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O08912

- GALT1_MOUSE

UniProt

O08912 - GALT1_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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 Muc7.1 Publication

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei156 – 1561SubstrateBy similarity
    Binding sitei186 – 1861SubstrateBy similarity
    Metal bindingi209 – 2091Manganese1 Publication
    Metal bindingi211 – 2111Manganese1 Publication
    Binding sitei316 – 3161SubstrateBy similarity
    Metal bindingi344 – 3441Manganese1 Publication
    Binding sitei347 – 3471SubstrateBy similarity
    Binding sitei352 – 3521SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein O-linked glycosylation Source: MGI
    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_198517. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:894693. 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
    Mutagenesisi125 – 1251H → F: No effect. 1 Publication
    Mutagenesisi125 – 1251H → Q: Induces a strong decrease in activity. 1 Publication
    Mutagenesisi127 – 1271E → Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi150 – 1501E → Q: No effect. 1 Publication
    Mutagenesisi155 – 1551D → N: No effect; specificity not affected. 1 Publication
    Mutagenesisi156 – 1561D → Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi209 – 2091D → N, A or E: Loss of enzyme activity. 1 Publication
    Mutagenesisi211 – 2111H → A or D: Loss of enzyme activity. 1 Publication
    Mutagenesisi213 – 2131E → Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi310 – 3101D → N: Loss of enzyme activity. 1 Publication
    Mutagenesisi319 – 3191E → Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi320 – 3201N → A: No effect. 1 Publication
    Mutagenesisi322 – 3221E → Q: Loss of enzyme activity. 1 Publication
    Mutagenesisi341 – 3411H → A, L, V, K or R: Little or no effect. 1 Publication
    Mutagenesisi375 – 3751D → A or N: Little or no effect. 1 Publication
    Mutagenesisi376 – 3761E → Q: No effect. 1 Publication
    Mutagenesisi444 – 4441D → H: Induces a decrease in activity. 1 Publication
    Mutagenesisi455 – 4551G → V: Induces a slight decrease in activity. 1 Publication
    Mutagenesisi457 – 4571F → H: Induces a slight decrease in activity. 1 Publication
    Mutagenesisi460 – 4601H → K or N: Induces a slight decrease in activity. 1 Publication
    Mutagenesisi464 – 4641G → A: Induces a slight decrease in activity. 1 Publication
    Mutagenesisi465 – 4662NQ → QN: Induces a decrease in activity. 1 Publication
    Mutagenesisi465 – 4651N → A: Little or no effect. Induces a slight decrease in activity; when associated with A-466. 1 Publication
    Mutagenesisi466 – 4661Q → A: Little or no effect. Induces a slight decrease in activity; when associated with A-465. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223388Add
    BLAST
    Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012259Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi106 ↔ 3391 PublicationPROSITE-ProRule annotation
    Disulfide bondi330 ↔ 4081 PublicationPROSITE-ProRule annotation
    Disulfide bondi442 ↔ 4591 PublicationPROSITE-ProRule annotation
    Disulfide bondi482 ↔ 4971 PublicationPROSITE-ProRule annotation
    Disulfide bondi523 ↔ 5401 PublicationPROSITE-ProRule annotation
    Glycosylationi552 – 5521N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO08912.
    PaxDbiO08912.
    PRIDEiO08912.

    PTM databases

    PhosphoSiteiO08912.

    Expressioni

    Tissue specificityi

    Widely expressed at high level. Higher expression in kidney, heart, small intestine and cervix and to a lesser extent in all the other tissues tested.2 Publications

    Gene expression databases

    ArrayExpressiO08912.
    BgeeiO08912.
    GenevestigatoriO08912.

    Interactioni

    Protein-protein interaction databases

    IntActiO08912. 1 interaction.
    MINTiMINT-4095517.

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi104 – 1074
    Beta strandi118 – 1269
    Helixi129 – 14113
    Helixi145 – 1473
    Beta strandi148 – 1558
    Helixi161 – 1633
    Helixi165 – 1728
    Beta strandi173 – 1764
    Beta strandi178 – 1825
    Helixi189 – 19911
    Beta strandi202 – 21413
    Helixi219 – 22810
    Beta strandi232 – 24110
    Beta strandi243 – 2453
    Beta strandi255 – 2595
    Beta strandi265 – 2695
    Helixi272 – 2776
    Turni278 – 2803
    Beta strandi293 – 2997
    Helixi300 – 3056
    Helixi322 – 3298
    Beta strandi333 – 34513
    Helixi360 – 37314
    Helixi375 – 3784
    Helixi379 – 3835
    Helixi388 – 3903
    Helixi397 – 4059
    Helixi411 – 4177
    Beta strandi426 – 4327
    Beta strandi434 – 4363
    Turni437 – 4393
    Beta strandi441 – 4444
    Beta strandi455 – 4584
    Helixi464 – 4663
    Beta strandi468 – 4714
    Beta strandi476 – 4783
    Beta strandi481 – 4844
    Beta strandi493 – 4964
    Helixi502 – 5043
    Beta strandi506 – 5094
    Turni510 – 5134
    Beta strandi514 – 5207
    Beta strandi522 – 5265
    Beta strandi529 – 5313
    Beta strandi536 – 5394
    Helixi544 – 5463
    Beta strandi548 – 5503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XHBX-ray2.50A88-559[»]
    ProteinModelPortaliO08912.
    SMRiO08912. Positions 95-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08912.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini29 – 559531LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 2819Helical; 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.1 Publication
    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.
    InParanoidiO08912.
    KOiK00710.
    OMAiIKHDRKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiO08912.
    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.

    O08912-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKQER GLPAGDVLEL    50
    VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD 100
    VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 150
    IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 200
    RGQVITFLDA HCECTAGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA 250
    GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 300
    DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 350
    PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL 400
    GLRRKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 450
    NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 500
    KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC TGSRSQQWLL 550
    RNVTLPEIF 559
    Length:559
    Mass (Da):64,255
    Last modified:July 1, 1997 - v1
    Checksum:iAC5AB655D91F83E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811I → T in AAH56215. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73820 mRNA. Translation: AAB58477.1.
    BC056215 mRNA. Translation: AAH56215.1.
    BC090962 mRNA. Translation: AAH90962.1.
    CCDSiCCDS29100.1.
    RefSeqiNP_001153876.1. NM_001160404.1.
    NP_038842.3. NM_013814.3.
    XP_006525713.1. XM_006525650.1.
    UniGeneiMm.30249.

    Genome annotation databases

    EnsembliENSMUST00000000430; ENSMUSP00000000430; ENSMUSG00000000420.
    ENSMUST00000170243; ENSMUSP00000132142; ENSMUSG00000000420.
    ENSMUST00000178605; ENSMUSP00000137427; ENSMUSG00000000420.
    GeneIDi14423.
    KEGGimmu:14423.
    UCSCiuc008egq.2. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73820 mRNA. Translation: AAB58477.1 .
    BC056215 mRNA. Translation: AAH56215.1 .
    BC090962 mRNA. Translation: AAH90962.1 .
    CCDSi CCDS29100.1.
    RefSeqi NP_001153876.1. NM_001160404.1.
    NP_038842.3. NM_013814.3.
    XP_006525713.1. XM_006525650.1.
    UniGenei Mm.30249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XHB X-ray 2.50 A 88-559 [» ]
    ProteinModelPortali O08912.
    SMRi O08912. Positions 95-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O08912. 1 interaction.
    MINTi MINT-4095517.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei O08912.

    Proteomic databases

    MaxQBi O08912.
    PaxDbi O08912.
    PRIDEi O08912.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000430 ; ENSMUSP00000000430 ; ENSMUSG00000000420 .
    ENSMUST00000170243 ; ENSMUSP00000132142 ; ENSMUSG00000000420 .
    ENSMUST00000178605 ; ENSMUSP00000137427 ; ENSMUSG00000000420 .
    GeneIDi 14423.
    KEGGi mmu:14423.
    UCSCi uc008egq.2. mouse.

    Organism-specific databases

    CTDi 2589.
    MGIi MGI:894693. Galnt1.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi O08912.
    KOi K00710.
    OMAi IKHDRKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi O08912.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_198517. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT1. mouse.
    EvolutionaryTracei O08912.
    NextBioi 286021.
    PROi O08912.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08912.
    Bgeei O08912.
    Genevestigatori O08912.

    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. "cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
      Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A.
      J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Brain and Embryo.
    3. "Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold."
      Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A.
      J. Biol. Chem. 274:6797-6803(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF HIS-125; GLU-127; GLU-150; ASP-155; ASP-156; ASP-209; HIS-211; GLU-213; ASP-310; GLU-319; ASN-320; GLU-322; HIS-341; ASP-375; GLU-376; ASP-444; GLY-455; PHE-457; HIS-460; GLY-464; ASN-465 AND GLN-466.
    4. "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family."
      Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.
      Glycobiology 13:549-557(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    5. "The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1."
      Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A.
      Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559 IN COMPLEX WITH MANGANESE, GLYCOSYLATION AT ASN-552, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGALT1_MOUSE
    AccessioniPrimary (citable) accession number: O08912
    Secondary accession number(s): Q5BKS3, Q7TND1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 141 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3