TRE1_ARATH
ID TRE1_ARATH Reviewed; 626 AA.
AC Q9SU50; O22986;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Trehalase;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE AltName: Full=Trehalase 1;
DE Short=AtTRE1;
GN Name=TRE1; OrderedLocusNames=At4g24040; ORFNames=T19F6.15, T19F6.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11161063; DOI=10.1104/pp.125.2.1086;
RA Mueller J., Aeschbacher R.A., Wingler A., Boller T., Wiemken A.;
RT "Trehalose and trehalase in Arabidopsis.";
RL Plant Physiol. 125:1086-1093(2001).
RN [6]
RP INDUCTION.
RX PubMed=15181209; DOI=10.1104/pp.104.039503;
RA Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M.,
RA Smeekens S.C.M.;
RT "Trehalose mediated growth inhibition of Arabidopsis seedlings is due to
RT trehalose-6-phosphate accumulation.";
RL Plant Physiol. 135:879-890(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15181208; DOI=10.1104/pp.104.039743;
RA van Dijken A.J.H., Schluepmann H., Smeekens S.C.M.;
RT "Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal
RT vegetative growth and transition to flowering.";
RL Plant Physiol. 135:969-977(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17673210; DOI=10.1016/j.febslet.2007.07.036;
RA Frison M., Parrou J.L., Guillaumot D., Masquelier D., Francois J.,
RA Chaumont F., Batoko H.;
RT "The Arabidopsis thaliana trehalase is a plasma membrane-bound enzyme with
RT extracellular activity.";
RL FEBS Lett. 581:4010-4016(2007).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=21394451; DOI=10.1007/s00216-011-4837-2;
RA Delatte T.L., Schluepmann H., Smeekens S.C., de Jong G.J., Somsen G.W.;
RT "Capillary electrophoresis-mass spectrometry analysis of trehalose-6-
RT phosphate in Arabidopsis thaliana seedlings.";
RL Anal. Bioanal. Chem. 400:1137-1144(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21426427; DOI=10.1111/j.1365-313x.2011.04583.x;
RA Singh V., Louis J., Ayre B.G., Reese J.C., Pegadaraju V., Shah J.;
RT "TREHALOSE PHOSPHATE SYNTHASE11-dependent trehalose metabolism promotes
RT Arabidopsis thaliana defense against the phloem-feeding insect Myzus
RT persicae.";
RL Plant J. 67:94-104(2011).
CC -!- FUNCTION: Involved in the regulation of trehalose content by
CC hydrolyzing trehalose to glucose. {ECO:0000269|PubMed:11161063,
CC ECO:0000269|PubMed:17673210, ECO:0000269|PubMed:21426427}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17673210};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17673210}. Note=Has
CC extracellular activity when expressed in yeast.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed at low
CC levels in leaves and stems. {ECO:0000269|PubMed:11161063,
CC ECO:0000269|PubMed:15181208}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants accumulate high levels of trehalose and starch.
CC {ECO:0000269|PubMed:21394451, ECO:0000269|PubMed:21426427}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63620.1; Type=Erroneous gene model prediction; Evidence={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; AC002343; AAB63620.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109619; CAB51647.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81322.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84844.1; -; Genomic_DNA.
DR EMBL; AK118407; BAC43016.1; -; mRNA.
DR EMBL; BT010732; AAR23702.1; -; mRNA.
DR PIR; T13444; T13444.
DR RefSeq; NP_194135.1; NM_118536.4.
DR PDB; 7E9U; X-ray; 2.10 A; A/B=63-626.
DR PDB; 7E9X; X-ray; 1.88 A; A/B/C/D=63-626.
DR PDB; 7EAW; X-ray; 1.80 A; A/B=63-626.
DR PDBsum; 7E9U; -.
DR PDBsum; 7E9X; -.
DR PDBsum; 7EAW; -.
DR AlphaFoldDB; Q9SU50; -.
DR SMR; Q9SU50; -.
DR STRING; 3702.AT4G24040.1; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR PaxDb; Q9SU50; -.
DR PRIDE; Q9SU50; -.
DR ProteomicsDB; 228389; -.
DR EnsemblPlants; AT4G24040.1; AT4G24040.1; AT4G24040.
DR GeneID; 828504; -.
DR Gramene; AT4G24040.1; AT4G24040.1; AT4G24040.
DR KEGG; ath:AT4G24040; -.
DR Araport; AT4G24040; -.
DR TAIR; locus:2134961; AT4G24040.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_4_2_1; -.
DR InParanoid; Q9SU50; -.
DR OMA; TNGVLIW; -.
DR OrthoDB; 417479at2759; -.
DR PhylomeDB; Q9SU50; -.
DR BRENDA; 3.2.1.28; 399.
DR PRO; PR:Q9SU50; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU50; baseline and differential.
DR Genevisible; Q9SU50; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:TAIR.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:TAIR.
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; PS00213; LIPOCALIN; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..626
FT /note="Trehalase"
FT /id="PRO_0000417663"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 380
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 580
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231..232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277..279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344..346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 71355 MW; A23D8E2C9C2D048F CRC64;
MKSYKLNNPN LLISTHTHNK LFLSSSPFNL LFSFPSFIYL KQQRSLFFFF FFFLCFSFTT
SMLDSDTDTD SGPVVATTKL VTFLQRVQHT ALRSYPKKQT PDPKSYIDLS LKRPYSLSTI
ESAFDDLTSE SHDQPVPVET LEKFVKEYFD GAGEDLLHHE PVDFVSDPSG FLSNVENEEV
REWAREVHGL WRNLSCRVSD SVRESADRHT LLPLPEPVII PGSRFREVYY WDSYWVIKGL
MTSQMFTTAK GLVTNLMSLV ETYGYALNGA RAYYTNRSQP PLLSSMVYEI YNVTKDEELV
RKAIPLLLKE YEFWNSGKHK VVIRDANGYD HVLSRYYAMW NKPRPESSVF DEESASGFST
MLEKQRFHRD IATAAESGCD FSTRWMRDPP NFTTMATTSV VPVDLNVFLL KMELDIAFMM
KVSGDQNGSD RFVKASKARE KAFQTVFWNE KAGQWLDYWL SSSGEESETW KAENQNTNVF
ASNFAPIWIN SINSDENLVK KVVTALKNSG LIAPAGILTS LTNSGQQWDS PNGWAPQQEM
IVTGLGRSSV KEAKEMAEDI ARRWIKSNYL VYKKSGTIHE KLKVTELGEY GGGGEYMPQT
GFGWSNGVIL AFLEEYGWPS HLSIEA
