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O02773

- MA1A1_PIG

UniProt

O02773 - MA1A1_PIG

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Protein
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
Gene
MAN1A1, MAN1A
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 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 By similarity.

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi639 – 6391Calcium By similarity

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

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei49 – 6921Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini70 – 659590Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
PRO_0000210310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi482 ↔ 514 By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004583.

Structurei

3D structure databases

ProteinModelPortaliO02773.
SMRiO02773. Positions 182-647.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
KOiK01230.

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.

O02773-1 [UniParc]FASTAAdd to Basket

« Hide

MPVGGLLPLF SSPAGGGLGG GLGGGLGGGG GGGGRKGSGP SAFRLTEKFV    50
LLLVFSAFIT LCFGAIFFLP DSSKLLSGVL FHSSPALQPA ADHKPGPGAR 100
AEDAADGRAR PGEEGAPGDP AAALEDNLAR IRENHERALM EAKETLQKLP 150
EEIQRDILME KEKVAQDQMS NRMGFRLPPV YLVPLIGAID REPADAAVRE 200
KRAKIKEMMK HAWNNYKLYA WGKNELKPVS KGGHSSSLFG NIKGATIVDA 250
LDTLFIMKMK NEFEEAKAWV EEHLNFNVNA EVSVFEVNIR FIGGLISAYY 300
LSGEEIFRKK AVELGVKLLP AFYTPSGIPW ALLNIKSGIG RNWPWASGGS 350
SILAEFGTLH LEFIHLSYLS GNPFFAEKVM NIRKVLNNLE KPQGLYPNYL 400
NPNSGQWGQY HVSVGGLGDS FYEYLLKAWL MSDKTDLEAK KMYFDAIKAI 450
ETHLIRKSRN GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL GADDAPDGLT 500
QHYLQLGAEI ARTCHESYSR TFVKLGPEAF RFDGGVEAIA TRQNEKYYIL 550
RPEVVETYLY MWRLTHDPKY RKWAWEAVEA LEKHCRVNGG YSGLRDVYVS 600
AQTYDDVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHPLPVLSRN 650
IKKVEDNEK 659
Length:659
Mass (Da):73,197
Last modified:July 1, 1997 - v1
Checksum:iAA7F17FEAAFE43A6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12503 mRNA. Translation: CAA73105.1.
PIRiS78554.
RefSeqiNP_999050.1. NM_213885.1.
UniGeneiSsc.14512.

Genome annotation databases

GeneIDi396919.
KEGGissc:396919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12503 mRNA. Translation: CAA73105.1 .
PIRi S78554.
RefSeqi NP_999050.1. NM_213885.1.
UniGenei Ssc.14512.

3D structure databases

ProteinModelPortali O02773.
SMRi O02773. Positions 182-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000004583.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396919.
KEGGi ssc:396919.

Organism-specific databases

CTDi 4121.

Phylogenomic databases

eggNOGi NOG300315.
HOGENOMi HOG000181988.
HOVERGENi HBG052389.
KOi K01230.

Enzyme and pathway databases

UniPathwayi UPA00378 .

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

  1. "Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells."
    Bieberich E., Treml K., Volker C., Rolfs A., Kalz-Fueller B., Bause E.
    Eur. J. Biochem. 246:681-689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
    Tissue: Liver.
  2. "Molecular cloning and primary structure of Man9-mannosidase from human kidney."
    Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B.
    Eur. J. Biochem. 217:535-540(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiMA1A1_PIG
AccessioniPrimary (citable) accession number: O02773
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 92 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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