Reviewed, UniProtKB/Swiss-Prot P53624 (MA121_DROME)

Names and origin

Protein names

Recommended name:
    Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform A
    EC=3.2.1.113
Alternative name(s):
    Man(9)-alpha-mannosidase
    Mannosidase-1

Gene names

Name:	alpha-Man-I
Synonyms:	ALPHA-MAN-1, mas-1
ORF Names:	CG32684

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	667 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.
Catalytic activity	Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Cofactor	Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Complex spatial distribution during embryogenesis, including expression in lobula plate giant neurons. Also expressed in adult wing and eyes.
Developmental stage	Expressed both maternally and zygotically during embryonic stages.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mbm	Q9VPM5	1	EBI-179043,EBI-178893
step	Q9V9Q6	1	EBI-179043,EBI-164677

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P53624-1)

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

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.

Isoform B (identifier: P53625-1)

The sequence of this isoform can be found in the external entry P53625-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 667	667	Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform A		PRO_0000210316
Regions
	Topological domain	1 – 18	18	Cytoplasmic Potential
	Transmembrane	19 – 39	21	Signal-anchor for type II membrane protein Potential
	Topological domain	40 – 667	628	Lumenal Potential
Amino acid modifications
	Glycosylation	278	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	21	1	I → T in CAA57962. Ref.1
	Sequence conflict	568	1	D → E in CAA57962. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (C) (D) (E) (F) (G) [UniParc]. Last modified March 15, 2004. Version 2. Checksum: D707F491E4AE47F2	FASTA	667	74,966
	10 20 30 40 50 60 MYRISPIGRK SNFHSREKCL IGLVLVTLCF LCFGGIFLLP DNFGSDRVLR VYKHFRKAGP 70 80 90 100 110 120 EIFIPAPPLA AHAPHRSEDP HFIGDRQRLE QKIRAELGDM LDEPPAAGGG EPGQFQVLAQ 130 140 150 160 170 180 QAQAPAPVAA LADQPLDQDE GHAAIPVLAA PVQGDNAASQ ASSHPQSSAQ QHNQQQPQLP 190 200 210 220 230 240 LGGGGNDQAP DTLDATLEER RQKVKEMMEH AWHNYKLYAW GKNELRPLSQ RPHSASIFGS 250 260 270 280 290 300 YDLGATIVDG LDTLYIMGLE KEYREGRDWI ERKFSLDNIS AELSVFETNI RFVGGMLTLY 310 320 330 340 350 360 AFTGDPLYKE KAQHVADKLL PAFQTPTGIP YALVNTKTGV AKNYGWASGG SSILSEFGTL 370 380 390 400 410 420 HLEFAYLSDI TGNPLYRERV QTIRQVLKEI EKPKGLYPNF LNPKTGKWGQ LHMSLGALGD 430 440 450 460 470 480 SYYEYLLKAW LQSGQTDEEA REMFDEAMLA ILDKMVRTSP GGLTYVSDLK FDRLEHKMDH 490 500 510 520 530 540 LACFSGGLFA LGAATRQNDY TDKYMEVGKG ITNTCHESYI RAPTQLGPEA FRFSEAVEAR 550 560 570 580 590 600 ALRSQEKYYI LRPETFESYF VLWRLTHDQK YRDWGWEAVL ALEKHCRTAH GYCGLRNVYQ 610 620 630 640 650 660 QEPQKDDVQQ SFFLAETLKY LYLLFSDDSV LPLDEWVFNT EAHPLPIKGA NAYYRQAPVT LPVSNAS
	Isoform B. See P53625.	FASTA	–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7729592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Berlin. Tissue: Ovary.
[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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"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.
[4]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X82640 mRNA. Translation: CAA57962.1. AE014298 Genomic DNA. Translation: AAF46570.1. AE014298 Genomic DNA. Translation: AAS65302.1. AE014298 Genomic DNA. Translation: AAS65303.1. AE014298 Genomic DNA. Translation: AAS65304.1. AE014298 Genomic DNA. Translation: AAS65305.1. AE014298 Genomic DNA. Translation: AAS65306.1. BT011036 mRNA. Translation: AAR30196.1.
PIR	S60709.
RefSeq	NP_727407.1. NP_996395.1. NP_996396.1. NP_996397.1. NP_996398.1. NP_996399.1.
UniGene	Dm.7316
3D structure databases
HSSP	HSSP built from PDB template 1FO3 based on UniProtKB Q9UKM7.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53624. 2 interactions.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Genome annotation databases
Ensembl	FBgn0010338. Drosophila melanogaster. [Contig view]
GeneID	31957.
Organism-specific databases
FlyBase	FBgn0259170. alpha-Man-I.
Phylogenomic databases
HOGENOM	P53624.
OMA	P53624. PEVIEGW.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001313-MON.
BRENDA	3.2.1.113. 48.
Gene expression databases
ArrayExpress	P53624.
GermOnline	CG32684. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
ProtoNet	Search...
Other Resources
NextBio	776122.

Entry information

Entry name

MA121_DROME

Accession

Primary (citable) accession number: P53624
Secondary accession number(s): A4V480, Q9W2W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 15, 2004
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project