Reviewed, UniProtKB/Swiss-Prot P53625 (MA122_DROME)

Names and origin

Protein names

Recommended name:
    Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform B
    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	643 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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
Complete GO annotation...

Alternative products

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

Isoform B (identifier: P53625-1)

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 A (identifier: P53624-1)

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

The sequence of this isoform can be found in the external entry P53624-1.
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 – 643	643	Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform B		PRO_0000210317
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Signal-anchor for type II membrane protein Potential
	Topological domain	33 – 643	611	Lumenal Potential
Amino acid modifications
	Glycosylation	36	1	N-linked (GlcNAc...) Potential
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	254	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	544	1	D → E in CAA57963. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified March 15, 2004. Version 2. Checksum: 8725B99D31DE7AC3	FASTA	643	72,525
	10 20 30 40 50 60 MCPKTSKTTP LLLIGGICFV IVLVGITGIT LINNINLSNI IRLNEKVASD SVSNNENQIK 70 80 90 100 110 120 ELNYVNNHPR NVYLKLNASS RDDEDDEQMQ KEQEQLELPK ISAVIGGSKP KVEDNQVKES 130 140 150 160 170 180 SEVISPSTST FSMRSSAGEL TSTSAPLSSI VSVTAPPMPF GGVKYNQSSG LIDYEKRNQV 190 200 210 220 230 240 VKMMEHAWHN YKLYAWGKNE LRPLSQRPHS ASIFGSYDLG ATIVDGLDTL YIMGLEKEYR 250 260 270 280 290 300 EGRDWIERKF SLDNISAELS VFETNIRFVG GMLTLYAFTG DPLYKEKAQH VADKLLPAFQ 310 320 330 340 350 360 TPTGIPYALV NTKTGVAKNY GWASGGSSIL SEFGTLHLEF AYLSDITGNP LYRERVQTIR 370 380 390 400 410 420 QVLKEIEKPK GLYPNFLNPK TGKWGQLHMS LGALGDSYYE YLLKAWLQSG QTDEEAREMF 430 440 450 460 470 480 DEAMLAILDK MVRTSPGGLT YVSDLKFDRL EHKMDHLACF SGGLFALGAA TRQNDYTDKY 490 500 510 520 530 540 MEVGKGITNT CHESYIRAPT QLGPEAFRFS EAVEARALRS QEKYYILRPE TFESYFVLWR 550 560 570 580 590 600 LTHDQKYRDW GWEAVLALEK HCRTAHGYCG LRNVYQQEPQ KDDVQQSFFL AETLKYLYLL 610 620 630 640 FSDDSVLPLD EWVFNTEAHP LPIKGANAYY RQAPVTLPVS NAS
	Isoform A (C) (D) (E) (F) (G). See P53624.	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: Head.
[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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X82641 mRNA. Translation: CAA57963.1. AE014298 Genomic DNA. Translation: AAF46571.3.
PIR	S60710.
RefSeq	NP_511105.2.
UniGene	Dm.7316
3D structure databases
HSSP	HSSP built from PDB template 1FO3 based on UniProtKB Q9UKM7.
ModBase	Search...
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Genome annotation databases
Ensembl	FBgn0010338. Drosophila melanogaster. [Contig view]
GeneID	31957.
NMPDR	fig|7227.3.peg.17243.
Organism-specific databases
FlyBase	FBgn0259170. alpha-Man-I.
Phylogenomic databases
OMA	P53625. THTEEET.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001314-MON.
BRENDA	3.2.1.113. 48.
Gene expression databases
ArrayExpress	P53625.
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

MA122_DROME

Accession

Primary (citable) accession number: P53625
Secondary accession number(s): Q9W2W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 15, 2004
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project