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P53624 (MA121_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform A
PRO_0000210316

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain40 – 667628Lumenal Potential

Amino acid modifications

Glycosylation2781N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict211I → T in CAA57962. Ref.1
Sequence conflict5681D → E in CAA57962. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C) (D) (E) (F) (G) [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: D707F491E4AE47F2

FASTA66774,966
        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 

« Hide

Isoform B [UniParc].

See P53625.

References

« Hide '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. 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.
[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. 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.
[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. expand/collapse author list , 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.
PIRS60709.
RefSeqNP_727407.1. NM_167223.2. [P53624-1]
NP_996395.1. NM_206672.2. [P53624-1]
NP_996396.1. NM_206673.2. [P53624-1]
NP_996397.1. NM_206674.2. [P53624-1]
NP_996398.1. NM_206675.2. [P53624-1]
NP_996399.1. NM_206676.2. [P53624-1]
UniGeneDm.7316.

3D structure databases

ProteinModelPortalP53624.
SMRP53624. Positions 194-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58390. 2 interactions.
IntActP53624. 2 interactions.
MINTMINT-946839.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbP53624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0299632; FBpp0288907; FBgn0259170. [P53624-1]
FBtr0300511; FBpp0289738; FBgn0259170. [P53624-1]
FBtr0300513; FBpp0289740; FBgn0259170. [P53624-1]
FBtr0300514; FBpp0289741; FBgn0259170. [P53624-1]
FBtr0300515; FBpp0289742; FBgn0259170. [P53624-1]
FBtr0300516; FBpp0289743; FBgn0259170. [P53624-1]
GeneID31957.
KEGGdme:Dmel_CG42275.

Organism-specific databases

CTD31957.
FlyBaseFBgn0259170. alpha-Man-I.

Phylogenomic databases

eggNOGNOG300315.
GeneTreeENSGT00390000016529.
InParanoidP53624.
KOK01230.
OMAYLIKSYV.
OrthoDBEOG7X0VH1.
PhylomeDBP53624.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeP53624.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Other

ChiTaRSalpha-Man-I. drosophila.
GenomeRNAi31957.
NextBio776122.

Entry information

Entry nameMA121_DROME
AccessionPrimary (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: July 9, 2014
This is version 123 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

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