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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

Gene

Man1a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactori

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi635 – 6351Calcium

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.113. 3474.
ReactomeiREACT_343896. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Man1a1
Synonyms:Man1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:104677. Man1a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4343CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei44 – 6421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini65 – 655591LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. Golgi apparatus Source: MGI
  5. Golgi membrane Source: MGI
  6. integral component of membrane Source: UniProtKB-KW
  7. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Mannosyl-oligosaccharide 1,2-alpha-mannosidase IAPRO_0000210309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi478 ↔ 5101 Publication
Glycosylationi515 – 5151N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-linked glycan at Asn-515 consists of Man(6)-GlcNAc2.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP45700.
PaxDbiP45700.
PRIDEiP45700.

PTM databases

PhosphoSiteiP45700.

Expressioni

Gene expression databases

BgeeiP45700.
CleanExiMM_MAN1A.
ExpressionAtlasiP45700. baseline and differential.
GenevestigatoriP45700.

Interactioni

Protein-protein interaction databases

IntActiP45700. 1 interaction.
MINTiMINT-1858603.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi192 – 21625Combined sources
Beta strandi219 – 2235Combined sources
Turni224 – 2274Combined sources
Beta strandi228 – 2303Combined sources
Helixi233 – 2353Combined sources
Helixi241 – 25212Combined sources
Helixi256 – 26914Combined sources
Beta strandi275 – 2795Combined sources
Helixi280 – 29819Combined sources
Helixi301 – 31414Combined sources
Helixi315 – 3184Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi327 – 3304Combined sources
Turni331 – 3333Combined sources
Helixi343 – 3453Combined sources
Helixi349 – 3524Combined sources
Helixi356 – 36611Combined sources
Helixi370 – 38415Combined sources
Helixi388 – 3903Combined sources
Beta strandi394 – 3963Combined sources
Turni398 – 4003Combined sources
Turni412 – 4143Combined sources
Helixi415 – 42713Combined sources
Turni428 – 4303Combined sources
Helixi433 – 44917Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi459 – 4613Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi468 – 4703Combined sources
Beta strandi472 – 4743Combined sources
Helixi476 – 4794Combined sources
Helixi480 – 4867Combined sources
Helixi496 – 51520Combined sources
Beta strandi517 – 5215Combined sources
Beta strandi524 – 5296Combined sources
Beta strandi533 – 5353Combined sources
Helixi539 – 5413Combined sources
Helixi549 – 56113Combined sources
Helixi564 – 58017Combined sources
Beta strandi595 – 5973Combined sources
Helixi606 – 6105Combined sources
Helixi612 – 6198Combined sources
Turni628 – 6303Combined sources
Beta strandi631 – 6333Combined sources
Beta strandi639 – 6413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NXCX-ray1.51A178-655[»]
ProteinModelPortaliP45700.
SMRiP45700. Positions 178-644.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45700.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiP45700.
KOiK01230.
OMAiAWEAVEX.
OrthoDBiEOG7X0VH1.
PhylomeDBiP45700.
TreeFamiTF313420.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

P45700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVGGLLPLF SSPGGGGLGS GLGGGLGGGR KGSGPAAFRL TEKFVLLLVF
60 70 80 90 100
SAFITLCFGA IFFLPDSSKL LSGVLFHSNP ALQPPAEHKP GLGARAEDAA
110 120 130 140 150
EGRVRHREEG APGDPGAGLE DNLARIRENH ERALREAKET LQKLPEEIQR
160 170 180 190 200
DILLEKEKVA QDQLRDKDLF RGLPKVDFLP PVGVENREPA DATIREKRAK
210 220 230 240 250
IKEMMTHAWN NYKRYAWGLN ELKPISKEGH SSSLFGNIKG ATIVDALDTL
260 270 280 290 300
FIMGMKTEFQ EAKSWIKKYL DFNVNAEVSV FEVNIRFVGG LLSAYYLSGE
310 320 330 340 350
EIFRKKAVEL GVKLLPAFHT PSGIPWALLN MKSGIGRNWP WASGGSSILA
360 370 380 390 400
EFGTLHLEFM HLSHLSGDPV FAEKVMKIRT VLNKLDKPEG LYPNYLNPSS
410 420 430 440 450
GQWGQHHVSV GGLGDSFYEY LLKAWLMSDK TDLEAKKMYF DAVQAIETHL
460 470 480 490 500
IRKSSGGLTY IAEWKGGLLE HKMGHLTCFA GGMFALGADG APEARAQHYL
510 520 530 540 550
ELGAEIARTC HESYNRTYVK LGPEAFRFDG GVEAIATRQN EKYYILRPEV
560 570 580 590 600
IETYMYMWRL THDPKYRTWA WEAVEALESH CRVNGGYSGL RDVYIARESY
610 620 630 640 650
DDVQQSFFLA ETLKYLYLIF SDDDLLPLEH WIFNTEAHPF PILREQKKEI

DGKEK
Length:655
Mass (Da):73,276
Last modified:November 1, 1995 - v1
Checksum:i15AF658364930BF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04299 mRNA. Translation: AAA17747.1.
BC015265 mRNA. Translation: AAH15265.1.
CCDSiCCDS23848.1.
PIRiA54408.
RefSeqiNP_032574.1. NM_008548.4.
XP_006512632.1. XM_006512569.2.
UniGeneiMm.117294.

Genome annotation databases

EnsembliENSMUST00000003843; ENSMUSP00000003843; ENSMUSG00000003746.
ENSMUST00000105470; ENSMUSP00000101110; ENSMUSG00000003746.
GeneIDi17155.
KEGGimmu:17155.
UCSCiuc007fbw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04299 mRNA. Translation: AAA17747.1.
BC015265 mRNA. Translation: AAH15265.1.
CCDSiCCDS23848.1.
PIRiA54408.
RefSeqiNP_032574.1. NM_008548.4.
XP_006512632.1. XM_006512569.2.
UniGeneiMm.117294.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NXCX-ray1.51A178-655[»]
ProteinModelPortaliP45700.
SMRiP45700. Positions 178-644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45700. 1 interaction.
MINTiMINT-1858603.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteiP45700.

Proteomic databases

MaxQBiP45700.
PaxDbiP45700.
PRIDEiP45700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003843; ENSMUSP00000003843; ENSMUSG00000003746.
ENSMUST00000105470; ENSMUSP00000101110; ENSMUSG00000003746.
GeneIDi17155.
KEGGimmu:17155.
UCSCiuc007fbw.1. mouse.

Organism-specific databases

CTDi17155.
MGIiMGI:104677. Man1a.

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiP45700.
KOiK01230.
OMAiAWEAVEX.
OrthoDBiEOG7X0VH1.
PhylomeDBiP45700.
TreeFamiTF313420.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.113. 3474.
ReactomeiREACT_343896. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

Miscellaneous databases

EvolutionaryTraceiP45700.
NextBioi291418.
PROiP45700.
SOURCEiSearch...

Gene expression databases

BgeeiP45700.
CleanExiMM_MAN1A.
ExpressionAtlasiP45700. baseline and differential.
GenevestigatoriP45700.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides."
    Lal A., Schutzbach J.S., Forsee W.T., Neame P.J., Moremen K.W.
    J. Biol. Chem. 269:9872-9881(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 424-437, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases."
    Tempel W., Karaveg K., Liu Z.-J., Rose J., Wang B.C., Moremen K.W.
    J. Biol. Chem. 279:29774-29786(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 178-655, DISULFIDE BOND, CALCIUM-BINDING SITE, GLYCOSYLATION AT ASN-515.

Entry informationi

Entry nameiMA1A1_MOUSE
AccessioniPrimary (citable) accession number: P45700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.