P53624 (MA121_DROME) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	667 AA.
Sequence status	Complete.
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 Transmembrane helix
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	determination of adult lifespan Inferred from mutant phenotype PubMed 19302370. Source: FlyBase encapsulation of foreign target Inferred from mutant phenotype PubMed 22829770. Source: FlyBase protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway response to anesthetic Inferred from mutant phenotype PubMed 19863272. Source: FlyBase
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: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: EC
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.
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	Helical; 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 [UniParc]. See P53625.		–	–

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_167223.2. NP_996395.1. NM_206672.2. NP_996396.1. NM_206673.2. NP_996397.1. NM_206674.2. NP_996398.1. NM_206675.2. NP_996399.1. NM_206676.2.
UniGene	Dm.7316.
3D structure databases
ProteinModelPortal	P53624.
SMR	P53624. Positions 194-647.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53624. 2 interactions.
MINT	MINT-946839.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Proteomic databases
PaxDb	P53624.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0299632; FBpp0288907; FBgn0259170. FBtr0300511; FBpp0289738; FBgn0259170. FBtr0300513; FBpp0289740; FBgn0259170. FBtr0300514; FBpp0289741; FBgn0259170. FBtr0300515; FBpp0289742; FBgn0259170. FBtr0300516; FBpp0289743; FBgn0259170.
GeneID	31957.
KEGG	dme:Dmel_CG42275.
Organism-specific databases
CTD	31957.
FlyBase	FBgn0259170. alpha-Man-I.
Phylogenomic databases
eggNOG	NOG300315.
GeneTree	ENSGT00390000016529.
InParanoid	P53624.
KO	K01230.
OMA	TTTCHES.
OrthoDB	EOG4B2RC8.
PhylomeDB	P53624.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	P53624.
GermOnline	CG32684. Drosophila melanogaster.
Family and domain databases
Gene3D	1.50.10.50. 1 hit.
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
PANTHER	PTHR11742. PTHR11742. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	alpha-Man-I. drosophila.
GenomeRNAi	31957.
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:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project