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P27115

- MGAT1_RABIT

UniProt

P27115 - MGAT1_RABIT

Protein

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Gene

MGAT1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

    Cofactori

    Manganese. The cofactor is mostly bound to the substrate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171Substrate
    Binding sitei144 – 1441Substrate
    Binding sitei190 – 1901Substrate
    Binding sitei212 – 2121Substrate
    Metal bindingi213 – 2131Manganese
    Active sitei291 – 2911Proton acceptorSequence Analysis
    Binding sitei322 – 3221Substrate

    GO - Molecular functioni

    1. alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. protein N-acetylglucosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. mannose metabolic process Source: UniProtKB
    2. protein N-linked glycosylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT13. Glycosyltransferase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC:2.4.1.101)
    Alternative name(s):
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
    Short name:
    GNT-I
    Short name:
    GlcNAc-T I
    Gene namesi
    Name:MGAT1
    Synonyms:GNT1
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi medial cisterna Source: UniProtKB
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000191387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi115 ↔ 145
    Disulfide bondi239 ↔ 305

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Appears to be present in all tissues.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi110 – 1167
    Helixi120 – 13011
    Turni134 – 1363
    Beta strandi139 – 1435
    Helixi148 – 1558
    Helixi156 – 1605
    Beta strandi161 – 1655
    Helixi179 – 1813
    Helixi182 – 19918
    Beta strandi205 – 2117
    Beta strandi214 – 2163
    Helixi220 – 23314
    Beta strandi237 – 2426
    Helixi249 – 2513
    Beta strandi260 – 2656
    Beta strandi269 – 2746
    Helixi275 – 2817
    Helixi282 – 2843
    Helixi290 – 2945
    Helixi297 – 3004
    Beta strandi304 – 31512
    Beta strandi318 – 3225
    Helixi325 – 3295
    Helixi331 – 3333
    Helixi343 – 3453
    Helixi349 – 3513
    Helixi353 – 36614
    Helixi372 – 3765
    Beta strandi384 – 3896
    Helixi393 – 40210
    Beta strandi421 – 4266
    Beta strandi429 – 4346

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FO8X-ray1.40A106-447[»]
    1FO9X-ray1.50A106-447[»]
    1FOAX-ray1.80A106-447[»]
    2AM3X-ray1.80A106-447[»]
    2AM4X-ray1.70A106-447[»]
    2AM5X-ray1.60A106-447[»]
    2APCX-ray1.50A106-447[»]
    ProteinModelPortaliP27115.
    SMRiP27115. Positions 106-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27115.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 447418LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG052466.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR004139. Glyco_trans_13.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR10468. PTHR10468. 1 hit.
    PfamiPF03071. GNT-I. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27115-1 [UniParc]FASTAAdd to Basket

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    MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPVPSRLPSD NALDDDPASL    50
    TREVIRLAQD AEVELERQRG LLQQIREHHA LWSQRWKVPT AAPPAQPHVP 100
    VTPPPAVIPI LVIACDRSTV RRCLDKLLHY RPSAELFPII VSQDCGHEET 150
    AQVIASYGSA VTHIRQPDLS NIAVQPDHRK FQGYYKIARH YRWALGQIFH 200
    NFNYPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV SAWNDNGKEQ 250
    MVDSSKPELL YRTDFFPGLG WLLLAELWAE LEPKWPKAFW DDWMRRPEQR 300
    KGRACVRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY 350
    LQQEAYDRDF LARVYGAPQL QVEKVRTNDR KELGEVRVQY TGRDSFKAFA 400
    KALGVMDDLK SGVPRAGYRG IVTFLFRGRR VHLAPPQTWD GYDPSWT 447
    Length:447
    Mass (Da):51,540
    Last modified:August 1, 1992 - v1
    Checksum:i18AC90994F0EB435
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57301 mRNA. Translation: AAA31493.1.
    PIRiA38561.
    RefSeqiNP_001076214.1. NM_001082745.1.
    UniGeneiOcu.1975.

    Genome annotation databases

    GeneIDi100009521.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57301 mRNA. Translation: AAA31493.1 .
    PIRi A38561.
    RefSeqi NP_001076214.1. NM_001082745.1.
    UniGenei Ocu.1975.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FO8 X-ray 1.40 A 106-447 [» ]
    1FO9 X-ray 1.50 A 106-447 [» ]
    1FOA X-ray 1.80 A 106-447 [» ]
    2AM3 X-ray 1.80 A 106-447 [» ]
    2AM4 X-ray 1.70 A 106-447 [» ]
    2AM5 X-ray 1.60 A 106-447 [» ]
    2APC X-ray 1.50 A 106-447 [» ]
    ProteinModelPortali P27115.
    SMRi P27115. Positions 106-447.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT13. Glycosyltransferase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009521.

    Organism-specific databases

    CTDi 4245.

    Phylogenomic databases

    HOVERGENi HBG052466.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    EvolutionaryTracei P27115.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR004139. Glyco_trans_13.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR10468. PTHR10468. 1 hit.
    Pfami PF03071. GNT-I. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans: UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I."
      Sarkar M., Hull E., Nishikawa Y., Simpson R.J., Moritz R.L., Dunn R., Schachter H.
      Proc. Natl. Acad. Sci. U.S.A. 88:234-238(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues."
      Gordon R.D., Sivarajah P., Satkunarajah M., Ma D., Tarling C.A., Vizitiu D., Withers S.G., Rini J.M.
      J. Mol. Biol. 360:67-79(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 106-447 IN COMPLEX WITH SUBSTRATE ANALOGS, MANGANESE-BINDING SITE, DISULFIDE BONDS.
    3. "X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily."
      Unligil U.M., Zhou S., Yuwaraj S., Sarkar M., Schachter H., Rini J.M.
      EMBO J. 19:5269-5280(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 106-447 ALONE AND IN COMPLEX WITH UDP-GLCNAC, ACTIVE SITE, COFACTOR, MANGANESE-BINDING SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiMGAT1_RABIT
    AccessioniPrimary (citable) accession number: P27115
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3