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 02-OCT-2024, entry version 158. 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}. 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; 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; 27. DR DIP; DIP-23202N; -. DR IntAct; Q9W2M2; 6. DR STRING; 7227.FBpp0071468; -. DR CAZy; GH37; Glycoside Hydrolase Family 37. DR GlyCosmos; Q9W2M2; 5 sites, No reported glycans. DR iPTMnet; Q9W2M2; -. DR PaxDb; 7227-FBpp0071468; -. 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 AGR; FB:FBgn0003748; -. DR CTD; 11181; -. DR FlyBase; FBgn0003748; Treh. DR VEuPathDB; VectorBase:FBgn0003748; -. DR eggNOG; KOG0602; Eukaryota. DR GeneTree; ENSGT00390000006949; -. DR InParanoid; Q9W2M2; -. DR OMA; NRYWDAS; -. DR OrthoDB; 1329212at2759; -. 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 cell types or tissues. DR ExpressionAtlas; Q9W2M2; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:FlyBase. DR GO; GO:0005615; C:extracellular space; 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 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; TREHALASE; 1. DR PANTHER; PTHR23403:SF1; TREHALASE; 1. DR Pfam; PF01204; Trehalase; 1. DR PRINTS; PR00744; GLHYDRLASE37. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 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 //