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P07191 (MAL2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maltase A2

EC=3.2.1.20
Alternative name(s):
Larval visceral protein D
Gene names
Name:Mal-A2
Synonyms:LvpD
ORF Names:CG8694
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Developmental stage

One of the proteins expressed by the 44D cuticle gene cluster. Expressed in first, second and early 3rd instar larvae and in adults, but not in embryos or pupae. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence caution

The sequence CAA23492.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncation binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 567544Maltase A2
PRO_0000001446

Sites

Active site2261Nucleophile By similarity
Active site2981Proton donor By similarity
Site3641Transition state stabilizer By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict5271P → T in CAA23492. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07191 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 51242BA9F185213D

FASTA56764,542
        10         20         30         40         50         60 
MPKWAHLGLA ALLLISTTQE GTADIDWWEN ASLYQIYPRS FQDSDGDGIG DLKGITSRLG 

        70         80         90        100        110        120 
YLKEIGITAT WLSPIFTSPM SDFGYDISNF YDIDPIFGTL EDFDDLIVEA KSLGVKIILD 

       130        140        150        160        170        180 
FVPNHSSDEN VWFEKSVNRE DGYDDFYVWD DGKLNEETGA RDPPSNWVSV FSGPMWTWNE 

       190        200        210        220        230        240 
KRQQYFLHQF QVKQPDLNFT NPMVREHMLD VLKFWLDRGV DGFRIDAVPH IYEHRNADGS 

       250        260        270        280        290        300 
YPDEPVSGWG SDPNAYDYHD HIYTKDQPAT VDLMYEWREF LDNYRAQNGG DSRVLLAEAY 

       310        320        330        340        350        360 
SSVETLSAYF GNSTHQGTQL PMNFQLMYLS GYSTAKDVVG SIDYWMNTMW KEHQTANWVV 

       370        380        390        400        410        420 
GNHDTNRVAD RMGAHKVDLL NVIVNALPGA SVTYYGEEIG MSNVDVECTG DSCEDRDGER 

       430        440        450        460        470        480 
TPMQWTAGKN ADFSDGESTW LPLSPEYQRY NVQTERGVSR SSLNIFKGLQ ELKSSSAFLA 

       490        500        510        520        530        540 
FKEDGGFSYE AVTEQVLQII RTNKISEEYR ILVNMGNGME ILDGLAPKTY EYVLATAYST 

       550        560 
HYSGQKADLS QRIILMPYEA VVLRWLA 

« Hide

References

« Hide 'large scale' references
[1]"Two gene families clustered in a small region of the Drosophila genome."
Snyder M., Davidson N.
J. Mol. Biol. 166:101-118(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
[2]"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.
[3]"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.
Strain: Berkeley.
[4]"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].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00204 Genomic DNA. Translation: CAA23492.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAF59088.1.
AY071566 mRNA. Translation: AAL49188.1.
PIRS08597.
RefSeqNP_476625.2. NM_057277.2.
UniGeneDm.5267.

3D structure databases

ProteinModelPortalP07191.
SMRP07191. Positions 22-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61677. 5 interactions.
MINTMINT-851985.
STRING7227.FBpp0087826.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbP07191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088747; FBpp0087826; FBgn0002569.
GeneID35825.
KEGGdme:Dmel_CG8694.

Organism-specific databases

CTD35825.
FlyBaseFBgn0002569. Mal-A2.

Phylogenomic databases

eggNOGCOG0366.
GeneTreeENSGT00530000063127.
InParanoidP07191.
KOK01187.
OMADAVPHIY.
OrthoDBEOG7B31NK.
PhylomeDBP07191.

Gene expression databases

BgeeP07191.

Family and domain databases

Gene3D3.20.20.80. 2 hits.
InterProIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi35825.
NextBio795392.

Entry information

Entry nameMAL2_DROME
AccessionPrimary (citable) accession number: P07191
Secondary accession number(s): Q9V4T7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 5, 2005
Last modified: March 19, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

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