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Protein

Trehalase

Gene

Treh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei165 – 1651SubstrateBy similarity
Binding sitei209 – 2091SubstrateBy similarity
Binding sitei316 – 3161Substrate; via carbonyl oxygenBy similarity
Active sitei318 – 3181Proton donor/acceptorBy similarity
Active sitei511 – 5111Proton donor/acceptorBy similarity
Binding sitei526 – 5261SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalase (EC:3.2.1.28)
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene namesi
Name:Treh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1926230. Treh.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • brush border Source: MGI
  • extracellular exosome Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 553533TrehalasePRO_0000012053Add
BLAST
Propeptidei554 – 57623Removed in mature formSequence analysisPRO_0000012054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence analysis
Lipidationi553 – 5531GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ9JLT2.
PaxDbiQ9JLT2.
PRIDEiQ9JLT2.

PTM databases

iPTMnetiQ9JLT2.
PhosphoSiteiQ9JLT2.

Expressioni

Gene expression databases

BgeeiQ9JLT2.
CleanExiMM_TREH.
ExpressionAtlasiQ9JLT2. baseline and differential.
GenevisibleiQ9JLT2. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034609.

Structurei

3D structure databases

ProteinModelPortaliQ9JLT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1732Substrate bindingBy similarity
Regioni218 – 2203Substrate bindingBy similarity
Regioni283 – 2853Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0602. Eukaryota.
COG1626. LUCA.
GeneTreeiENSGT00390000006949.
HOGENOMiHOG000215465.
HOVERGENiHBG014956.
InParanoidiQ9JLT2.
KOiK01194.
OMAiWAGQLHQ.
OrthoDBiEOG7P02H6.
PhylomeDBiQ9JLT2.
TreeFamiTF314239.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JLT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTWELHLLLL LGLGLRSQEA LPPPCESQIY CHGELLHQVQ MAQLYQDDKQ
60 70 80 90 100
FVDMSLATSP DEVLQKFSEL ATVHNHSIPK EQLQEFVQSH FQPVGQELQS
110 120 130 140 150
WTPEDWKDSP QFLQKISDAN LRVWAEELHK IWKKLGKKMK AEVLSYPERS
160 170 180 190 200
SLIYSKHPFI VPGGRFVEFY YWDSYWVMEG LLLSEMASTV KGMLQNFLDL
210 220 230 240 250
VKTYGHIPNG GRIYYLQRSQ PPLLTLMMDR YVAHTKDVAF LQENIGTLAS
260 270 280 290 300
ELDFWTVNRT VSVVSGGQSY VLNRYYVPYG GPRPESYRKD AELANSVPEG
310 320 330 340 350
DRETLWAELK AGAESGWDFS SRWLVGGPDP DLLSSIRTSK MVPADLNAFL
360 370 380 390 400
CQAEELMSNF YSRLGNDTEA TKYRNLRAQR LAAMEAVLWD EQKGAWFDYD
410 420 430 440 450
LEKGKKNLEF YPSNLSPLWA GCFSDPSVAD KALKYLEDSK ILTYQYGIPT
460 470 480 490 500
SLRNTGQQWD FPNAWAPLQD LVIRGLAKSA SPRTQEVAFQ LAQNWIKTNF
510 520 530 540 550
KVYSQKSAMF EKYDISNGGH PGGGGEYEVQ EGFGWTNGLA LMLLDRYGDQ
560 570
LTSGTQLASL GPHCLVAALL LSLLLQ
Length:576
Mass (Da):65,401
Last modified:October 1, 2000 - v1
Checksum:i53CDA6A10511520E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821Q → R in AAK97631 (PubMed:11404018).Curated
Sequence conflicti416 – 4161S → T in AAK97631 (PubMed:11404018).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136944 mRNA. Translation: AAF61430.1.
AK008912 mRNA. Translation: BAB25963.1.
AF404760 Genomic DNA. Translation: AAK97631.1.
CCDSiCCDS23117.1.
RefSeqiNP_067456.1. NM_021481.3.
UniGeneiMm.45380.

Genome annotation databases

EnsembliENSMUST00000034609; ENSMUSP00000034609; ENSMUSG00000032098.
GeneIDi58866.
KEGGimmu:58866.
UCSCiuc009pec.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136944 mRNA. Translation: AAF61430.1.
AK008912 mRNA. Translation: BAB25963.1.
AF404760 Genomic DNA. Translation: AAK97631.1.
CCDSiCCDS23117.1.
RefSeqiNP_067456.1. NM_021481.3.
UniGeneiMm.45380.

3D structure databases

ProteinModelPortaliQ9JLT2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034609.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

PTM databases

iPTMnetiQ9JLT2.
PhosphoSiteiQ9JLT2.

Proteomic databases

MaxQBiQ9JLT2.
PaxDbiQ9JLT2.
PRIDEiQ9JLT2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034609; ENSMUSP00000034609; ENSMUSG00000032098.
GeneIDi58866.
KEGGimmu:58866.
UCSCiuc009pec.2. mouse.

Organism-specific databases

CTDi11181.
MGIiMGI:1926230. Treh.

Phylogenomic databases

eggNOGiKOG0602. Eukaryota.
COG1626. LUCA.
GeneTreeiENSGT00390000006949.
HOGENOMiHOG000215465.
HOVERGENiHBG014956.
InParanoidiQ9JLT2.
KOiK01194.
OMAiWAGQLHQ.
OrthoDBiEOG7P02H6.
PhylomeDBiQ9JLT2.
TreeFamiTF314239.

Miscellaneous databases

PROiQ9JLT2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLT2.
CleanExiMM_TREH.
ExpressionAtlasiQ9JLT2. baseline and differential.
GenevisibleiQ9JLT2. MM.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Ohta T., Kudo N., Ariyasu H., Yanai Y., Takeuchi M., Ikegami H., Kurimoto M.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ddY.
    Tissue: Intestinal mucosa.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Stomach.
  3. "Cloning, characterization and mapping of the mouse trehalase (Treh) gene."
    Oesterreicher T.J., Markesich D.C., Henning S.J.
    Gene 270:211-220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-576.
    Strain: 129/SvJ.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiTREA_MOUSE
AccessioniPrimary (citable) accession number: Q9JLT2
Secondary accession number(s): Q91ZS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.