Reviewed, UniProtKB/Swiss-Prot Q24451 (MAN2_DROME)

Names and origin

Protein names

Recommended name:
    Alpha-mannosidase 2
    EC=3.2.1.114
Alternative name(s):
    Alpha-mannosidase II
      Short name=AMAN II
      Short name=MAN II
    Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
    Golgi alpha-mannosidase II

Gene names

Name:	alpha-Man-II
Synonyms:	GmII
ORF Names:	CG18802

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mannose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Non-traceable author statement. Source: FlyBase endoplasmic reticulum Non-traceable author statement. Source: FlyBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-mannosidase activity Inferred from electronic annotation. Source: InterPro carbohydrate binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1108

1108

Alpha-mannosidase 2

PRO_0000206906

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 30

21

Signal-anchor for type II membrane protein Potential

Topological domain

31 – 1108

1078

Lumenal Potential

Sites

Active site

267

1

Nucleophile By similarity

Metal binding

153

1

Zinc By similarity

Metal binding

155

1

Zinc By similarity

Metal binding

267

1

Zinc By similarity

Metal binding

534

1

Zinc By similarity

Experimental info

Sequence conflict

71

1

E → K in CAA54732. Ref.1

Sequence conflict

305 – 306

2

QL → HV in CAA10755. Ref.2

Sequence conflict

397

1

L → V in CAA10755. Ref.2

Sequence conflict

970

1

E → K in CAA54732. Ref.1

Secondary structure

1

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1108

Helix Strand Turn

Details...

Beta strand

97 – 99

3

Beta strand

105 – 107

3

Helix

108 – 114

7

Beta strand

123 – 125

3

Helix

135 – 137

3

Beta strand

144 – 153

10

Beta strand

156 – 160

5

Helix

162 – 168

7

Helix

170 – 183

14

Beta strand

189 – 191

3

Helix

194 – 201

8

Helix

206 – 217

12

Beta strand

220 – 225

6

Beta strand

233 – 235

3

Helix

238 – 255

18

Beta strand

262 – 265

4

Beta strand

268 – 271

4

Helix

274 – 280

7

Turn

281 – 283

3

Beta strand

286 – 289

4

Helix

294 – 302

9

Beta strand

306 – 310

5

Beta strand

322 – 326

5

Helix

334 – 336

3

Beta strand

338 – 340

3

Helix

342 – 345

4

Helix

346 – 348

3

Turn

371 – 373

3

Helix

374 – 389

16

Beta strand

392 – 404

13

Helix

410 – 429

20

Helix

431 – 433

3

Beta strand

435 – 439

5

Helix

442 – 454

13

Beta strand

462 – 465

4

Beta strand

471 – 473

3

Helix

480 – 482

3

Helix

486 – 507

22

Helix

513 – 515

3

Helix

517 – 531

15

Turn

534 – 538

5

Helix

543 – 571

29

Turn

575 – 577

3

Beta strand

586 – 590

5

Turn

593 – 599

7

Turn

610 – 612

3

Beta strand

613 – 622

10

Beta strand

624 – 626

3

Beta strand

628 – 637

10

Beta strand

641 – 645

5

Beta strand

653 – 664

12

Turn

665 – 668

4

Beta strand

669 – 687

19

Beta strand

691 – 699

9

Beta strand

707 – 709

3

Beta strand

711 – 715

5

Beta strand

732 – 734

3

Beta strand

739 – 742

4

Beta strand

748 – 751

4

Beta strand

757 – 766

10

Beta strand

769 – 778

10

Beta strand

782 – 785

4

Beta strand

795 – 797

3

Beta strand

808 – 812

5

Beta strand

817 – 823

7

Beta strand

826 – 836

11

Beta strand

838 – 843

6

Beta strand

851 – 859

9

Beta strand

866 – 871

6

Turn

872 – 874

3

Beta strand

875 – 880

6

Helix

887 – 890

4

Beta strand

892 – 901

10

Beta strand

903 – 913

11

Beta strand

915 – 918

4

Beta strand

924 – 935

12

Beta strand

938 – 940

3

Beta strand

951 – 961

11

Beta strand

973 – 975

3

Helix

979 – 989

11

Beta strand

993 – 997

5

Beta strand

1007 – 1009

3

Beta strand

1020 – 1027

8

Beta strand

1034 – 1044

11

Helix

1062 – 1064

3

Beta strand

1065 – 1075

11

Beta strand

1081 – 1085

5

Helix

1087 – 1089

3

Beta strand

1099 – 1106

8

Sequences

	Sequence		Length	Mass (Da)
	Q24451-1 [UniParc]. Last modified June 16, 2003. Version 2. Checksum: 55E370EC8CAC6D4A	FASTA	1,108	126,721
	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

References

	« Hide 'large scale' referencesShow '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: 7890162] [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: 10504337] [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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X77652 mRNA. Translation: CAA54732.1.
AJ132715 Genomic DNA. Translation: CAA10755.1.
AE014297 Genomic DNA. Translation: AAF54375.1.
AY119464 mRNA. Translation: AAM50118.1.

PIR

JC4037.

RefSeq

NP_524291.2.

UniGene

Dm.2459

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:22953N.

IntAct

Q24451. 2 interactions.

Protein family/group databases

CAZy

GH38. Glycoside Hydrolase Family 38.

Genome annotation databases

Ensembl

FBgn0011740. Drosophila melanogaster. [Contig view]

GeneID

41126.

KEGG

dme:Dmel_CG18802.

NMPDR

fig|7227.3.peg.11872.

Organism-specific databases

FlyBase

FBgn0011740. alpha-Man-II.

Phylogenomic databases

HOGENOM

Q24451.

OMA

Q24451. DGGAWKQ.

Enzyme and pathway databases

BioCyc

DMEL-XXX-02:DMEL-XXX-02-010719-MON.

BRENDA

3.2.1.114. 48.

Gene expression databases

ArrayExpress

Q24451.

GermOnline

CG18802. Drosophila melanogaster.

Family and domain databases

InterPro

IPR013780. Glyco_hydro_13_b.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_central.
IPR000602. Glyco_hydro_38_core.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit.

Pfam

PF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

822320.

Entry information

Entry name

MAN2_DROME

Accession

Primary (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:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project