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Q9W2M2 (TREA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
ORF Names:CG9364
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 37 family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtrehalose metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionalpha,alpha-trehalase activity

Traceable author statement PubMed 1582561. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: Q9W2M2-1)

Also known as: F;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform A (identifier: Q9W2M2-2)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MFKLPTISLLLVSWSCLVALSQAKTYSLPDLTTDYNNAIPVDEEEAQDPFASC → MASPANPSSNHKMNGNG
Note: No experimental confirmation available.
Isoform B (identifier: Q9W2M2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 596573Trehalase
PRO_0000012058

Regions

Region200 – 2012Substrate binding By similarity
Region246 – 2483Substrate binding By similarity
Region307 – 3093Substrate binding By similarity

Sites

Active site3431Proton donor/acceptor By similarity
Active site5411Proton donor/acceptor By similarity
Binding site1931Substrate By similarity
Binding site2371Substrate By similarity
Binding site3411Substrate; via carbonyl oxygen By similarity
Binding site5561Substrate By similarity

Amino acid modifications

Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Ref.4
Glycosylation5161N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 8181Missing in isoform B.
VSP_021831
Alternative sequence1 – 5353MFKLP…PFASC → MASPANPSSNHKMNGNG in isoform A.
VSP_007735

Sequences

Sequence LengthMass (Da)Tools
Isoform C (F) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 600D03B2087929EC

FASTA59667,689
        10         20         30         40         50         60 
MFKLPTISLL LVSWSCLVAL SQAKTYSLPD LTTDYNNAIP VDEEEAQDPF ASCKIYCEGN 

        70         80         90        100        110        120 
LLHTIQTAVP KLFADSKTFV DMKLNNSPDK TLEDFNAMME AKNQTPSSED LKQFVDKYFS 

       130        140        150        160        170        180 
APGTELEKWT PTDWKENPSF LDLISDPDLK QWGVELNSIW KDLGRKMKDE VSKNPEYYSI 

       190        200        210        220        230        240 
IPVPNPVIVP GGRFIEFYYW DSYWIIRGLL YSQMFDTARG MIENFFSIVN RFGFIPNGGR 

       250        260        270        280        290        300 
VYYHGRSQPP LLTGMVKSYV DFTNDDKFAI DALDTLEHEF EFFVNNHNVT VKNHSLCVYR 

       310        320        330        340        350        360 
DSSSGPRPES YREDVETGEE FPTDEAKELH YSELKAGAES GMDFSSRWFI SPTGTNDGNR 

       370        380        390        400        410        420 
SALSTTSIVP VDLNAYLYWN AKLIAEFHSK AGNTKKVTEY ETKAEKLLLG IQEVLWNEEA 

       430        440        450        460        470        480 
GVWLDYDMIN QKPRDYYTPT NLSPLWVKAF NISESEKISA SVMAYIERNK LDSFPGGVPN 

       490        500        510        520        530        540 
TLSYTGEQWD APNVWAPMQY ILVEGLNNLN TPEAKNMSLK WATRWVKTNF AAFSKDRHMY 

       550        560        570        580        590 
EKYNADEFGV GGGGGEYEVQ TGFGWSNGVI IEWLSKHGRD ISIGSGCGCL AGEKRQ

« Hide

Isoform A (D) [UniParc].

Checksum: AB9992F3BB522733
Show »

FASTA56063,552
Isoform B [UniParc].

Checksum: 1580AADE103A1E25
Show »

FASTA51558,722

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[4]"Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-451, MASS SPECTROMETRY.
Strain: Oregon-R.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAF46668.1.
AE013599 Genomic DNA. Translation: AAF46669.1.
AE013599 Genomic DNA. Translation: AAM68192.1.
AY051466 mRNA. Translation: AAK92890.1.
RefSeqNP_001261115.1. NM_001274186.1.
NP_524821.1. NM_080082.3.
NP_726023.1. NM_166421.2.
NP_726024.1. NM_166422.2.
NP_726025.1. NM_166423.3.
NP_726026.1. NM_166424.2.
NP_726027.1. NM_166425.2.
UniGeneDm.6686.

3D structure databases

ProteinModelPortalQ9W2M2.
SMRQ9W2M2. Positions 59-574.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-23202N.
IntActQ9W2M2. 6 interactions.
MINTMINT-994217.

Protein family/group databases

CAZyGH37. Glycoside Hydrolase Family 37.

Proteomic databases

PaxDbQ9W2M2.
PRIDEQ9W2M2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071539; FBpp0071468; FBgn0003748.
FBtr0071540; FBpp0071469; FBgn0003748.
GeneID45368.
KEGGdme:Dmel_CG9364.
UCSCCG9364-RA. d. melanogaster.

Organism-specific databases

CTD11181.
FlyBaseFBgn0003748. Treh.

Phylogenomic databases

eggNOGCOG1626.
GeneTreeENSGT00390000006949.
InParanoidQ9W2M2.
KOK01194.
OMANRYWDAS.
OrthoDBEOG4MGQPK.
PhylomeDBQ9W2M2.

Gene expression databases

BgeeQ9W2M2.
GermOnlineCG9364. Drosophila melanogaster.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERPTHR23403. PTHR23403. 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

GenomeRNAi45368.
NextBio838071.

Entry information

Entry nameTREA_DROME
AccessionPrimary (citable) accession number: Q9W2M2
Secondary accession number(s): Q0E903 expand/collapse secondary AC list , Q0E904, Q7YWL2, Q961P0, Q9W2M1, Q9W2M3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: May 1, 2000
Last modified: May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

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