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P53625

- MA122_DROME

UniProt

P53625 - MA122_DROME

Protein

Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform B

Gene

alpha-Man-I

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      Previous versions | rss
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    Functioni

    Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

    Catalytic activityi

    Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

    Cofactori

    Calcium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. determination of adult lifespan Source: FlyBase
    2. encapsulation of foreign target Source: FlyBase
    3. protein glycosylation Source: UniProtKB-UniPathway
    4. response to anesthetic Source: FlyBase

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_180226. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform B (EC:3.2.1.113)
    Alternative name(s):
    Man(9)-alpha-mannosidase
    Mannosidase-1
    Gene namesi
    Name:alpha-Man-I
    Synonyms:ALPHA-MAN-1, mas-1
    ORF Names:CG32684
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0259170. alpha-Man-I.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 643643Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform BPRO_0000210317Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Tissue specificityi

    Complex spatial distribution during embryogenesis, including expression in lobula plate giant neurons. Also expressed in adult wing and eyes.

    Developmental stagei

    Expressed both maternally and zygotically during embryonic stages.

    Gene expression databases

    BgeeiP53625.

    Interactioni

    Protein-protein interaction databases

    BioGridi58390. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP53625.
    SMRiP53625. Positions 158-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 643611LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00390000016529.
    InParanoidiP53625.
    KOiK01230.
    OMAiYFREENS.

    Family and domain databases

    Gene3Di1.50.10.50. 1 hit.
    InterProiIPR001382. Glyco_hydro_47.
    [Graphical view]
    PANTHERiPTHR11742. PTHR11742. 1 hit.
    PfamiPF01532. Glyco_hydro_47. 1 hit.
    [Graphical view]
    PRINTSiPR00747. GLYHDRLASE47.
    SUPFAMiSSF48225. SSF48225. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P53625-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MCPKTSKTTP LLLIGGICFV IVLVGITGIT LINNINLSNI IRLNEKVASD    50
    SVSNNENQIK ELNYVNNHPR NVYLKLNASS RDDEDDEQMQ KEQEQLELPK 100
    ISAVIGGSKP KVEDNQVKES SEVISPSTST FSMRSSAGEL TSTSAPLSSI 150
    VSVTAPPMPF GGVKYNQSSG LIDYEKRNQV VKMMEHAWHN YKLYAWGKNE 200
    LRPLSQRPHS ASIFGSYDLG ATIVDGLDTL YIMGLEKEYR EGRDWIERKF 250
    SLDNISAELS VFETNIRFVG GMLTLYAFTG DPLYKEKAQH VADKLLPAFQ 300
    TPTGIPYALV NTKTGVAKNY GWASGGSSIL SEFGTLHLEF AYLSDITGNP 350
    LYRERVQTIR QVLKEIEKPK GLYPNFLNPK TGKWGQLHMS LGALGDSYYE 400
    YLLKAWLQSG QTDEEAREMF DEAMLAILDK MVRTSPGGLT YVSDLKFDRL 450
    EHKMDHLACF SGGLFALGAA TRQNDYTDKY MEVGKGITNT CHESYIRAPT 500
    QLGPEAFRFS EAVEARALRS QEKYYILRPE TFESYFVLWR LTHDQKYRDW 550
    GWEAVLALEK HCRTAHGYCG LRNVYQQEPQ KDDVQQSFFL AETLKYLYLL 600
    FSDDSVLPLD EWVFNTEAHP LPIKGANAYY RQAPVTLPVS NAS 643
    Length:643
    Mass (Da):72,525
    Last modified:March 15, 2004 - v2
    Checksum:i8725B99D31DE7AC3
    GO
    Isoform A (identifier: P53624-1) [UniParc]FASTAAdd to Basket

    Also known as: C, D, E, F, G

    The sequence of this isoform can be found in the external entry P53624.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:667
    Mass (Da):74,966
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti544 – 5441D → E in CAA57963. (PubMed:7729592)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82641 mRNA. Translation: CAA57963.1.
    AE014298 Genomic DNA. Translation: AAF46571.3.
    PIRiS60710.
    RefSeqiNP_001259402.1. NM_001272473.1. [P53625-1]
    NP_511105.2. NM_078550.3. [P53625-1]
    UniGeneiDm.7316.

    Genome annotation databases

    EnsemblMetazoaiFBtr0300512; FBpp0289739; FBgn0259170. [P53625-1]
    FBtr0331759; FBpp0304147; FBgn0259170. [P53625-1]
    GeneIDi31957.
    KEGGidme:Dmel_CG42275.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82641 mRNA. Translation: CAA57963.1 .
    AE014298 Genomic DNA. Translation: AAF46571.3 .
    PIRi S60710.
    RefSeqi NP_001259402.1. NM_001272473.1. [P53625-1 ]
    NP_511105.2. NM_078550.3. [P53625-1 ]
    UniGenei Dm.7316.

    3D structure databases

    ProteinModelPortali P53625.
    SMRi P53625. Positions 158-623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58390. 2 interactions.

    Chemistry

    BindingDBi P53625.
    ChEMBLi CHEMBL1697673.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0300512 ; FBpp0289739 ; FBgn0259170 . [P53625-1 ]
    FBtr0331759 ; FBpp0304147 ; FBgn0259170 . [P53625-1 ]
    GeneIDi 31957.
    KEGGi dme:Dmel_CG42275.

    Organism-specific databases

    CTDi 31957.
    FlyBasei FBgn0259170. alpha-Man-I.

    Phylogenomic databases

    GeneTreei ENSGT00390000016529.
    InParanoidi P53625.
    KOi K01230.
    OMAi YFREENS.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_180226. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

    Miscellaneous databases

    ChiTaRSi alpha-Man-I. drosophila.
    GenomeRNAii 31957.
    NextBioi 776122.

    Gene expression databases

    Bgeei P53625.

    Family and domain databases

    Gene3Di 1.50.10.50. 1 hit.
    InterProi IPR001382. Glyco_hydro_47.
    [Graphical view ]
    PANTHERi PTHR11742. PTHR11742. 1 hit.
    Pfami PF01532. Glyco_hydro_47. 1 hit.
    [Graphical view ]
    PRINTSi PR00747. GLYHDRLASE47.
    SUPFAMi SSF48225. SSF48225. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-1) gene which encodes a glycoprotein processing alpha 1,2-mannosidase."
      Kerscher S., Albert S., Wucherpfennig D., Heisenberg M., Schneuwly S.
      Dev. Biol. 168:613-626(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Berlin.
      Tissue: Head.
    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.

    Entry informationi

    Entry nameiMA122_DROME
    AccessioniPrimary (citable) accession number: P53625
    Secondary accession number(s): Q9W2W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: March 15, 2004
    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3