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Protein

Maltase A3

Gene

Mal-A3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei220 – 2201NucleophileBy similarity
Active sitei293 – 2931Proton donorBy similarity
Sitei359 – 3591Transition state stabilizerBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_294641. Amino acid transport across the plasma membrane.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltase A3 (EC:3.2.1.20)
Alternative name(s):
Larval visceral protein L
Gene namesi
Name:Mal-A3
Synonyms:LvpL
ORF Names:CG8695
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0002571. Mal-A3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 574555Maltase A3PRO_0000001448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP07192.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiP07192.
GenevisibleiP07192. DM.

Interactioni

Protein-protein interaction databases

IntActiP07192. 1 interaction.
STRINGi7227.FBpp0087837.

Structurei

3D structure databases

ProteinModelPortaliP07192.
SMRiP07192. Positions 20-574.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00530000063127.
InParanoidiP07192.
KOiK01187.
OMAiSNEQEFE.
OrthoDBiEOG7B31NK.
PhylomeDBiP07192.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P07192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKLLVLSCL LALALPSLAE VGWWKTGQFY QIYPRSFKDS DGDGVGDLIG
60 70 80 90 100
ITQQLPYLKE IGITATWLSP IFTSPMADFG YDVADLKGID PIFGTMEDFE
110 120 130 140 150
ALLARAKELD IKIILDFVPN HTSDECDWFI RSAAGEEEYK DFYVWHTGKV
160 170 180 190 200
VNGIRQPPTN WVSVFRGSMW TWNEQRQAYY LHQFHAKQPD LNYRNPKVVE
210 220 230 240 250
AMKDVLRFWL RKGAYGFRID AVPHVYEIPA DADGNWPDEP RNEAVSDPED
260 270 280 290 300
YTYLQHIYTT DQPETLELVY AFRDVIEEID AELGGDDRVL LTEAYSPLEV
310 320 330 340 350
LMQYYGNGTH LGSQIPFNFE LLAKISYSSD AYHYSELIHN WLDNMPEGQV
360 370 380 390 400
ANWVFGNHDQ SRIGSRLGAD RIDACNMIIL GLPGVSVTYQ GEEMGMTDVW
410 420 430 440 450
ISWEDTVDPQ ACQSNEQEFE RLTRDPVRTP FQWSDEVNAG FSNASVTWLP
460 470 480 490 500
VASNYKLVNV KKERGIALSH LNVYKQLRAL RDEPTLKQGD VSVTAIGPNV
510 520 530 540 550
LAFKRSLAGY KSYITLININ DDVESINLDS VFTSITTQLQ YVVVNDKSVR
560 570
RKNDLTFANS VLLLPKEAVV LSTV
Length:574
Mass (Da):65,235
Last modified:June 21, 2005 - v2
Checksum:i6CDD5C92868DE098
GO

Sequence cautioni

The sequence CAA23493.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461H → P in CAA23493 (PubMed:6854639).Curated
Sequence conflicti175 – 1751Q → E in CAA23493 (PubMed:6854639).Curated
Sequence conflicti324 – 3241K → Q in CAA23493 (PubMed:6854639).Curated
Sequence conflicti553 – 5531N → S in CAA23493 (PubMed:6854639).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00204 Genomic DNA. Translation: CAA23493.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAF59087.2.
AY119654 mRNA. Translation: AAM50308.1.
PIRiS08598.
RefSeqiNP_476628.2. NM_057280.4.
UniGeneiDm.529.

Genome annotation databases

EnsemblMetazoaiFBtr0088758; FBpp0087837; FBgn0002571.
GeneIDi35826.
KEGGidme:Dmel_CG8695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00204 Genomic DNA. Translation: CAA23493.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAF59087.2.
AY119654 mRNA. Translation: AAM50308.1.
PIRiS08598.
RefSeqiNP_476628.2. NM_057280.4.
UniGeneiDm.529.

3D structure databases

ProteinModelPortaliP07192.
SMRiP07192. Positions 20-574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07192. 1 interaction.
STRINGi7227.FBpp0087837.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP07192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088758; FBpp0087837; FBgn0002571.
GeneIDi35826.
KEGGidme:Dmel_CG8695.

Organism-specific databases

CTDi35826.
FlyBaseiFBgn0002571. Mal-A3.

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00530000063127.
InParanoidiP07192.
KOiK01187.
OMAiSNEQEFE.
OrthoDBiEOG7B31NK.
PhylomeDBiP07192.

Enzyme and pathway databases

ReactomeiREACT_294641. Amino acid transport across the plasma membrane.

Miscellaneous databases

GenomeRNAii35826.
NextBioi795397.
PROiP07192.

Gene expression databases

BgeeiP07192.
GenevisibleiP07192. DM.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Characterization of maltase clusters in the genus Drosophila."
    Gabrisko M., Janecek S.
    J. Mol. Evol. 72:104-118(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiMAL3_DROME
AccessioniPrimary (citable) accession number: P07192
Secondary accession number(s): Q9V4T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 21, 2005
Last modified: June 24, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.