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P33908 (MA1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 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.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
PRO_0000210308

Regions

Topological domain1 – 4141Cytoplasmic Potential
Transmembrane42 – 6221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain63 – 653591Lumenal Potential

Amino acid modifications

Glycosylation5131N-linked (GlcNAc...) Potential
Disulfide bond476 ↔ 508 By similarity

Natural variations

Natural variant6511R → G.
Corresponds to variant rs35544784 [ dbSNP | Ensembl ].
VAR_034102

Experimental info

Sequence conflict29 – 4719KGSGP…VLLLV → MNSNFITFDLKMSLLPSNL in CAA52831. Ref.2
Sequence conflict4641G → R in CAA52831. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P33908 [UniParc].

Last modified April 26, 2005. Version 3.
Checksum: 9B164926636D8554

FASTA65372,969
        10         20         30         40         50         60 
MPVGGLLPLF SSPAGGVLGG GLGGGGGRKG SGPAALRLTE KFVLLLVFSA FITLCFGAIF 

        70         80         90        100        110        120 
FLPDSSKLLS GVLFHSSPAL QPAADHKPGP GARAEDAAEG RARRREEGAP GDPEAALEDN 

       130        140        150        160        170        180 
LARIRENHER ALREAKETLQ KLPEEIQRDI LLEKKKVAQD QLRDKAPFRG LPPVDFVPPI 

       190        200        210        220        230        240 
GVESREPADA AIREKRAKIK EMMKHAWNNY KGYAWGLNEL KPISKGGHSS SLFGNIKGAT 

       250        260        270        280        290        300 
IVDALDTLFI MEMKHEFEEA KSWVEENLDF NVNAEISVFE VNIRFVGGLL SAYYLSGEEI 

       310        320        330        340        350        360 
FRKKAVELGV KLLPAFHTPS GIPWALLNMK SGIGRNWPWA SGGSSILAEF GTLHLEFMHL 

       370        380        390        400        410        420 
SHLSGNPIFA EKVMNIRTVL NKLEKPQGLY PNYLNPSSGQ WGQHHVSVGG LGDSFYEYLL 

       430        440        450        460        470        480 
KAWLMSDKTD LEAKKMYFDA VQAIETHLIR KSSSGLTYIA EWKGGLLEHK MGHLTCFAGG 

       490        500        510        520        530        540 
MFALGADAAP EGMAQHYLEL GAEIARTCHE SYNRTFMKLG PEAFRFDGGV EAIATRQNEK 

       550        560        570        580        590        600 
YYILRPEVME TYMYMWRLTH DPKYRKWAWE AVEALENHCR VNGGYSGLRD VYLLHESYDD 

       610        620        630        640        650 
VQQSFFLAET LKYLYLIFSD DDLLPLEHWI FNSEAHLLPI LPKDKKEVEI REE 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: NUCLEOTIDE SEQUENCE [MRNA] OF 29-653.
Tissue: Kidney.
[3]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL022722, AL078600 Genomic DNA. Translation: CAI20315.1.
AL078600 Genomic DNA. Translation: CAB75695.2.
X74837 mRNA. Translation: CAA52831.1.
PIRS38965.
RefSeqNP_005898.2. NM_005907.3.
UniGeneHs.102788.
Hs.742378.

3D structure databases

ProteinModelPortalP33908.
SMRP33908. Positions 176-641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000357453.

Chemistry

ChEMBLCHEMBL5915.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteP33908.

Polymorphism databases

DMDM62906886.

Proteomic databases

PaxDbP33908.
PRIDEP33908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368468; ENSP00000357453; ENSG00000111885.
GeneID4121.
KEGGhsa:4121.
UCSCuc003pym.2. human.

Organism-specific databases

CTD4121.
GeneCardsGC06M119540.
HGNCHGNC:6821. MAN1A1.
HPACAB037058.
MIM604344. gene.
neXtProtNX_P33908.
PharmGKBPA30570.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181988.
HOVERGENHBG052389.
KOK01230.
OMAMAQHYLE.
OrthoDBEOG7X0VH1.
PhylomeDBP33908.
TreeFamTF313420.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP33908.
BgeeP33908.
CleanExHS_MAN1A1.
GenevestigatorP33908.

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

GeneWikiMAN1A1.
GenomeRNAi4121.
NextBio16180.
PROP33908.
SOURCESearch...

Entry information

Entry nameMA1A1_HUMAN
AccessionPrimary (citable) accession number: P33908
Secondary accession number(s): Q9NU44, Q9UJI3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries