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Q24451 (MAN2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:alpha-Man-II
Synonyms:GmII
ORF Names:CG18802
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1108 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3. Ref.2

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.2.

Induction

Inhibited by swainsonine and by copper sulfate. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11081108Alpha-mannosidase 2
PRO_0000206906

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 11081078Lumenal Potential

Sites

Active site2671Nucleophile By similarity
Metal binding1531Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding2671Zinc By similarity
Metal binding5341Zinc By similarity

Experimental info

Sequence conflict711E → K in CAA54732. Ref.1
Sequence conflict305 – 3062QL → HV in CAA10755. Ref.2
Sequence conflict3971L → V in CAA10755. Ref.2
Sequence conflict9701E → K in CAA54732. Ref.1

Secondary structure

............................................................................................................................................................................... 1108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q24451 [UniParc].

Last modified June 16, 2003. Version 2.
Checksum: 55E370EC8CAC6D4A

FASTA1,108126,721
        10         20         30         40         50         60 
MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE LENGLQEHGE 

        70         80         90        100        110        120 
EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD VPNVDVQMLE LYDRMSFKDI 

       130        140        150        160        170        180 
DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP HSHNDPGWIQ TFEEYYQHDT KHILSNALRH 

       190        200        210        220        230        240 
LHDNPEMKFI WAEISYFARF YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN 

       250        260        270        280        290        300 
VLLQLTEGQT WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL 

       310        320        330        340        350        360 
AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF KRMGSFGLSC 

       370        380        390        400        410        420 
PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP LGDDFRFKQN TEWDVQRVNY 

       430        440        450        460        470        480 
ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH QAERAGQAEF PTLSGDFFTY ADRSDNYWSG 

       490        500        510        520        530        540 
YYTSRPYHKR MDRVLMHYVR AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT 

       550        560        570        580        590        600 
AKTHVVVDYE QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE 

       610        620        630        640        650        660 
DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP VEAQVSPVWS 

       670        680        690        700        710        720 
WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS DSKPEHTSYA SNLLLRKNPT 

       730        740        750        760        770        780 
SLPLGQYPED VKFGDPREIS LRVGNGPTLA FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV 

       790        800        810        820        830        840 
RSHGDRSGAY LFLPNGPASP VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR 

       850        860        870        880        890        900 
NLVDIGSLDN TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI 

       910        920        930        940        950        960 
EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP VLHIYRLVLE 

       970        980        990       1000       1010       1020 
KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN EWIGAQGQFG GDHPSAREDL 

      1030       1040       1050       1060       1070       1080 
DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC GTPEEHTQKL DVCHLLPNVA RCERTTLTFL 

      1090       1100 
QNLEHLDGMV APEVCPMETA AYVSSHSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77652 mRNA. Translation: CAA54732.1.
AJ132715 Genomic DNA. Translation: CAA10755.1.
AE014297 Genomic DNA. Translation: AAF54375.1.
AY119464 mRNA. Translation: AAM50118.1.
PIRJC4037.
RefSeqNP_524291.2. NM_079567.3.
UniGeneDm.2459.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ24451.
SMRQ24451. Positions 93-1108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66291. 2 interactions.
DIPDIP-22953N.
MINTMINT-874970.

Chemistry

BindingDBQ24451.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbQ24451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082031; FBpp0081509; FBgn0011740.
GeneID41126.
KEGGdme:Dmel_CG18802.

Organism-specific databases

CTD41126.
FlyBaseFBgn0011740. alpha-Man-II.

Phylogenomic databases

eggNOGCOG0383.
GeneTreeENSGT00510000046304.
InParanoidQ24451.
KOK01231.
OMAAREGNSH.
OrthoDBEOG7JQBMJ.
PhylomeDBQ24451.

Enzyme and pathway databases

BRENDA3.2.1.114. 1994.
SABIO-RKQ24451.
UniPathwayUPA00378.

Gene expression databases

BgeeQ24451.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. 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.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

ChiTaRSalpha-Man-II. drosophila.
EvolutionaryTraceQ24451.
GenomeRNAi41126.
NextBio822320.
PROQ24451.

Entry information

Entry nameMAN2_DROME
AccessionPrimary (citable) accession number: Q24451
Secondary accession number(s): Q9TYG5, Q9VHD8, Q9VHD9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 16, 2003
Last modified: March 19, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase