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Protein

Alpha-mannosidase 2

Gene

alpha-Man-II

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

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

Zn2+By similarityNote: 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

GO - Biological processi

  • encapsulation of foreign target Source: FlyBase
  • mannose metabolic process Source: InterPro
  • N-glycan processing Source: FlyBase
  • protein deglycosylation Source: FlyBase
  • rhodopsin biosynthetic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.1.114. 1994.
ReactomeiREACT_296874. Reactions specific to the complex N-glycan synthesis pathway.
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 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0011740. alpha-Man-II.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini31 – 11081078LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • Golgi membrane Source: UniProtKB-SubCell
  • Golgi stack Source: FlyBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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.
IntActiQ24451. 5 interactions.
MINTiMINT-874970.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
OMAiRCERTTL.
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

        10         20         30         40         50
MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE
60 70 80 90 100
LENGLQEHGE EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD
110 120 130 140 150
VPNVDVQMLE LYDRMSFKDI DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP
160 170 180 190 200
HSHNDPGWIQ TFEEYYQHDT KHILSNALRH LHDNPEMKFI WAEISYFARF
210 220 230 240 250
YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN VLLQLTEGQT
260 270 280 290 300
WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL
310 320 330 340 350
AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF
360 370 380 390 400
KRMGSFGLSC PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP
410 420 430 440 450
LGDDFRFKQN TEWDVQRVNY ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH
460 470 480 490 500
QAERAGQAEF PTLSGDFFTY ADRSDNYWSG YYTSRPYHKR MDRVLMHYVR
510 520 530 540 550
AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT AKTHVVVDYE
560 570 580 590 600
QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE
610 620 630 640 650
DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP
660 670 680 690 700
VEAQVSPVWS WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS
710 720 730 740 750
DSKPEHTSYA SNLLLRKNPT SLPLGQYPED VKFGDPREIS LRVGNGPTLA
760 770 780 790 800
FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV RSHGDRSGAY LFLPNGPASP
810 820 830 840 850
VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR NLVDIGSLDN
860 870 880 890 900
TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI
910 920 930 940 950
EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP
960 970 980 990 1000
VLHIYRLVLE KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN
1010 1020 1030 1040 1050
EWIGAQGQFG GDHPSAREDL DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC
1060 1070 1080 1090 1100
GTPEEHTQKL DVCHLLPNVA RCERTTLTFL QNLEHLDGMV APEVCPMETA

AYVSSHSS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi66291. 2 interactions.
DIPiDIP-22953N.
IntActiQ24451. 5 interactions.
MINTiMINT-874970.

Chemistry

BindingDBiQ24451.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbiQ24451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi41126.
FlyBaseiFBgn0011740. alpha-Man-II.

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
InParanoidiQ24451.
KOiK01231.
OMAiRCERTTL.
OrthoDBiEOG7JQBMJ.
PhylomeDBiQ24451.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.114. 1994.
ReactomeiREACT_296874. Reactions specific to the complex N-glycan synthesis pathway.
SABIO-RKQ24451.

Miscellaneous databases

ChiTaRSialpha-Man-II. fly.
EvolutionaryTraceiQ24451.
GenomeRNAii41126.
NextBioi822320.
PROiQ24451.

Gene expression databases

BgeeiQ24451.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 139 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

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.