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P45701

- MA1A1_RABIT

UniProt

P45701 - MA1A1_RABIT

Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

Gene

MAN1A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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 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

    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: Unplaced

    Subcellular locationi

    GO - Cellular componenti

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

    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...

    Topological domain

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181988.
    HOVERGENiHBG052389.

    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

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    REPADAAVRE KRAKIKEMME HAWNSYKRYA WGLNELKPIT KEGHSSSLFG    50
    TIKGATIVDA LDTLFIMGME SEFQEAKSWI AENLDFNVNA EISVFEVNIR 100
    FVGGLLSAYY LSGEEIFRKK AVELGIKLLP AFHTPSGIPW ALLNIKSGIG 150
    RNWPWASGGS SILAEFGTLH LEFMHLSHLS GNPIFAEKVM NIRKVLNKLE 200
    KPEGLYPNYL NPSSGQWGQH HVSIGGLGDS FYEYLLKAWL MSEKTDLEAK 250
    KMYFDAVQAI ETHLIRKSSG GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL 300
    GADGAPEGRA QHYLELGAEI ARTCHESYNR TFMKLGPEAF RFDGGVEAIA 350
    TRQNEKYYIL RPEVVETYMY MWRLTHDPKY RKWAWEAVEA LESHCRVNGG 400
    YSGLRDVYFT HEKYDNVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE 450
    AHLLPILPTD QKEVEVKVK 469
    Length:469
    Mass (Da):53,427
    Last modified:November 1, 1995 - v1
    Checksum:iA1B9128144FD0D39
    GO

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04301 mRNA. Translation: AAA17748.1.
    UniGeneiOcu.6237.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04301 mRNA. Translation: AAA17748.1 .
    UniGenei Ocu.6237.

    3D structure databases

    ProteinModelPortali P45701.
    SMRi P45701. Positions 1-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000005793.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181988.
    HOVERGENi HBG052389.

    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. "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], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.

    Entry informationi

    Entry nameiMA1A1_RABIT
    AccessioniPrimary (citable) accession number: P45701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 96 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