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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

Gene

MAN1A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: 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

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi449 – 4491CalciumBy 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
Mannosidase alpha class 1A member 1
Processing alpha-1,2-mannosidase IA
Short name:
Alpha-1,2-mannosidase IA
Gene namesi
Name:MAN1A1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 469›469LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. Golgi membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 469›469Mannosyl-oligosaccharide 1,2-alpha-mannosidase IAPRO_0000210311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi292 ↔ 324By similarity
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005793.

Structurei

3D structure databases

ProteinModelPortaliP45701.
SMRiP45701. Positions 1-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiP45701.

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: Fragment.

P45701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
REPADAAVRE KRAKIKEMME HAWNSYKRYA WGLNELKPIT KEGHSSSLFG
60 70 80 90 100
TIKGATIVDA LDTLFIMGME SEFQEAKSWI AENLDFNVNA EISVFEVNIR
110 120 130 140 150
FVGGLLSAYY LSGEEIFRKK AVELGIKLLP AFHTPSGIPW ALLNIKSGIG
160 170 180 190 200
RNWPWASGGS SILAEFGTLH LEFMHLSHLS GNPIFAEKVM NIRKVLNKLE
210 220 230 240 250
KPEGLYPNYL NPSSGQWGQH HVSIGGLGDS FYEYLLKAWL MSEKTDLEAK
260 270 280 290 300
KMYFDAVQAI ETHLIRKSSG GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL
310 320 330 340 350
GADGAPEGRA QHYLELGAEI ARTCHESYNR TFMKLGPEAF RFDGGVEAIA
360 370 380 390 400
TRQNEKYYIL RPEVVETYMY MWRLTHDPKY RKWAWEAVEA LESHCRVNGG
410 420 430 440 450
YSGLRDVYFT HEKYDNVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE
460
AHLLPILPTD QKEVEVKVK
Length:469
Mass (Da):53,427
Last modified:October 31, 1995 - v1
Checksum:iA1B9128144FD0D39
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04301 mRNA. Translation: AAA17748.1.
UniGeneiOcu.6237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04301 mRNA. Translation: AAA17748.1.
UniGeneiOcu.6237.

3D structure databases

ProteinModelPortaliP45701.
SMRiP45701. Positions 1-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005793.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiP45701.

Enzyme and pathway databases

UniPathwayiUPA00378.

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

  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], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiMA1A1_RABIT
AccessioniPrimary (citable) accession number: P45701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: January 6, 2015
This is version 99 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

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.