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Q16706 (MA2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Alpha-mannosidase 2

EC=3.2.1.114
Alternative name(s):
Golgi alpha-mannosidase II
Short name=AMan II
Short name=Man II
Mannosidase alpha class 2A member 1
Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
Gene names
Name:MAN2A1
Synonyms:MANA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1144 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.

Catalytic activity

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

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

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-glycan processing

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

mannose metabolic process

Inferred from electronic annotation. Source: InterPro

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

retina morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

vacuole organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hydrolase activity, hydrolyzing N-glycosyl compounds

Inferred from electronic annotation. Source: Ensembl

mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11441144Alpha-mannosidase 2
PRO_0000206902

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 11441118Lumenal Potential

Sites

Active site2891Nucleophile By similarity
Metal binding1751Zinc By similarity
Metal binding1771Zinc By similarity
Metal binding2891Zinc By similarity
Metal binding5691Zinc By similarity

Amino acid modifications

Modified residue801Phosphoserine By similarity
Modified residue821Phosphoserine By similarity
Glycosylation781N-linked (GlcNAc...) Ref.3
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation11251N-linked (GlcNAc...) Ref.3

Experimental info

Sequence conflict6081L → G in AAC50302. Ref.1
Sequence conflict10261Missing in BAA10017. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q16706 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: A1814C63D1CE4FAC

FASTA1,144131,141
        10         20         30         40         50         60 
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPRNPRRE GSFPQGQLSM LQEKIDHLER 

        70         80         90        100        110        120 
LLAENNEIIS NIRDSVINLS ESVEDGPKSS QSNFSQGAGS HLLPSQLSLS VDTADCLFAS 

       130        140        150        160        170        180 
QSGSHNSDVQ MLDVYSLISF DNPDGGVWKQ GFDITYESNE WDTEPLQVFV VPHSHNDPGW 

       190        200        210        220        230        240 
LKTFNDYFRD KTQYIFNNMV LKLKEDSRRK FIWSEISYLS KWWDIIDIQK KDAVKSLIEN 

       250        260        270        280        290        300 
GQLEIVTGGW VMPDEATPHY FALIDQLIEG HQWLENNIGV KPRSGWAIDP FGHSPTMAYL 

       310        320        330        340        350        360 
LNRAGLSHML IQRVHYAVKK HFALHKTLEF FWRQNWDLGS VTDILCHMMP FYSYDIPHTC 

       370        380        390        400        410        420 
GPDPKICCQF DFKRLPGGRF GCPWGVPPET IHPGNVQSRA RMLLDQYRKK SKLFRTKVLL 

       430        440        450        460        470        480 
APLGDDFRYC EYTEWDLQFK NYQQLFDYMN SQSKFKVKIQ FGTLSDFFDA LDKADETQRD 

       490        500        510        520        530        540 
KGQSMFPVLS GDFFTYADRD DHYWSGYFTS RPFYKRMDRI MESHLRAAEI LYYFALRQAH 

       550        560        570        580        590        600 
KYKINKFLSS SLYTALTEAR RNLGLFQHHD AITGTAKDWV VVDYGTRLFH SLMVLEKIIG 

       610        620        630        640        650        660 
NSAFLLILKD KLTYDSYSPD TFLEMDLKQK SQDSLPQKNI IRLSAEPRYL VVYNPLEQDR 

       670        680        690        700        710        720 
ISLVSVYVSS PTVQVFSASG KPVEVQVSAV WDTANTISET AYEISFRAHI PPLGLKVYKI 

       730        740        750        760        770        780 
LESASSNSHL ADYVLYKNKV EDSGIFTIKN MINTEEGITL ENSFVLLRFD QTGLMKQMMT 

       790        800        810        820        830        840 
KEDGKHHEVN VQFSWYGTTI KRDKSGAYLF LPDGNAKPYV YTTPPFVRVT HGRIYSEVTC 

       850        860        870        880        890        900 
FFDHVTHRVR LYHIQGIEGQ SVEVSNIVDI RKVYNREIAM KISSDIKSQN RFYTDLNGYQ 

       910        920        930        940        950        960 
IQPRMTLSKL PLQANVYPMT TMAYIQDAKH RLTLLSAQSL GVSSLNSGQI EVIMDRRLMQ 

       970        980        990       1000       1010       1020 
DDNRGLEQGI QDNKITANLF RILLEKRSAV NTEEEKKSVS YPSLLSHITS SLMNHPVIPM 

      1030       1040       1050       1060       1070       1080 
ANKFSSPTLE LQGEFSPLQS SLPCDIHLVN LRTIQSKVGN GHSNEAALIL HRKGFDCRFS 

      1090       1100       1110       1120       1130       1140 
SKGTGLFCST TQGKILVQKL LNKFIVESLT PSSLSLMHSP PGTQNISEIN LSPMEISTFR 


IQLR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme."
Misago M., Liao Y.-F., Kudo S., Eto S., Mattei M.-G., Moremen K.W., Fukuda M.N.
Proc. Natl. Acad. Sci. U.S.A. 92:11766-11770(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning and sequence analysis of human Golgi mannosidase II."
Misumi Y., Hashimoto C., Sohoda M., Ogata S., Ikehara Y.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-1125.
Tissue: Plasma.
[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
U31520 mRNA. Translation: AAC50302.1.
D63998 mRNA. Translation: BAA10017.1.
RefSeqNP_002363.2. NM_002372.3.
UniGeneHs.432822.

3D structure databases

ProteinModelPortalQ16706.
SMRQ16706. Positions 126-1072.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110297. 4 interactions.
IntActQ16706. 1 interaction.
MINTMINT-2807655.
STRING9606.ENSP00000261483.

Chemistry

BindingDBQ16706.
ChEMBLCHEMBL4056.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

PTM databases

PhosphoSiteQ16706.

Polymorphism databases

DMDM146345453.

Proteomic databases

PaxDbQ16706.
PRIDEQ16706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261483; ENSP00000261483; ENSG00000112893.
GeneID4124.
KEGGhsa:4124.
UCSCuc003kou.1. human.

Organism-specific databases

CTD4124.
GeneCardsGC05P109053.
H-InvDBHIX0005076.
HGNCHGNC:6824. MAN2A1.
HPACAB022377.
HPA026896.
MIM154582. gene.
neXtProtNX_Q16706.
PharmGKBPA30573.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0383.
HOGENOMHOG000293253.
HOVERGENHBG052390.
InParanoidQ16706.
KOK01231.
OMAQIQPRMT.
OrthoDBEOG7JQBMJ.
PhylomeDBQ16706.
TreeFamTF313152.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ16706.
BgeeQ16706.
CleanExHS_MAN2A1.
GenevestigatorQ16706.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

GeneWikiMAN2A1.
GenomeRNAi4124.
NextBio16192.
PROQ16706.
SOURCESearch...

Entry information

Entry nameMA2A1_HUMAN
AccessionPrimary (citable) accession number: Q16706
Secondary accession number(s): Q16767
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 2 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 chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries