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Q10473

- GALT1_RAT

UniProt

Q10473 - GALT1_RAT

Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

    Cofactori

    Manganese.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei156 – 1561SubstrateBy similarity
    Binding sitei186 – 1861SubstrateBy similarity
    Metal bindingi209 – 2091ManganeseBy similarity
    Metal bindingi211 – 2111ManganeseBy similarity
    Binding sitei316 – 3161SubstrateBy similarity
    Metal bindingi344 – 3441ManganeseBy similarity
    Binding sitei347 – 3471SubstrateBy similarity
    Binding sitei352 – 3521SubstrateBy similarity

    GO - Molecular functioni

    1. manganese ion binding Source: UniProtKB
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: RGD

    GO - Biological processi

    1. protein O-linked glycosylation Source: UniProtKB
    2. protein O-linked glycosylation via serine Source: Ensembl
    3. protein O-linked glycosylation via threonine Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196259. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 1 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 1
    Short name:
    GalNAc-T1
    Short name:
    pp-GaNTase 1
    Protein-UDP acetylgalactosaminyltransferase 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
    Cleaved into the following chain:
    Gene namesi
    Name:Galnt1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 18

    Organism-specific databases

    RGDi620358. Galnt1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi212 – 2121C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication
    Mutagenesisi214 – 2141C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication
    Mutagenesisi235 – 2351C → A: No effect. 1 Publication
    Mutagenesisi330 – 3301C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi339 – 3391C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi408 – 4081C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi442 – 4421C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi444 – 4441D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. 2 Publications
    Mutagenesisi455 – 4551G → Q: Induces a decrease in activity. 1 Publication
    Mutagenesisi457 – 4571F → A: Little or no effect. 1 Publication
    Mutagenesisi459 – 4591C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi465 – 4651N → A: Little or no effect. 1 Publication
    Mutagenesisi466 – 4661Q → A: Induces a decrease in activity. 1 Publication
    Mutagenesisi468 – 4681F → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi468 – 4681F → W or Y: Little or no effect. 1 Publication
    Mutagenesisi482 – 4821C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi484 – 4841D → A: Loss of enzyme activity; when associated with A-444 and A-525. 2 Publications
    Mutagenesisi497 – 4971C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi523 – 5231C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi525 – 5251D → A: Loss of enzyme activity; when associated with A-444 and A-484. 2 Publications
    Mutagenesisi540 – 5401C → A: Loss of enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223390Add
    BLAST
    Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012263Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi106 ↔ 339PROSITE-ProRule annotation
    Disulfide bondi330 ↔ 408PROSITE-ProRule annotation
    Disulfide bondi442 ↔ 459PROSITE-ProRule annotation
    Disulfide bondi482 ↔ 497PROSITE-ProRule annotation
    Disulfide bondi523 ↔ 540PROSITE-ProRule annotation
    Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ10473.
    PRIDEiQ10473.

    Expressioni

    Tissue specificityi

    Heart, brain, spleen, liver, skeletal muscle and kidney.

    Gene expression databases

    GenevestigatoriQ10473.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4566270.
    STRINGi10116.ENSRNOP00000022117.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10473.
    SMRiQ10473. Positions 95-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini29 – 559531LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini429 – 551123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni115 – 225111Catalytic subdomain AAdd
    BLAST
    Regioni285 – 34763Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
    The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG239675.
    GeneTreeiENSGT00750000117385.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ10473.
    KOiK00710.
    OMAiIKHDRKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ10473.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q10473-1 [UniParc]FASTAAdd to Basket

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    MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL    50
    VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD 100
    VRLEGCKTKV YPDSLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 150
    IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 200
    KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA 250
    GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 300
    DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 350
    PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV 400
    GLRHKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 450
    NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 500
    KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC TGSRSQQWLL 550
    RNVTLPEIF 559
    Length:559
    Mass (Da):64,229
    Last modified:October 1, 1996 - v1
    Checksum:i5E36A95D9422C853
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35890 mRNA. Translation: AAC52511.1.
    RefSeqiNP_077349.1. NM_024373.1.
    XP_006254533.1. XM_006254471.1.
    UniGeneiRn.10266.

    Genome annotation databases

    EnsembliENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207.
    GeneIDi79214.
    KEGGirno:79214.
    UCSCiRGD:620358. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35890 mRNA. Translation: AAC52511.1 .
    RefSeqi NP_077349.1. NM_024373.1.
    XP_006254533.1. XM_006254471.1.
    UniGenei Rn.10266.

    3D structure databases

    ProteinModelPortali Q10473.
    SMRi Q10473. Positions 95-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4566270.
    STRINGi 10116.ENSRNOP00000022117.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Proteomic databases

    PaxDbi Q10473.
    PRIDEi Q10473.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022117 ; ENSRNOP00000022117 ; ENSRNOG00000016207 .
    GeneIDi 79214.
    KEGGi rno:79214.
    UCSCi RGD:620358. rat.

    Organism-specific databases

    CTDi 2589.
    RGDi 620358. Galnt1.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q10473.
    KOi K00710.
    OMAi IKHDRKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q10473.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_196259. O-linked glycosylation of mucins.

    Miscellaneous databases

    NextBioi 614616.
    PROi Q10473.

    Gene expression databases

    Genevestigatori Q10473.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
      Hagen F., Gregorie C.A., Tabak L.A.
      Glycoconj. J. 12:901-909(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Sublingual gland.
    2. "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)."
      Tenno M., Toba S., Kezdy F.J., Elhammer A.P., Kurosaka A.
      Eur. J. Biochem. 269:4308-4316(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-106; CYS-212; CYS-214; CYS-235; CYS-330; CYS-339 AND CYS-408.
    3. "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites."
      Tenno M., Saeki A., Kezdy F.J., Elhammer A.P., Kurosaka A.
      J. Biol. Chem. 277:47088-47096(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-442; ASP-444; GLY-455; PHE-457; CYS-459; ASN-465; GLN-466; PHE-468; CYS-482; ASP-484; CYS-497; CYS-523; ASP-525 AND CYS-540.
    4. "Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1."
      Tenno M., Kezdy F.J., Elhammer A.P., Kurosaka A.
      Biochem. Biophys. Res. Commun. 298:755-759(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.

    Entry informationi

    Entry nameiGALT1_RAT
    AccessioniPrimary (citable) accession number: Q10473
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 123 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3