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Q24451

- MAN2_DROME

UniProt

Q24451 - MAN2_DROME

Protein

Alpha-mannosidase 2

Gene

alpha-Man-II

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (16 Jun 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway By similarity.By similarity

    Catalytic activityi

    Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531ZincBy similarity
    Metal bindingi155 – 1551ZincBy similarity
    Active sitei267 – 2671NucleophileBy similarity
    Metal bindingi267 – 2671ZincBy similarity
    Metal bindingi534 – 5341ZincBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. mannosidase activity Source: FlyBase
    3. mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Source: UniProtKB-EC
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. encapsulation of foreign target Source: FlyBase
    2. mannose metabolic process Source: InterPro
    3. protein deglycosylation Source: FlyBase
    4. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.2.1.114. 1994.
    SABIO-RKQ24451.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH38. Glycoside Hydrolase Family 38.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-mannosidase 2 (EC:3.2.1.114)
    Alternative name(s):
    Golgi alpha-mannosidase II
    Short name:
    AMan II
    Short name:
    Man II
    Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
    Gene namesi
    Name:alpha-Man-II
    Synonyms:GmII
    ORF Names:CG18802
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0011740. alpha-Man-II.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: FlyBase
    2. Golgi membrane Source: UniProtKB-SubCell
    3. Golgi stack Source: FlyBase
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11081108Alpha-mannosidase 2PRO_0000206906Add
    BLAST

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ24451.

    Expressioni

    Inductioni

    Inhibited by swainsonine and by copper sulfate.1 Publication

    Gene expression databases

    BgeeiQ24451.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Protein-protein interaction databases

    BioGridi66291. 2 interactions.
    DIPiDIP-22953N.
    MINTiMINT-874970.

    Structurei

    Secondary structure

    1
    1108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi97 – 993
    Beta strandi105 – 1073
    Helixi108 – 1147
    Beta strandi123 – 1253
    Helixi135 – 1373
    Beta strandi144 – 15310
    Beta strandi156 – 1605
    Helixi162 – 1687
    Helixi170 – 18314
    Beta strandi189 – 1913
    Helixi194 – 20310
    Helixi206 – 21712
    Beta strandi220 – 2256
    Beta strandi233 – 2353
    Helixi238 – 25619
    Beta strandi262 – 2654
    Beta strandi268 – 2714
    Helixi274 – 2807
    Turni281 – 2833
    Beta strandi286 – 2894
    Helixi294 – 3029
    Beta strandi306 – 3105
    Beta strandi322 – 3265
    Helixi334 – 3363
    Beta strandi338 – 3403
    Helixi342 – 3454
    Helixi346 – 3483
    Helixi350 – 3523
    Turni371 – 3733
    Helixi374 – 38916
    Beta strandi392 – 40413
    Helixi410 – 42920
    Helixi431 – 4333
    Beta strandi435 – 4395
    Helixi442 – 45413
    Beta strandi462 – 4654
    Beta strandi471 – 4733
    Helixi480 – 4823
    Helixi486 – 50722
    Helixi513 – 5153
    Helixi517 – 53115
    Turni534 – 5385
    Helixi543 – 57129
    Turni575 – 5773
    Beta strandi586 – 5905
    Beta strandi592 – 5954
    Turni597 – 5993
    Turni610 – 6123
    Beta strandi613 – 62210
    Beta strandi624 – 6263
    Beta strandi628 – 63710
    Beta strandi641 – 6455
    Beta strandi653 – 66412
    Turni665 – 6684
    Beta strandi669 – 68719
    Beta strandi691 – 6999
    Beta strandi707 – 7093
    Beta strandi711 – 7155
    Beta strandi732 – 7343
    Beta strandi739 – 7424
    Beta strandi748 – 7514
    Beta strandi757 – 7615
    Beta strandi763 – 7664
    Beta strandi769 – 77810
    Beta strandi782 – 7843
    Beta strandi794 – 7974
    Beta strandi808 – 8125
    Beta strandi817 – 8237
    Beta strandi826 – 83611
    Beta strandi838 – 8436
    Beta strandi851 – 8599
    Beta strandi866 – 8716
    Turni872 – 8743
    Beta strandi875 – 8806
    Helixi887 – 8904
    Beta strandi892 – 90110
    Beta strandi903 – 91311
    Beta strandi915 – 9184
    Beta strandi924 – 93310
    Beta strandi938 – 9403
    Beta strandi951 – 96111
    Beta strandi973 – 9753
    Helixi979 – 98911
    Beta strandi993 – 9975
    Beta strandi1007 – 10093
    Beta strandi1020 – 10278
    Beta strandi1034 – 104411
    Helixi1062 – 10643
    Beta strandi1065 – 107511
    Beta strandi1081 – 10855
    Helixi1087 – 10893
    Beta strandi1099 – 11079

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HTYX-ray1.40A94-1108[»]
    1HWWX-ray1.87A94-1108[»]
    1HXKX-ray1.50A94-1108[»]
    1PS3X-ray1.80A64-1108[»]
    1QWNX-ray1.20A76-1108[»]
    1QWUX-ray2.03A76-1108[»]
    1QX1X-ray1.30A76-1108[»]
    1R33X-ray1.80A76-1108[»]
    1R34X-ray1.95A76-1108[»]
    1TQSX-ray1.30A76-1108[»]
    1TQTX-ray1.90A76-1108[»]
    1TQUX-ray2.03A76-1108[»]
    1TQVX-ray2.03A76-1108[»]
    1TQWX-ray1.20A76-1108[»]
    2ALWX-ray1.86A76-1108[»]
    2F18X-ray1.30A76-1108[»]
    2F1AX-ray1.45A76-1108[»]
    2F1BX-ray1.45A76-1108[»]
    2F7OX-ray1.43A76-1108[»]
    2F7PX-ray1.28A76-1108[»]
    2F7QX-ray1.85A76-1108[»]
    2F7RX-ray1.35A76-1108[»]
    2FYVX-ray1.90A76-1108[»]
    2OW6X-ray1.19A76-1108[»]
    2OW7X-ray1.77A76-1108[»]
    3BLBX-ray1.30A76-1108[»]
    3BUBX-ray1.38A76-1108[»]
    3BUDX-ray1.85A76-1108[»]
    3BUIX-ray1.25A76-1108[»]
    3BUPX-ray2.03A76-1108[»]
    3BUQX-ray2.01A76-1108[»]
    3BVTX-ray1.30A76-1108[»]
    3BVUX-ray1.12A76-1108[»]
    3BVVX-ray1.30A76-1108[»]
    3BVWX-ray1.20A76-1108[»]
    3BVXX-ray1.10A76-1108[»]
    3CV5X-ray1.60A76-1108[»]
    3CZNX-ray1.40A76-1108[»]
    3CZSX-ray1.30A76-1108[»]
    3D4YX-ray1.52A76-1108[»]
    3D4ZX-ray1.39A76-1108[»]
    3D50X-ray1.79A76-1108[»]
    3D51X-ray1.43A76-1108[»]
    3D52X-ray1.60A76-1108[»]
    3DDFX-ray1.20A76-1108[»]
    3DDGX-ray1.74A76-1108[»]
    3DX0X-ray1.70A76-1108[»]
    3DX1X-ray1.21A76-1108[»]
    3DX2X-ray1.40A76-1108[»]
    3DX3X-ray1.42A76-1108[»]
    3DX4X-ray1.38A76-1108[»]
    3EJPX-ray1.32A76-1108[»]
    3EJQX-ray1.45A76-1108[»]
    3EJRX-ray1.27A76-1108[»]
    3EJSX-ray1.35A76-1108[»]
    3EJTX-ray1.35A76-1108[»]
    3EJUX-ray1.32A76-1108[»]
    ProteinModelPortaliQ24451.
    SMRiQ24451. Positions 93-1108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ24451.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini31 – 11081078LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0383.
    GeneTreeiENSGT00510000046304.
    InParanoidiQ24451.
    KOiK01231.
    OMAiNTEIVMR.
    OrthoDBiEOG7JQBMJ.
    PhylomeDBiQ24451.

    Family and domain databases

    Gene3Di1.20.1270.50. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.110.10. 1 hit.
    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR013780. Glyco_hydro_13_b.
    IPR027291. Glyco_hydro_38/57_N.
    IPR011682. Glyco_hydro_38_C.
    IPR015341. Glyco_hydro_38_cen.
    IPR000602. Glyco_hydro_38_N.
    IPR028995. Glyco_hydro_57/38_cen.
    [Graphical view]
    PfamiPF09261. Alpha-mann_mid. 1 hit.
    PF01074. Glyco_hydro_38. 1 hit.
    PF07748. Glyco_hydro_38C. 1 hit.
    [Graphical view]
    SMARTiSM00872. Alpha-mann_mid. 1 hit.
    [Graphical view]
    SUPFAMiSSF74650. SSF74650. 1 hit.
    SSF88688. SSF88688. 1 hit.
    SSF88713. SSF88713. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q24451-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE     50
    LENGLQEHGE EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD 100
    VPNVDVQMLE LYDRMSFKDI DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP 150
    HSHNDPGWIQ TFEEYYQHDT KHILSNALRH LHDNPEMKFI WAEISYFARF 200
    YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN VLLQLTEGQT 250
    WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL 300
    AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF 350
    KRMGSFGLSC PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP 400
    LGDDFRFKQN TEWDVQRVNY ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH 450
    QAERAGQAEF PTLSGDFFTY ADRSDNYWSG YYTSRPYHKR MDRVLMHYVR 500
    AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT AKTHVVVDYE 550
    QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE 600
    DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP 650
    VEAQVSPVWS WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS 700
    DSKPEHTSYA SNLLLRKNPT SLPLGQYPED VKFGDPREIS LRVGNGPTLA 750
    FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV RSHGDRSGAY LFLPNGPASP 800
    VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR NLVDIGSLDN 850
    TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI 900
    EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP 950
    VLHIYRLVLE KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN 1000
    EWIGAQGQFG GDHPSAREDL DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC 1050
    GTPEEHTQKL DVCHLLPNVA RCERTTLTFL QNLEHLDGMV APEVCPMETA 1100
    AYVSSHSS 1108
    Length:1,108
    Mass (Da):126,721
    Last modified:June 16, 2003 - v2
    Checksum:i55E370EC8CAC6D4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711E → K in CAA54732. (PubMed:7890162)Curated
    Sequence conflicti305 – 3062QL → HV in CAA10755. (PubMed:10504337)Curated
    Sequence conflicti397 – 3971L → V in CAA10755. (PubMed:10504337)Curated
    Sequence conflicti970 – 9701E → K in CAA54732. (PubMed:7890162)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77652 mRNA. Translation: CAA54732.1.
    AJ132715 Genomic DNA. Translation: CAA10755.1.
    AE014297 Genomic DNA. Translation: AAF54375.1.
    AY119464 mRNA. Translation: AAM50118.1.
    PIRiJC4037.
    RefSeqiNP_524291.2. NM_079567.3.
    UniGeneiDm.2459.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082031; FBpp0081509; FBgn0011740.
    GeneIDi41126.
    KEGGidme:Dmel_CG18802.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77652 mRNA. Translation: CAA54732.1 .
    AJ132715 Genomic DNA. Translation: CAA10755.1 .
    AE014297 Genomic DNA. Translation: AAF54375.1 .
    AY119464 mRNA. Translation: AAM50118.1 .
    PIRi JC4037.
    RefSeqi NP_524291.2. NM_079567.3.
    UniGenei Dm.2459.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HTY X-ray 1.40 A 94-1108 [» ]
    1HWW X-ray 1.87 A 94-1108 [» ]
    1HXK X-ray 1.50 A 94-1108 [» ]
    1PS3 X-ray 1.80 A 64-1108 [» ]
    1QWN X-ray 1.20 A 76-1108 [» ]
    1QWU X-ray 2.03 A 76-1108 [» ]
    1QX1 X-ray 1.30 A 76-1108 [» ]
    1R33 X-ray 1.80 A 76-1108 [» ]
    1R34 X-ray 1.95 A 76-1108 [» ]
    1TQS X-ray 1.30 A 76-1108 [» ]
    1TQT X-ray 1.90 A 76-1108 [» ]
    1TQU X-ray 2.03 A 76-1108 [» ]
    1TQV X-ray 2.03 A 76-1108 [» ]
    1TQW X-ray 1.20 A 76-1108 [» ]
    2ALW X-ray 1.86 A 76-1108 [» ]
    2F18 X-ray 1.30 A 76-1108 [» ]
    2F1A X-ray 1.45 A 76-1108 [» ]
    2F1B X-ray 1.45 A 76-1108 [» ]
    2F7O X-ray 1.43 A 76-1108 [» ]
    2F7P X-ray 1.28 A 76-1108 [» ]
    2F7Q X-ray 1.85 A 76-1108 [» ]
    2F7R X-ray 1.35 A 76-1108 [» ]
    2FYV X-ray 1.90 A 76-1108 [» ]
    2OW6 X-ray 1.19 A 76-1108 [» ]
    2OW7 X-ray 1.77 A 76-1108 [» ]
    3BLB X-ray 1.30 A 76-1108 [» ]
    3BUB X-ray 1.38 A 76-1108 [» ]
    3BUD X-ray 1.85 A 76-1108 [» ]
    3BUI X-ray 1.25 A 76-1108 [» ]
    3BUP X-ray 2.03 A 76-1108 [» ]
    3BUQ X-ray 2.01 A 76-1108 [» ]
    3BVT X-ray 1.30 A 76-1108 [» ]
    3BVU X-ray 1.12 A 76-1108 [» ]
    3BVV X-ray 1.30 A 76-1108 [» ]
    3BVW X-ray 1.20 A 76-1108 [» ]
    3BVX X-ray 1.10 A 76-1108 [» ]
    3CV5 X-ray 1.60 A 76-1108 [» ]
    3CZN X-ray 1.40 A 76-1108 [» ]
    3CZS X-ray 1.30 A 76-1108 [» ]
    3D4Y X-ray 1.52 A 76-1108 [» ]
    3D4Z X-ray 1.39 A 76-1108 [» ]
    3D50 X-ray 1.79 A 76-1108 [» ]
    3D51 X-ray 1.43 A 76-1108 [» ]
    3D52 X-ray 1.60 A 76-1108 [» ]
    3DDF X-ray 1.20 A 76-1108 [» ]
    3DDG X-ray 1.74 A 76-1108 [» ]
    3DX0 X-ray 1.70 A 76-1108 [» ]
    3DX1 X-ray 1.21 A 76-1108 [» ]
    3DX2 X-ray 1.40 A 76-1108 [» ]
    3DX3 X-ray 1.42 A 76-1108 [» ]
    3DX4 X-ray 1.38 A 76-1108 [» ]
    3EJP X-ray 1.32 A 76-1108 [» ]
    3EJQ X-ray 1.45 A 76-1108 [» ]
    3EJR X-ray 1.27 A 76-1108 [» ]
    3EJS X-ray 1.35 A 76-1108 [» ]
    3EJT X-ray 1.35 A 76-1108 [» ]
    3EJU X-ray 1.32 A 76-1108 [» ]
    ProteinModelPortali Q24451.
    SMRi Q24451. Positions 93-1108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66291. 2 interactions.
    DIPi DIP-22953N.
    MINTi MINT-874970.

    Chemistry

    BindingDBi Q24451.

    Protein family/group databases

    CAZyi GH38. Glycoside Hydrolase Family 38.

    Proteomic databases

    PaxDbi Q24451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082031 ; FBpp0081509 ; FBgn0011740 .
    GeneIDi 41126.
    KEGGi dme:Dmel_CG18802.

    Organism-specific databases

    CTDi 41126.
    FlyBasei FBgn0011740. alpha-Man-II.

    Phylogenomic databases

    eggNOGi COG0383.
    GeneTreei ENSGT00510000046304.
    InParanoidi Q24451.
    KOi K01231.
    OMAi NTEIVMR.
    OrthoDBi EOG7JQBMJ.
    PhylomeDBi Q24451.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 3.2.1.114. 1994.
    SABIO-RK Q24451.

    Miscellaneous databases

    ChiTaRSi alpha-Man-II. drosophila.
    EvolutionaryTracei Q24451.
    GenomeRNAii 41126.
    NextBioi 822320.
    PROi Q24451.

    Gene expression databases

    Bgeei Q24451.

    Family and domain databases

    Gene3Di 1.20.1270.50. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.110.10. 1 hit.
    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR013780. Glyco_hydro_13_b.
    IPR027291. Glyco_hydro_38/57_N.
    IPR011682. Glyco_hydro_38_C.
    IPR015341. Glyco_hydro_38_cen.
    IPR000602. Glyco_hydro_38_N.
    IPR028995. Glyco_hydro_57/38_cen.
    [Graphical view ]
    Pfami PF09261. Alpha-mann_mid. 1 hit.
    PF01074. Glyco_hydro_38. 1 hit.
    PF07748. Glyco_hydro_38C. 1 hit.
    [Graphical view ]
    SMARTi SM00872. Alpha-mann_mid. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74650. SSF74650. 1 hit.
    SSF88688. SSF88688. 1 hit.
    SSF88713. SSF88713. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of GmII, a Drosophila melanogaster homologue of the cDNA encoding murine Golgi alpha-mannosidase II."
      Foster J.M., Yudkin B., Lockyer A.E., Roberts D.B.
      Gene 154:183-186(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The Drosophila GMII gene encodes a Golgi alpha-mannosidase II."
      Rabouille C., Kuntz D.A., Lockyer A.E., Watson R., Signorelli T., Rose D.R., van den Heuvel M., Roberts D.B.
      J. Cell Sci. 112:3319-3330(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiMAN2_DROME
    AccessioniPrimary (citable) accession number: Q24451
    Secondary accession number(s): Q9TYG5, Q9VHD8, Q9VHD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 16, 2003
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3