TREA_MOUSE
ID TREA_MOUSE Reviewed; 576 AA.
AC Q9JLT2; Q91ZS4;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Trehalase {ECO:0000303|PubMed:11404018};
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 {ECO:0000312|MGI:MGI:1926230};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ddY; TISSUE=Intestinal mucosa;
RA Ohta T., Kudo N., Ariyasu H., Yanai Y., Takeuchi M., Ikegami H.,
RA Kurimoto M.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-576.
RC STRAIN=129/SvJ;
RX PubMed=11404018; DOI=10.1016/s0378-1119(01)00474-7;
RA Oesterreicher T.J., Markesich D.C., Henning S.J.;
RT "Cloning, characterization and mapping of the mouse trehalase (Treh)
RT gene.";
RL Gene 270:211-220(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Intestinal trehalase is probably involved in the hydrolysis
CC of ingested trehalose. {ECO:0000250|UniProtKB:O43280}.
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P19813}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19813};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19813}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AF136944; AAF61430.1; -; mRNA.
DR EMBL; AK008912; BAB25963.1; -; mRNA.
DR EMBL; AF404760; AAK97631.1; -; Genomic_DNA.
DR CCDS; CCDS23117.1; -.
DR RefSeq; NP_067456.1; NM_021481.3.
DR AlphaFoldDB; Q9JLT2; -.
DR SMR; Q9JLT2; -.
DR STRING; 10090.ENSMUSP00000034609; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GlyGen; Q9JLT2; 3 sites.
DR iPTMnet; Q9JLT2; -.
DR PhosphoSitePlus; Q9JLT2; -.
DR jPOST; Q9JLT2; -.
DR MaxQB; Q9JLT2; -.
DR PaxDb; Q9JLT2; -.
DR PeptideAtlas; Q9JLT2; -.
DR PRIDE; Q9JLT2; -.
DR ProteomicsDB; 259310; -.
DR Antibodypedia; 48758; 123 antibodies from 20 providers.
DR DNASU; 58866; -.
DR Ensembl; ENSMUST00000034609; ENSMUSP00000034609; ENSMUSG00000032098.
DR GeneID; 58866; -.
DR KEGG; mmu:58866; -.
DR UCSC; uc009pec.2; mouse.
DR CTD; 11181; -.
DR MGI; MGI:1926230; Treh.
DR VEuPathDB; HostDB:ENSMUSG00000032098; -.
DR eggNOG; KOG0602; Eukaryota.
DR GeneTree; ENSGT00390000006949; -.
DR HOGENOM; CLU_006451_4_3_1; -.
DR InParanoid; Q9JLT2; -.
DR OMA; TNGVLIW; -.
DR OrthoDB; 417479at2759; -.
DR PhylomeDB; Q9JLT2; -.
DR TreeFam; TF314239; -.
DR BRENDA; 3.2.1.28; 3474.
DR BioGRID-ORCS; 58866; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9JLT2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JLT2; protein.
DR Bgee; ENSMUSG00000032098; Expressed in small intestine Peyer's patch and 31 other tissues.
DR ExpressionAtlas; Q9JLT2; baseline and differential.
DR Genevisible; Q9JLT2; MM.
DR GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:MGI.
DR GO; GO:0005993; P:trehalose catabolic process; ISS:UniProtKB.
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 Cell membrane; Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..553
FT /note="Trehalase"
FT /id="PRO_0000012053"
FT PROPEP 554..576
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012054"
FT ACT_SITE 318
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 511
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 172..173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 283..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT LIPID 553
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 82
FT /note="Q -> R (in Ref. 3; AAK97631)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="S -> T (in Ref. 3; AAK97631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 65401 MW; 53CDA6A10511520E CRC64;
MTWELHLLLL LGLGLRSQEA LPPPCESQIY CHGELLHQVQ MAQLYQDDKQ FVDMSLATSP
DEVLQKFSEL ATVHNHSIPK EQLQEFVQSH FQPVGQELQS WTPEDWKDSP QFLQKISDAN
LRVWAEELHK IWKKLGKKMK AEVLSYPERS SLIYSKHPFI VPGGRFVEFY YWDSYWVMEG
LLLSEMASTV KGMLQNFLDL VKTYGHIPNG GRIYYLQRSQ PPLLTLMMDR YVAHTKDVAF
LQENIGTLAS ELDFWTVNRT VSVVSGGQSY VLNRYYVPYG GPRPESYRKD AELANSVPEG
DRETLWAELK AGAESGWDFS SRWLVGGPDP DLLSSIRTSK MVPADLNAFL CQAEELMSNF
YSRLGNDTEA TKYRNLRAQR LAAMEAVLWD EQKGAWFDYD LEKGKKNLEF YPSNLSPLWA
GCFSDPSVAD KALKYLEDSK ILTYQYGIPT SLRNTGQQWD FPNAWAPLQD LVIRGLAKSA
SPRTQEVAFQ LAQNWIKTNF KVYSQKSAMF EKYDISNGGH PGGGGEYEVQ EGFGWTNGLA
LMLLDRYGDQ LTSGTQLASL GPHCLVAALL LSLLLQ
