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P28494 (MA2A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length489 AA.
Sequence statusFragment.
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. Ref.2 Ref.3

Subcellular location

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

Tissue specificity

All tissues, mostly in adrenal and thymus.

Post-translational modification

Glycosylated. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 489›489Alpha-mannosidase 2
PRO_0000206904

Sites

Active site2551Nucleophile By similarity
Metal binding1411Zinc By similarity
Metal binding1431Zinc By similarity
Metal binding2551Zinc By similarity

Amino acid modifications

Modified residue471Phosphoserine By similarity
Modified residue491Phosphoserine By similarity
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation601N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1241A → G AA sequence Ref.2
Sequence conflict1271W → I AA sequence Ref.2
Sequence conflict2111I → G AA sequence Ref.2
Sequence conflict2141G → K AA sequence Ref.2
Sequence conflict4601F → I AA sequence Ref.3
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P28494 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 8193E9CDAD3AFAF5

FASTA48956,736
        10         20         30         40         50         60 
GFSPHIIRVE RKGQLSILQE KIDHLERLLA ENNEIISNIR DSVINLSESV EDGPRGPAGN 

        70         80         90        100        110        120 
ASQGSAHLHS AQLALQADPK DCLFASQSGN QHRDVQMLDV YDLIPFDNPD GGVWKQGFDI 

       130        140        150        160        170        180 
KYEADEWDRE PLQVFVVPHS HNDPGWLKTF NDYFRDKTQY IFNNMVLKLK EDSSRKFIWS 

       190        200        210        220        230        240 
EISYLAKWWD IIDNPKKEAV KSLLQNGQLE IVTGGWVMAD EATTHYFALI DQLIEGHQWL 

       250        260        270        280        290        300 
EKNLGVKPRS GWAIDPFGHS PTMTYLLKRA GFSHMLIQRV HYSVKKHFSL QKTLEFFWRQ 

       310        320        330        340        350        360 
NWDLGSTTDI LCHMMPFYSY DIPHTCGPDP KICCQFDFKR LPGGRYGCPW GVPPEAISPG 

       370        380        390        400        410        420 
NVQSRAQMLL DQYRKKSKLF RTKVLLAPLG DDFRFSEYTE WDLQYRNYEQ LFSYMNSQPH 

       430        440        450        460        470        480 
LKVKIQFGTL SDYFDALEKS VAAEKKGGQS VFPALSGDFF TYADRDDHYW SGYFTSRPFY 


KRMDRIMEF

« Hide

References

[1]"Isolation of a rat liver Golgi mannosidase II clone by mixed oligonucleotide-primed amplification of cDNA."
Moremen K.W.
Proc. Natl. Acad. Sci. U.S.A. 86:5276-5280(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Mannosidase II and the 135-kDa Golgi-specific antigen recognized monoclonal antibody 53FC3 are the same dimeric protein."
Baron M.D., Garoff H.
J. Biol. Chem. 265:19928-19931(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 123-138 AND 210-223, SUBUNIT.
[3]"Novel purification of the catalytic domain of Golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme."
Moremen K.W., Touster O., Robbins P.W.
J. Biol. Chem. 266:16876-16885(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 74-103 AND 445-463, GLYCOSYLATION, SUBUNIT.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M24353 mRNA. Translation: AAA66457.1. Different termination.
IPIIPI00367150.
PIRA33901.
UniGeneRn.163804.

3D structure databases

ProteinModelPortalP28494.
SMRP28494. Positions 82-488.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4574652.
STRING10116.ENSRNOP00000020767.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

PTM databases

PhosphoSiteP28494.

Proteomic databases

PaxDbP28494.
PRIDEP28494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3038. rat.

Organism-specific databases

RGD3038. Man2a1.

Phylogenomic databases

eggNOGCOG0383.
HOGENOMHOG000293253.
HOVERGENHBG052390.
InParanoidP28494.
OrthoDBEOG4T782F.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressP28494.
GenevestigatorP28494.
GermOnlineENSRNOG00000015439. Rattus norvegicus.

Family and domain databases

Gene3D3.20.110.10. 1 hit.
InterProIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR000602. Glyco_hydro_38_N.
[Graphical view]
PfamPF01074. Glyco_hydro_38. 1 hit.
[Graphical view]
SUPFAMSSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNetSearch...

Other

ChEMBLCHEMBL2257.

Entry information

Entry nameMA2A1_RAT
AccessionPrimary (citable) accession number: P28494
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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