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P07192

- MAL3_DROME

UniProt

P07192 - MAL3_DROME

Protein

Maltase A3

Gene

Mal-A3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    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

    1. cation binding Source: InterPro
    2. maltose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    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: 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.

    Interactioni

    Protein-protein interaction databases

    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.
    OMAiASYRDIE.
    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

    MFKLLVLSCL LALALPSLAE VGWWKTGQFY QIYPRSFKDS DGDGVGDLIG    50
    ITQQLPYLKE IGITATWLSP IFTSPMADFG YDVADLKGID PIFGTMEDFE 100
    ALLARAKELD IKIILDFVPN HTSDECDWFI RSAAGEEEYK DFYVWHTGKV 150
    VNGIRQPPTN WVSVFRGSMW TWNEQRQAYY LHQFHAKQPD LNYRNPKVVE 200
    AMKDVLRFWL RKGAYGFRID AVPHVYEIPA DADGNWPDEP RNEAVSDPED 250
    YTYLQHIYTT DQPETLELVY AFRDVIEEID AELGGDDRVL LTEAYSPLEV 300
    LMQYYGNGTH LGSQIPFNFE LLAKISYSSD AYHYSELIHN WLDNMPEGQV 350
    ANWVFGNHDQ SRIGSRLGAD RIDACNMIIL GLPGVSVTYQ GEEMGMTDVW 400
    ISWEDTVDPQ ACQSNEQEFE RLTRDPVRTP FQWSDEVNAG FSNASVTWLP 450
    VASNYKLVNV KKERGIALSH LNVYKQLRAL RDEPTLKQGD VSVTAIGPNV 500
    LAFKRSLAGY KSYITLININ DDVESINLDS VFTSITTQLQ YVVVNDKSVR 550
    RKNDLTFANS VLLLPKEAVV LSTV 574
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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_057280.3.
    UniGeneiDm.529.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00204 Genomic DNA. Translation: CAA23493.1 . Sequence problems.
    AE013599 Genomic DNA. Translation: AAF59087.2 .
    AY119654 mRNA. Translation: AAM50308.1 .
    PIRi S08598.
    RefSeqi NP_476628.2. NM_057280.3.
    UniGenei Dm.529.

    3D structure databases

    ProteinModelPortali P07192.
    SMRi P07192. Positions 20-574.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0087837.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbi P07192.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088758 ; FBpp0087837 ; FBgn0002571 .
    GeneIDi 35826.
    KEGGi dme:Dmel_CG8695.

    Organism-specific databases

    CTDi 35826.
    FlyBasei FBgn0002571. Mal-A3.

    Phylogenomic databases

    eggNOGi COG0366.
    GeneTreei ENSGT00530000063127.
    InParanoidi P07192.
    KOi K01187.
    OMAi ASYRDIE.
    OrthoDBi EOG7B31NK.
    PhylomeDBi P07192.

    Miscellaneous databases

    GenomeRNAii 35826.
    NextBioi 795397.

    Gene expression databases

    Bgeei P07192.

    Family and domain databases

    Gene3Di 3.20.20.80. 2 hits.
    InterProi IPR015902. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 122 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