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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Mus musculus and UniProt Accession P45700
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3.2.1.113 mannosyl-oligosaccharide 1,2-alpha-mannosidaseIUBMB Comments
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al .
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naturalistic
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
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
mania, manic, mannosidase i, man1b1, man1a1, man9-mannosidase, man1c1, man1a2, golgi alpha-mannosidase i, mns1p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(alpha1,2)-mannosidase-I
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
alpha-1,2-mannosidase
-
-
-
-
alpha-1,2-mannosidase IC
-
-
-
-
ER alpha-1,2-mannosidase
-
-
-
-
exo-alpha-1,2-mannanase
-
-
-
-
glycoprotein processing mannosidase I
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-
-
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HMIC
-
-
-
-
Man(9)-alpha-mannosidase
-
-
-
-
Man9-mannosidase
-
-
-
-
Man9GlcNAc2-specific processing alpha-mannosidase
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-
-
-
mannose-9 processing alpha-mannosidase
-
-
-
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mannosidase 1A
-
-
-
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mannosidase 1B
-
-
-
-
mannosidase I
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-
-
-
mannosidase, exo-1,2-alpha-
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-
-
-
N-glycan processing class I alpha-1,2-mannosidase
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-
-
-
processing alpha-1,2-mannosidase IC
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein] alpha-2-mannohydrolase (configuration-inverting)
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7].
CAS REGISTRY NUMBER
COMMENTARY
9068-25-1
-
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
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + 4 H2O
alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + 4 beta-D-mannopyranose
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + 4 H2O
alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + 4 beta-D-mannopyranose
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the enzyme assumes an (alphaalpha)7 barrel structure with a Ca2+ ion coordinated at the bas of the barrel
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
In situ hybridization shows high levels of alpha1,2-mannosidase IA
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization
In situ hybridization shows high levels of alpha1,2-mannosidase IB
levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
In situ hybridization shows high levels of alpha1,2-mannosidase IB
In situ hybridization shows high levels of alpha1,2-mannosidase IB
In situ hybridization shows high levels of alpha1,2-mannosidase IB, Golgi alpha1,2-mannosidase IB
In situ hybridization shows high levels of alpha1,2-mannosidase IA
In situ hybridization shows high levels of alpha1,2-mannosidase IA
In situ hybridization shows high levels of alpha1,2-mannosidase IB
levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization. In situ hybridization shows high levels of alpha1,2-mannosidase IB
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hydridization
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
blocking alpha-1,2-mannosidase in regulatory T cells results in the migration of significantly lower numbers to the peripheral lymph nodes in skin grafted mice following adoptive transfer
physiological function
-
alpha-1,2-mannosidase function is not required for the suppressive capacity of regulatory T cells in vitro, but influences regulatory T cell adherence in vitro andmigration in vivo
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). MA1A1_MOUSE
655
2
73276
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F468L
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
M411T
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
additional information
additional information
-
alpha1,2-mannosidase IB null mice (-/-). Null mice with normal gross appearance at birth, but they display respiratory distress and die within a few hours with evident lung hemorrhage. Demonstrates the specific role of Golgi alpha1,2-mannosidase IB in pulmonary function and development. Histological comparison of lungs from wild type (+/+) and alpha1,2-mannosidase IB null mice (-/-)
additional information
alpha1,2-mannosidase IB null mice (-/-). Null mice with normal gross appearance at birth, but they display respiratory distress and die within a few hours with evident lung hemorrhage. Demonstrates the specific role of Golgi alpha1,2-mannosidase IB in pulmonary function and development. Histological comparison of lungs from wild type (+/+) and alpha1,2-mannosidase IB null mice (-/-)
additional information
alpha1,2-mannosidase IB null mice (-/-). Null mice with normal gross appearance at birth, but they display respiratory distress and die within a few hours with evident lung hemorrhage. Demonstrates the specific role of Golgi alpha1,2-mannosidase IB in pulmonary function and development. Histological comparison of lungs from wild type (+/+) and alpha1,2-mannosidase IB null mice (-/-)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-1,2-mannosidase expression increases in CD25+CD4+ regulatory T cells when they encounter alloantigen in vivo
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vallee, F.; Lal, A.; Moremen, K.W.; Howell, P.L.
Purification, crystallization and preliminary X-ray crystallographic analysis of recombinant murine Golgi mannosidase IA, a class I alpha-mannosidase involved in Asn-linked oligosaccharide maturation
Acta Crystallogr. Sect. D
55
571-573
1999
Mus musculus
Schneikert, J.; Herscovics, A.
Two naturally occurring mouse alpha-1,2-mannosidase IB cDNA clones differ in three point mutations. Mutation of Phe592 to Ser592 is sufficient to abolish enzyme activity
J. Biol. Chem.
270
17736-17740
1995
Mus musculus
Tempel, W.; Karaveg, K.; Liu, Z.J.; Rose, J.; Wang, B.C.; Moremen, K.W.
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases
J. Biol. Chem.
279
29774-29786
2004
Mus musculus (P45700)
Tremblay, L.O.; Nagy Kovacs, E.; Daniels, E.; Wong, N.K.; Sutton-Smith, M.; Morris, H.R.; Dell, A.; Marcinkiewicz, E.; Seidah, N.G.; McKerlie, C.; Herscovics, A.
Respiratory distress and neonatal lethality in mice lacking Golgi alpha1,2-mannosidase IB involved in N-glycan maturation
J. Biol. Chem.
282
2558-2566
2007
Mus musculus, Mus musculus (P39098), Mus musculus (P45700)
Mast, S.W.; Moremen, K.W.
Family 47 alpha-mannosidases in N-glycan processing
Methods Enzymol.
415
31-46
2006
Mus musculus (P45700)
Long, E.T.; Baker, S.; Oliveira, V.; Sawitzki, B.; Wood, K.J.
Alpha-1,2-mannosidase and hence N-glycosylation are required for regulatory T cell migration and allograft tolerance in mice
PLoS ONE
5
e8894
2010
Mus musculus
Lal, A.; Pang, P.; Kalelkar, S.; Romero, P.A.; Herscovics, A.; Moremen, K.W.
Substrate specificities of recombinant murine Golgi alpha-1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing alpha-1,2-mannosidases
Glycobiology
8
981-995
1998
Mus musculus (P39098), Mus musculus (P45700)
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