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P45700

- MA1A1_MOUSE

UniProt

P45700 - MA1A1_MOUSE

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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

Gene
Man1a1, Man1a
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Calcium.

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_198545. 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: Chromosome 10

Organism-specific databases

MGIiMGI:104677. Man1a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4343Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei44 – 6421Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini65 – 655591Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  2. Golgi membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP45700.
PaxDbiP45700.
PRIDEiP45700.

PTM databases

PhosphoSiteiP45700.

Expressioni

Gene expression databases

ArrayExpressiP45700.
BgeeiP45700.
CleanExiMM_MAN1A.
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 – 21625
Beta strandi219 – 2235
Turni224 – 2274
Beta strandi228 – 2303
Helixi233 – 2353
Helixi241 – 25212
Helixi256 – 26914
Beta strandi275 – 2795
Helixi280 – 29819
Helixi301 – 31414
Helixi315 – 3184
Beta strandi320 – 3234
Beta strandi327 – 3304
Turni331 – 3333
Helixi343 – 3453
Helixi349 – 3524
Helixi356 – 36611
Helixi370 – 38415
Helixi388 – 3903
Beta strandi394 – 3963
Turni398 – 4003
Turni412 – 4143
Helixi415 – 42713
Turni428 – 4303
Helixi433 – 44917
Beta strandi451 – 4533
Beta strandi459 – 4613
Beta strandi463 – 4653
Beta strandi468 – 4703
Beta strandi472 – 4743
Helixi476 – 4794
Helixi480 – 4867
Helixi496 – 51520
Beta strandi517 – 5215
Beta strandi524 – 5296
Beta strandi533 – 5353
Helixi539 – 5413
Helixi549 – 56113
Helixi564 – 58017
Beta strandi595 – 5973
Helixi606 – 6105
Helixi612 – 6198
Turni628 – 6303
Beta strandi631 – 6333
Beta strandi639 – 6413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NXCX-ray1.51A178-655[»]
ProteinModelPortaliP45700.
SMRiP45700. Positions 178-644.

Miscellaneous databases

EvolutionaryTraceiP45700.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiP45700.
KOiK01230.
OMAiMAQHYLE.
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

MPVGGLLPLF SSPGGGGLGS GLGGGLGGGR KGSGPAAFRL TEKFVLLLVF    50
SAFITLCFGA IFFLPDSSKL LSGVLFHSNP ALQPPAEHKP GLGARAEDAA 100
EGRVRHREEG APGDPGAGLE DNLARIRENH ERALREAKET LQKLPEEIQR 150
DILLEKEKVA QDQLRDKDLF RGLPKVDFLP PVGVENREPA DATIREKRAK 200
IKEMMTHAWN NYKRYAWGLN ELKPISKEGH SSSLFGNIKG ATIVDALDTL 250
FIMGMKTEFQ EAKSWIKKYL DFNVNAEVSV FEVNIRFVGG LLSAYYLSGE 300
EIFRKKAVEL GVKLLPAFHT PSGIPWALLN MKSGIGRNWP WASGGSSILA 350
EFGTLHLEFM HLSHLSGDPV FAEKVMKIRT VLNKLDKPEG LYPNYLNPSS 400
GQWGQHHVSV GGLGDSFYEY LLKAWLMSDK TDLEAKKMYF DAVQAIETHL 450
IRKSSGGLTY IAEWKGGLLE HKMGHLTCFA GGMFALGADG APEARAQHYL 500
ELGAEIARTC HESYNRTYVK LGPEAFRFDG GVEAIATRQN EKYYILRPEV 550
IETYMYMWRL THDPKYRTWA WEAVEALESH CRVNGGYSGL RDVYIARESY 600
DDVQQSFFLA ETLKYLYLIF SDDDLLPLEH WIFNTEAHPF PILREQKKEI 650
DGKEK 655
Length:655
Mass (Da):73,276
Last modified:November 1, 1995 - v1
Checksum:i15AF658364930BF4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006512569.1.
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:
EMBL
GenBank
DDBJ
Links Updated
U04299 mRNA. Translation: AAA17747.1 .
BC015265 mRNA. Translation: AAH15265.1 .
CCDSi CCDS23848.1.
PIRi A54408.
RefSeqi NP_032574.1. NM_008548.4.
XP_006512632.1. XM_006512569.1.
UniGenei Mm.117294.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NXC X-ray 1.51 A 178-655 [» ]
ProteinModelPortali P45700.
SMRi P45700. Positions 178-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P45700. 1 interaction.
MINTi MINT-1858603.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSitei P45700.

Proteomic databases

MaxQBi P45700.
PaxDbi P45700.
PRIDEi P45700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003843 ; ENSMUSP00000003843 ; ENSMUSG00000003746 .
ENSMUST00000105470 ; ENSMUSP00000101110 ; ENSMUSG00000003746 .
GeneIDi 17155.
KEGGi mmu:17155.
UCSCi uc007fbw.1. mouse.

Organism-specific databases

CTDi 17155.
MGIi MGI:104677. Man1a.

Phylogenomic databases

eggNOGi NOG300315.
HOGENOMi HOG000181988.
HOVERGENi HBG052389.
InParanoidi P45700.
KOi K01230.
OMAi MAQHYLE.
OrthoDBi EOG7X0VH1.
PhylomeDBi P45700.
TreeFami TF313420.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 3.2.1.113. 3474.
Reactomei REACT_198545. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

Miscellaneous databases

EvolutionaryTracei P45700.
NextBioi 291418.
PROi P45700.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45700.
Bgeei P45700.
CleanExi MM_MAN1A.
Genevestigatori P45700.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

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(1994) [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(2004) [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 (JAN-2009) 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(2004) [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: September 3, 2014
This is version 122 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

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