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O02773 (MA1A1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

EC=3.2.1.113
Alternative name(s):
Man(9)-alpha-mannosidase
Short name=Man9-mannosidase
Mannosidase alpha class 1A member 1
Processing alpha-1,2-mannosidase IA
Short name=Alpha-1,2-mannosidase IA
Gene names
Name:MAN1A1
Synonyms:MAN1A
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length659 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.

Enzyme regulation

Inhibited by both 1-deoxymannojirimycin and kifunensine By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 659659Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
PRO_0000210310

Regions

Topological domain1 – 4848Cytoplasmic Potential
Transmembrane49 – 6921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain70 – 659590Lumenal Potential

Sites

Metal binding6391Calcium By similarity

Amino acid modifications

Disulfide bond482 ↔ 514 By similarity

Sequences

Sequence LengthMass (Da)Tools
O02773 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: AA7F17FEAAFE43A6

FASTA65973,197
        10         20         30         40         50         60 
MPVGGLLPLF SSPAGGGLGG GLGGGLGGGG GGGGRKGSGP SAFRLTEKFV LLLVFSAFIT 

        70         80         90        100        110        120 
LCFGAIFFLP DSSKLLSGVL FHSSPALQPA ADHKPGPGAR AEDAADGRAR PGEEGAPGDP 

       130        140        150        160        170        180 
AAALEDNLAR IRENHERALM EAKETLQKLP EEIQRDILME KEKVAQDQMS NRMGFRLPPV 

       190        200        210        220        230        240 
YLVPLIGAID REPADAAVRE KRAKIKEMMK HAWNNYKLYA WGKNELKPVS KGGHSSSLFG 

       250        260        270        280        290        300 
NIKGATIVDA LDTLFIMKMK NEFEEAKAWV EEHLNFNVNA EVSVFEVNIR FIGGLISAYY 

       310        320        330        340        350        360 
LSGEEIFRKK AVELGVKLLP AFYTPSGIPW ALLNIKSGIG RNWPWASGGS SILAEFGTLH 

       370        380        390        400        410        420 
LEFIHLSYLS GNPFFAEKVM NIRKVLNNLE KPQGLYPNYL NPNSGQWGQY HVSVGGLGDS 

       430        440        450        460        470        480 
FYEYLLKAWL MSDKTDLEAK KMYFDAIKAI ETHLIRKSRN GLTYIAEWKG GLLEHKMGHL 

       490        500        510        520        530        540 
TCFAGGMFAL GADDAPDGLT QHYLQLGAEI ARTCHESYSR TFVKLGPEAF RFDGGVEAIA 

       550        560        570        580        590        600 
TRQNEKYYIL RPEVVETYLY MWRLTHDPKY RKWAWEAVEA LEKHCRVNGG YSGLRDVYVS 

       610        620        630        640        650 
AQTYDDVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHPLPVLSRN IKKVEDNEK 

« Hide

References

[1]"Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells."
Bieberich E., Treml K., Volker C., Rolfs A., Kalz-Fueller B., Bause E.
Eur. J. Biochem. 246:681-689(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
Tissue: Liver.
[2]"Molecular cloning and primary structure of Man9-mannosidase from human kidney."
Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B.
Eur. J. Biochem. 217:535-540(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12503 mRNA. Translation: CAA73105.1.
PIRS78554.
RefSeqNP_999050.1. NM_213885.1.
UniGeneSsc.14512.

3D structure databases

ProteinModelPortalO02773.
SMRO02773. Positions 182-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000004583.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396919.
KEGGssc:396919.

Organism-specific databases

CTD4121.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181988.
HOVERGENHBG052389.
KOK01230.

Enzyme and pathway databases

UniPathwayUPA00378.

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...

Entry information

Entry nameMA1A1_PIG
AccessionPrimary (citable) accession number: O02773
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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