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Reviewed, UniProtKB/Swiss-Prot O60476 (MA1A2_HUMAN)

Last modified November 3, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
    EC=3.2.1.113
Alternative name(s):
    Processing alpha-1,2-mannosidase IB
      Short name=Alpha-1,2-mannosidase IB
    Mannosidase alpha class 1A member 2
Gene names
Name: MAN1A2
Synonyms: MAN1B
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Enzyme regulation

Inhibited by both 1-deoxymannojirimycin and kifunensine.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Tissue specificity

Highest levels of expression in placenta and testis.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
   LigandCalcium
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processN-glycan processing Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane Ref.1

Traceable author statement. Source: ProtInc

membrane fraction Ref.1

Traceable author statement. Source: ProtInc

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
PRO_0000210312

Regions

Topological domain1 – 3636Cytoplasmic Potential
Transmembrane37 – 5721Signal-anchor for type II membrane protein Potential
Topological domain58 – 641584Lumenal Potential

Amino acid modifications

Glycosylation6311N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O60476-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 19DA691A9C4B0ED3

FASTA64173,004
        10         20         30         40         50         60 
MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC FGAFFFLPDS 

        70         80         90        100        110        120 
SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH REEEERLRNK IRADHEKALE 

       130        140        150        160        170        180 
EAKEKLRKSR EEIRAEIQTE KNKVVQEMKI KENKPLPPVP IPNLVGIRGG DPEDNDIREK 

       190        200        210        220        230        240 
REKIKEMMKH AWDNYRTYGW GHNELRPIAR KGHSPNIFGS SQMGATIVDA LDTLYIMGLH 

       250        260        270        280        290        300 
DEFLDGQRWI EDNLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKIK AVQLAEKLLP 

       310        320        330        340        350        360 
AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFIHLSYLT GDLTYYKKVM 

       370        380        390        400        410        420 
HIRKLLQKMD RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS FYEYLLKAWL MSDKTDHEAR 

       430        440        450        460        470        480 
KMYDDAIEAI EKHLIKKSRG GLTFIGEWKN GHLEKKMGHL ACFAGGMFAL GADGSRADKA 

       490        500        510        520        530        540 
GHYLELGAEI ARTCHESYDR TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY 

       550        560        570        580        590        600 
LWRFTHDPRY RQWGWEAALA IEKYCRVNGG FSGVKDVYSS TPTHDDVQQS FFLAETLKYL 

       610        620        630        640 
YLLFSGDDLL PLDHWVFNTE AHPLPVLHLA NTTLSGNPAV R 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha-1,2-mannosidase gene involved in N-glycan maturation."
Tremblay L.O., Campbell-Dyke N., Herscovics A.
Glycobiology 8:585-595(1998) [PubMed: 9592125] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain and Placenta.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF053626 expand/collapse EMBL AC list , AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1.
AF027156 mRNA. Translation: AAC26169.1.
AF053621 expand/collapse EMBL AC list , AF053619, AF053620, AF053615, AF053616, AF053617, AF053618 Genomic DNA. Translation: AAC26200.1.
AL157902, AL358072 Genomic DNA. Translation: CAI22315.1.
AL358072, AL157902 Genomic DNA. Translation: CAH71079.1.
BC063300 mRNA. Translation: AAH63300.1.
IPIIPI00009145.
RefSeqNP_006690.1.
UniGeneHs.435938

3D structure databases

HSSPHSSP built from PDB template 1DL2 based on UniProtKB P32906.
ModBaseSearch...

Protein-protein interaction databases

STRINGO60476.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PRIDEO60476.

Genome annotation databases

EnsemblENST00000329466; ENSP00000358462; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000356554; ENSP00000348959; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000369450; ENSP00000358461; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000413355; ENSP00000399773; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000421535; ENSP00000396362; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000422329; ENSP00000402416; ENSG00000198162; Homo sapiens. [Genome view]
ENST00000449370; ENSP00000412706; ENSG00000198162; Homo sapiens. [Genome view]
GeneID10905.
KEGGhsa:10905.
UCSCuc001ehd.1. human.

Organism-specific databases

CTD10905.
GeneCardsGC01P117623.
H-InvDBHIX0000937.
HGNCHGNC:6822. MAN1A2.
MIM604345. gene.
PharmGKBPA30571.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO60476.
HOVERGENO60476.
OMADHEARKM.

Enzyme and pathway databases

BRENDA3.2.1.113. 247.

Gene expression databases

ArrayExpressO60476.
BgeeO60476.
CleanExHS_MAN1A2.
GenevestigatorO60476.
GermOnlineENSG00000198162. Homo sapiens.

Family and domain databases

InterProIPR001382. Glyco_hydro_47.
[Graphical view]
Gene3DG3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
PANTHERPTHR11742. Glyco_hydro_47. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
ProtoNetSearch...

Other Resources

NextBio41419.
SOURCESearch...

Entry information

Entry nameMA1A2_HUMAN
AccessionPrimary (citable) accession number: O60476
Secondary accession number(s): Q9H510
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents