoId=Q9W2M2-2; Sequence=VSP_007735;
CC Name=B;
CC IsoId=Q9W2M2-3; Sequence=VSP_021831;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF46668.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46669.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68192.1; -; Genomic_DNA.
DR EMBL; AY051466; AAK92890.1; -; mRNA.
DR RefSeq; NP_001261115.1; NM_001274186.1. [Q9W2M2-2]
DR RefSeq; NP_524821.1; NM_080082.3. [Q9W2M2-2]
DR RefSeq; NP_726023.1; NM_166421.2. [Q9W2M2-2]
DR RefSeq; NP_726024.1; NM_166422.2. [Q9W2M2-2]
DR RefSeq; NP_726025.1; NM_166423.3. [Q9W2M2-1]
DR RefSeq; NP_726026.1; NM_166424.2. [Q9W2M2-1]
DR RefSeq; NP_726027.1; NM_166425.2. [Q9W2M2-3]
DR AlphaFoldDB; Q9W2M2; -.
DR SMR; Q9W2M2; -.
DR BioGRID; 69627; 26.
DR DIP; DIP-23202N; -.
DR IntAct; Q9W2M2; 6.
DR STRING; 7227.FBpp0071468; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GlyGen; Q9W2M2; 5 sites.
DR iPTMnet; Q9W2M2; -.
DR PaxDb; Q9W2M2; -.
DR PRIDE; Q9W2M2; -.
DR DNASU; 45368; -.
DR EnsemblMetazoa; FBtr0071535; FBpp0071464; FBgn0003748. [Q9W2M2-2]
DR EnsemblMetazoa; FBtr0071536; FBpp0071465; FBgn0003748. [Q9W2M2-2]
DR EnsemblMetazoa; FBtr0071537; FBpp0071466; FBgn0003748. [Q9W2M2-2]
DR EnsemblMetazoa; FBtr0071538; FBpp0071467; FBgn0003748. [Q9W2M2-3]
DR EnsemblMetazoa; FBtr0071539; FBpp0071468; FBgn0003748. [Q9W2M2-1]
DR EnsemblMetazoa; FBtr0071540; FBpp0071469; FBgn0003748. [Q9W2M2-1]
DR EnsemblMetazoa; FBtr0332423; FBpp0304696; FBgn0003748. [Q9W2M2-2]
DR GeneID; 45368; -.
DR KEGG; dme:Dmel_CG9364; -.
DR UCSC; CG9364-RA; d. melanogaster. [Q9W2M2-1]
DR CTD; 11181; -.
DR FlyBase; FBgn0003748; Treh.
DR VEuPathDB; VectorBase:FBgn0003748; -.
DR eggNOG; KOG0602; Eukaryota.
DR GeneTree; ENSGT00390000006949; -.
DR InParanoid; Q9W2M2; -.
DR OMA; TNGVLIW; -.
DR PhylomeDB; Q9W2M2; -.
DR BRENDA; 3.2.1.28; 1994.
DR BioGRID-ORCS; 45368; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 45368; -.
DR PRO; PR:Q9W2M2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003748; Expressed in oviduct (Drosophila) and 47 other tissues.
DR ExpressionAtlas; Q9W2M2; baseline and differential.
DR Genevisible; Q9W2M2; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:FlyBase.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0005993; P:trehalose catabolic process; IMP:FlyBase.
DR GO; GO:0005991; P:trehalose metabolic process; IMP:FlyBase.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..596
FT /note="Trehalase"
FT /id="PRO_0000012058"
FT REGION 303..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 343
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 541
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 246..248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 307..309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 556
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_021831"
FT VAR_SEQ 1..53
FT /note="MFKLPTISLLLVSWSCLVALSQAKTYSLPDLTTDYNNAIPVDEEEAQDPFAS
FT C -> MASPANPSSNHKMNGNG (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007735"
SQ SEQUENCE 596 AA; 67689 MW; 600D03B2087929EC CRC64;
MFKLPTISLL LVSWSCLVAL SQAKTYSLPD LTTDYNNAIP VDEEEAQDPF ASCKIYCEGN
LLHTIQTAVP KLFADSKTFV DMKLNNSPDK TLEDFNAMME AKNQTPSSED LKQFVDKYFS
APGTELEKWT PTDWKENPSF LDLISDPDLK QWGVELNSIW KDLGRKMKDE VSKNPEYYSI
IPVPNPVIVP GGRFIEFYYW DSYWIIRGLL YSQMFDTARG MIENFFSIVN RFGFIPNGGR
VYYHGRSQPP LLTGMVKSYV DFTNDDKFAI DALDTLEHEF EFFVNNHNVT VKNHSLCVYR
DSSSGPRPES YREDVETGEE FPTDEAKELH YSELKAGAES GMDFSSRWFI SPTGTNDGNR
SALSTTSIVP VDLNAYLYWN AKLIAEFHSK AGNTKKVTEY ETKAEKLLLG IQEVLWNEEA
GVWLDYDMIN QKPRDYYTPT NLSPLWVKAF NISESEKISA SVMAYIERNK LDSFPGGVPN
TLSYTGEQWD APNVWAPMQY ILVEGLNNLN TPEAKNMSLK WATRWVKTNF AAFSKDRHMY
EKYNADEFGV GGGGGEYEVQ TGFGWSNGVI IEWLSKHGRD ISIGSGCGCL AGEKRQ
