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Q07537

- GALT1_BOVIN

UniProt

Q07537 - GALT1_BOVIN

Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GALNT1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 Muc7.2 Publications

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.2 Publications

    Cofactori

    Manganese.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei141 – 1411Not glycosylatedCurated
    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: UniProtKB

    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

    BRENDAi2.4.1.41. 908.
    ReactomeiREACT_208023. 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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 24

    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
    Mutagenesisi95 – 951N → Q: Induces decrease in glycosylation. 1 Publication
    Mutagenesisi125 – 1251H → A: Induces a strong decrease in activity. 1 Publication
    Mutagenesisi137 – 1371H → A: No effect. 1 Publication
    Mutagenesisi141 – 1411N → Q: No effect. 1 Publication
    Mutagenesisi146 – 1461H → A: No effect. 1 Publication
    Mutagenesisi179 – 1791H → A: No effect. 1 Publication
    Mutagenesisi211 – 2111H → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi228 – 2281H → A: No effect. 1 Publication
    Mutagenesisi341 – 3411H → A: Induces a strong decrease in activity. 1 Publication
    Mutagenesisi344 – 3441H → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi404 – 4041H → A: No effect. 1 Publication
    Mutagenesisi427 – 4271H → A: No effect. 1 Publication
    Mutagenesisi460 – 4601H → A: No effect. 1 Publication
    Mutagenesisi498 – 4981H → A: No effect. 1 Publication
    Mutagenesisi499 – 4991H → A: No effect. 1 Publication
    Mutagenesisi517 – 5171H → A: No effect. 1 Publication
    Mutagenesisi552 – 5521N → Q: Induces decrease in glycosylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223386Add
    BLAST
    Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012255Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
    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...)1 Publication

    Post-translational modificationi

    N-glycosylated, contains two N-linked oligosaccharides.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ07537.

    Expressioni

    Tissue specificityi

    Colostrum contains a soluble form.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000014882.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07537.
    SMRiQ07537. 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

    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.By similarity
    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 By similarity.By similarity

    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.
    InParanoidiQ07537.
    KOiK00710.
    OMAiIKHDRKT.
    OrthoDBiEOG7J9VP2.
    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.

    Q07537-1 [UniParc]FASTAAdd to Basket

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    MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP    50
    VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD 100
    VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMLEE 150
    IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 200
    KGQVITFLDA HCECTVGWLE PLLARIKHDR KTVVCPIIDV ISDDTFEYMA 250
    GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 300
    DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 350
    PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL 400
    GLRHKLQCRP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 450
    NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 500
    KGNQLWEYDP VKLTLQHVNS NQCLDKATDE DSQVPSIRDC SGSRSQQWLL 550
    RNVTLPEIF 559
    Length:559
    Mass (Da):64,192
    Last modified:November 1, 1995 - v1
    Checksum:iE3E538C4DE569B40
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07780 mRNA. Translation: AAA30532.1.
    L17437 mRNA. Translation: AAA68489.1.
    PIRiA45987.
    RefSeqiNP_803485.1. NM_177519.2.
    UniGeneiBt.65693.

    Genome annotation databases

    EnsembliENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
    GeneIDi282241.
    KEGGibta:282241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07780 mRNA. Translation: AAA30532.1 .
    L17437 mRNA. Translation: AAA68489.1 .
    PIRi A45987.
    RefSeqi NP_803485.1. NM_177519.2.
    UniGenei Bt.65693.

    3D structure databases

    ProteinModelPortali Q07537.
    SMRi Q07537. Positions 95-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000014882.

    Protein family/group databases

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

    Proteomic databases

    PRIDEi Q07537.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000014882 ; ENSBTAP00000014882 ; ENSBTAG00000011206 .
    GeneIDi 282241.
    KEGGi bta:282241.

    Organism-specific databases

    CTDi 2589.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q07537.
    KOi K00710.
    OMAi IKHDRKT.
    OrthoDBi EOG7J9VP2.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 908.
    Reactomei REACT_208023. O-linked glycosylation of mucins.

    Miscellaneous databases

    NextBioi 20806060.

    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. "Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
      Homa F.L., Hollander T., Lehman D.J., Thomsen D.R., Elhammer A.P.
      J. Biol. Chem. 268:12609-12616(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 41-74.
      Tissue: Colostrum and Intestine.
    2. "Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase."
      Hagen F.K., van Wuyckhuyse B., Tabak L.A.
      J. Biol. Chem. 268:18960-18965(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-559, PARTIAL PROTEIN SEQUENCE.
      Tissue: Colostrum and Placenta.
    3. "Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells."
      Elhammer A., Kornfeld S.
      J. Biol. Chem. 261:5249-5255(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
    4. "Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1."
      Wragg S., Hagen F.K., Tabak L.A.
      Biochem. J. 328:193-197(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-95; HIS-125; HIS-137; ASN-141; HIS-146; HIS-179; HIS-211; HIS-228; HIS-341; HIS-344; HIS-404; HIS-427; HIS-460; HIS-498; HIS-499; HIS-517 AND ASN-552.

    Entry informationi

    Entry nameiGALT1_BOVIN
    AccessioniPrimary (citable) accession number: Q07537
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 124 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3