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Q9JLT2 (TREA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trehalase
EC=3.2.1.28
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene names
Name:Treh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

Alpha,alpha-trehalose + H2O = 2 D-glucose.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 37 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtrehalose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

brush border

Traceable author statement. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha,alpha-trehalase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 553533Trehalase
PRO_0000012053
Propeptide554 – 57623Removed in mature form Potential
PRO_0000012054

Amino acid modifications

Lipidation5531GPI-anchor amidated serine Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict821Q → R in AAK97631. Ref.3
Sequence conflict4161S → T in AAK97631. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9JLT2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 53CDA6A10511520E

FASTA57665,401
        10         20         30         40         50         60 
MTWELHLLLL LGLGLRSQEA LPPPCESQIY CHGELLHQVQ MAQLYQDDKQ FVDMSLATSP 

        70         80         90        100        110        120 
DEVLQKFSEL ATVHNHSIPK EQLQEFVQSH FQPVGQELQS WTPEDWKDSP QFLQKISDAN 

       130        140        150        160        170        180 
LRVWAEELHK IWKKLGKKMK AEVLSYPERS SLIYSKHPFI VPGGRFVEFY YWDSYWVMEG 

       190        200        210        220        230        240 
LLLSEMASTV KGMLQNFLDL VKTYGHIPNG GRIYYLQRSQ PPLLTLMMDR YVAHTKDVAF 

       250        260        270        280        290        300 
LQENIGTLAS ELDFWTVNRT VSVVSGGQSY VLNRYYVPYG GPRPESYRKD AELANSVPEG 

       310        320        330        340        350        360 
DRETLWAELK AGAESGWDFS SRWLVGGPDP DLLSSIRTSK MVPADLNAFL CQAEELMSNF 

       370        380        390        400        410        420 
YSRLGNDTEA TKYRNLRAQR LAAMEAVLWD EQKGAWFDYD LEKGKKNLEF YPSNLSPLWA 

       430        440        450        460        470        480 
GCFSDPSVAD KALKYLEDSK ILTYQYGIPT SLRNTGQQWD FPNAWAPLQD LVIRGLAKSA 

       490        500        510        520        530        540 
SPRTQEVAFQ LAQNWIKTNF KVYSQKSAMF EKYDISNGGH PGGGGEYEVQ EGFGWTNGLA 

       550        560        570 
LMLLDRYGDQ LTSGTQLASL GPHCLVAALL LSLLLQ

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 16141072] [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: 11404018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-576.
Strain: 129/SvJ.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF136944 mRNA. Translation: AAF61430.1.
AK008912 mRNA. Translation: BAB25963.1.
AF404760 Genomic DNA. Translation: AAK97631.1.
IPIIPI00124697.
RefSeqNP_067456.1. NM_021481.2.
UniGeneMm.45380.

3D structure databases

ProteinModelPortalQ9JLT2.
SMRQ9JLT2. Positions 26-560.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JLT2.

Protein family/group databases

CAZyGH37. Glycoside Hydrolase Family 37.

Proteomic databases

PRIDEQ9JLT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034609; ENSMUSP00000034609; ENSMUSG00000032098.
GeneID58866.
KEGGmmu:58866.
UCSCuc009pec.1. mouse.

Organism-specific databases

CTD11181.
MGIMGI:1926230. Treh.

Phylogenomic databases

GeneTreeENSGT00390000006949.
HOGENOMHBG485982.
HOVERGENHBG014956.
InParanoidQ9JLT2.
OMANRYWDAS.
OrthoDBEOG4R23TH.
PhylomeDBQ9JLT2.

Gene expression databases

ArrayExpressQ9JLT2.
BgeeQ9JLT2.
CleanExMM_TREH.
GenevestigatorQ9JLT2.
GermOnlineENSMUSG00000032098. Mus musculus.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
KOK01194.
PANTHERPTHR23403. Glyco_hydro_37. 1 hit.
PfamPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSPR00744. GLHYDRLASE37.
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314428.
SOURCESearch...

Entry information

Entry nameTREA_MOUSE
AccessionPrimary (citable) accession number: Q9JLT2
Secondary accession number(s): Q91ZS4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents