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P45701 (MA1A1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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
Mannosidase alpha class 1A member 1
Processing alpha-1,2-mannosidase IA
Short name=Alpha-1,2-mannosidase IA
Gene names
Name:MAN1A1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length469 AA.
Sequence statusFragment.
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.

Enzyme regulation

Inhibited by both 1-deoxymannojirimycin and kifunensine By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 469›469Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
PRO_0000210311

Regions

Topological domain‹1 – 469›469Lumenal Potential

Sites

Metal binding4491Calcium By similarity

Amino acid modifications

Glycosylation3291N-linked (GlcNAc...) Potential
Disulfide bond292 ↔ 324 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P45701 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A1B9128144FD0D39

FASTA46953,427
        10         20         30         40         50         60 
REPADAAVRE KRAKIKEMME HAWNSYKRYA WGLNELKPIT KEGHSSSLFG TIKGATIVDA 

        70         80         90        100        110        120 
LDTLFIMGME SEFQEAKSWI AENLDFNVNA EISVFEVNIR FVGGLLSAYY LSGEEIFRKK 

       130        140        150        160        170        180 
AVELGIKLLP AFHTPSGIPW ALLNIKSGIG RNWPWASGGS SILAEFGTLH LEFMHLSHLS 

       190        200        210        220        230        240 
GNPIFAEKVM NIRKVLNKLE KPEGLYPNYL NPSSGQWGQH HVSIGGLGDS FYEYLLKAWL 

       250        260        270        280        290        300 
MSEKTDLEAK KMYFDAVQAI ETHLIRKSSG GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL 

       310        320        330        340        350        360 
GADGAPEGRA QHYLELGAEI ARTCHESYNR TFMKLGPEAF RFDGGVEAIA TRQNEKYYIL 

       370        380        390        400        410        420 
RPEVVETYMY MWRLTHDPKY RKWAWEAVEA LESHCRVNGG YSGLRDVYFT HEKYDNVQQS 

       430        440        450        460 
FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHLLPILPTD QKEVEVKVK 

« Hide

References

[1]"Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides."
Lal A., Schutzbach J.S., Forsee W.T., Neame P.J., Moremen K.W.
J. Biol. Chem. 269:9872-9881(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04301 mRNA. Translation: AAA17748.1.
UniGeneOcu.6237.

3D structure databases

ProteinModelPortalP45701.
SMRP45701. Positions 1-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000005793.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181988.
HOVERGENHBG052389.

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_RABIT
AccessionPrimary (citable) accession number: P45701
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 95 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