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Information on EC 3.2.1.114 - mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase and Organism(s) Mus musculus and UniProt Accession P27046
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3.2.1.114 mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidaseIUBMB Comments
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
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Word Map
- 3.2.1.114
- swainsonine
-
n-linked
- n-glycans
- brefeldin
- castanospermine
-
endoglycosidase
-
asparagine-linked
-
high-mannose
-
hybrid-type
-
complex-type
- alpha-mannosidases
-
locoweed
-
indolizidine
- 1-deoxymannojirimycin
-
locoism
- kifunensine
- giantin
- medicine
-
swainsonine-treated
- man5glcnac
-
intra-golgi
- 1-deoxynojirimycin
- oxytropis
-
high-mannose-type
- beta-cop
- mannostatins
- glcnacman5glcnac2
- biotechnology
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mannosidase ii, jack bean alpha-mannosidase, man2a1, alpha-mannosidase iix, dgmii, manii, alpha-mii, drosophila gmii, alpha-d-mannosidase ii, afams1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-D-mannosidase II
-
-
-
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alpha-mannosidase II
alpha-mannosidase III
-
-
-
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alpha1-3,6-mannosidase
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-
-
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exo-1,3-1,6-alpha-mannosidase
-
-
-
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GlcNAc transferase I-dependent alpha1,3[alpha1,6]mannosidase
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-
-
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Golgi alpha-mannosidase II
-
-
-
-
Golgi mannosidase IIx
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close homolog to Golgi mannosidase II with different substrate specificity
Man II
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-
-
-
MAN IIx
-
-
-
-
ManIII
-
-
-
-
mannosidase II
-
-
-
-
mannosidase, exo-1,3-1,6-alpha-
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-
-
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mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
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-
-
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alpha-mannosidase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->6)-mannosyl-oligosaccharide alpha-D-mannohydrolase (configuration-retaining)
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
CAS REGISTRY NUMBER
COMMENTARY
349553-33-9
alpha-mannosidase III
82047-77-6
alpha-mannosidase II
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
?
4-methylumbelliferyl alpha-D-mannoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
-
?
D-Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
D-Manalpha(1-6)(GlcNAcbeta(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
-
-
-
?
GlcNAc(Man)5GlcNAc2 + H2O
GlcNAc(Man)3GlcNAc2 + D-mannose
-
alpha-mannosidase IIx protein
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-
?
additional information
?
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
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-
?
additional information
?
-
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Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
?
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
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-
?
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner
-
-
?
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner. Alpha-mannosidase IIx shows no reactivity to high-mannose-type carbohydrates
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
?
additional information
?
-
-
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
-
-
?
additional information
?
-
-
involved in trimming reactions in N-glycan maturation in the Golgi complex
-
-
?
additional information
?
-
-
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
endogenous enzyme in 3T3 cells and recombinant enzyme expressed in COS cells
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
cells selectively express alpha-mannosidase II, with minimal expression of its isozyme, alpha-mannosidase IIx
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
type II transmembrane protein with short cytoplasmic tail, single transmembrane domain and large C-terminal catalytic domain
-
type II transmembrane protein with short cytoplasmic tail, single transmembrane domain and large hydrophilic C-terminal domain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
alpha-mannosidase II deficiency has a minimal effect on N-glycan maturation in most cell types due to the compensation by alpha-mannosidase IIx, ablation of alpha-MII impairs the maturation of N-glycans in intestinal epithelial cells. alpha-mannosidase II (DELTA intestinal epithelial cell) mice are less susceptible to dextran sulfate sodium-induced colitis compared with control littermates. Neutrophil infiltration in the colonic mucosa is attenuated in alpha-mannosidase II (DELTA intestinal epithelial cell) mice. Gene expression levels of neutrophil-attracting chemokines are downregulated in the colonic tissue
physiological function
the enzyme plays a crucial, but not exclusive, role in the maturation of N-glycans. Intestinal epithelial cell alpha-mannosidase II promotes intestinal inflammation by facilitating chemokine expression
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MA2A1_MOUSE
1150
1
131631
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
addition of asparagine-linked oligosaccharides, not O-glycosylated
lipoprotein
-
[3H]palmitate can be incorporated into enzyme, glycosylation is not required for fatty acid attachment
additional information
-
study of posttanslational modifications, sulfate is attached to N-linked oligosaccharide, no proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutants without GlcNAc(Man)5(GlcNAc)2 activity, Golgi mannosidase II-null mice phenotype
additional information
-
MII/alpha-mannosidase IIx double knockout mice synthesize no complex-type N-glycans
additional information
-
MII/alpha-mannosidase IIx double knockout mice, completely lack complex-type N-glycans, some double-nulls die between embryonic days 15.5 and 18.5, but most survive until shortly after birth and die of respiratory failure. Alpha-mannosidase IIx-null mice are mainly complex-type and also contain high-mannose-type but not significant levels of hybrid-type N-glycans. In contrast, MII-null embryos show high levels of hybrid-type N-glycans and reduced levels of complex-type N-glycans
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length cDNA is cloned and sequenced, 8-12fold overexpression in COS cells
cDNA fragments encoding full-length enzymes subcloned into the pcDNA3.1 mammalian expression vector. cDNA fragments encoding soluble forms of enzymes subcloned into pcDNA-HSH. Full-length alpha-mannosidase IIx expressed in MII/alpha-mannosidase IIx double-null fibroblasts. Soluble recombinant alpha-mannosidase IIx expressed in COS cells
-
pcDNA-HSH-MX expression vector encoding the soluble alpha-mannosidase IIx, transfection into Cos-1 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
single nucleotide polymorphisms in MAN2A1 may be a genetic factor for inflammatory bowel disease
medicine
medicine
-
enzyme deficiency causes congenital dyserythropoietic anemia with splenomegaly and various additional abnormalities and complications
medicine
-
alpha-mannosidase IIx is an isozyme of MII. Either MII or alpha-mannosidase IIx can biochemically compensate for the deficiency of the other in vivo, and either of two is required for late embryonic and early postnatal development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moremen, K.W.; Touster, O.
Biosynthesis and modification of Golgi mannosidase II in HeLa and 3T3 cells
J. Biol. Chem.
260
6654-6662
1985
Homo sapiens, Mus musculus, Rattus norvegicus
Moremen, K.W.; Robbins, P.W.
Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
J. Cell Biol.
115
1521-1534
1991
Homo sapiens, Mus musculus (P27046), Mus musculus, Rattus norvegicus
Foster, J.M.; Yudkin, B.; Lockyer, A.E.; Roberts, D.B.
Cloning and sequence analysis of GmII, a Drosophila melanogaster homologue of the cDNA encoding murine Golgi alpha-mannosidase II
Gene
154
183-186
1995
Drosophila melanogaster (Q24451), Drosophila melanogaster, Mus musculus
Moremen, K.W.
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals
Biochim. Biophys. Acta
1573
225-235
2002
Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Akama, T.O.; Fukuda, M.N.
N-Glycan structure analysis using lectins and an alpha-mannosidase activity assay
Methods Enzymol.
416
304-314
2006
Mus musculus
Akama, T.O.; Nakagawa, H.; Wong, N.K.; Sutton-Smith, M.; Dell, A.; Morris, H.R.; Nakayama, J.; Nishimura, S.; Pai, A.; Moremen, K.W.; Marth, J.D.; Fukuda, M.N.
Essential and mutually compensatory roles of {alpha}-mannosidase II and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
Proc. Natl. Acad. Sci. USA
103
8983-8988
2006
Mus musculus
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