Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8C7U7

- GALT6_MOUSE

UniProt

Q8C7U7 - GALT6_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 6

Gene

Galnt6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171SubstrateBy similarity
    Binding sitei246 – 2461SubstrateBy similarity
    Metal bindingi269 – 2691ManganeseBy similarity
    Metal bindingi271 – 2711ManganeseBy similarity
    Binding sitei379 – 3791SubstrateBy similarity
    Metal bindingi407 – 4071ManganeseBy similarity
    Binding sitei410 – 4101SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    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 6 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 6
    Short name:
    GalNAc-T6
    Short name:
    pp-GaNTase 6
    Protein-UDP acetylgalactosaminyltransferase 6
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
    Gene namesi
    Name:Galnt6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1891640. Galnt6.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 622622Polypeptide N-acetylgalactosaminyltransferase 6PRO_0000059115Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi165 ↔ 402PROSITE-ProRule annotation
    Disulfide bondi393 ↔ 474PROSITE-ProRule annotation
    Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi509 ↔ 527PROSITE-ProRule annotation
    Disulfide bondi553 ↔ 566PROSITE-ProRule annotation
    Disulfide bondi597 ↔ 610PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8C7U7.
    PaxDbiQ8C7U7.
    PRIDEiQ8C7U7.

    PTM databases

    PhosphoSiteiQ8C7U7.

    Expressioni

    Gene expression databases

    BgeeiQ8C7U7.
    GenevestigatoriQ8C7U7.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000056705.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C7U7.
    SMRiQ8C7U7. Positions 117-621.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini29 – 622594LumenalSequence 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
    Domaini496 – 622127Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni176 – 285110Catalytic subdomain AAdd
    BLAST
    Regioni348 – 41063Catalytic 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 binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG239675.
    GeneTreeiENSGT00750000117451.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ0VE84.
    KOiK00710.
    OMAiNQCLDVG.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8C7U7.
    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.

    Q8C7U7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK    50
    DQVLDFMLGA VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK 100
    PFWDRPPQDP NSPGADGKAF QKKEWTNLET KEKEEGYKKH CFNAFASDRI 150
    SLQRSLGPDT RPPECVDQKF RRCPPLPTTS VIIVFHNEAW STLLRTVYSV 200
    LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV VRQRERKGLI 250
    TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT 300
    IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK 350
    SPTFAGGLFS ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII 400
    PCSVVGHVFR TKSPHTFPKG TSVIARNQVR LAEVWMDDYK KIFYRRNLQA 450
    AKMVQENNFG DISERLRLRE QLRCHNFSWY LHNVYPEMFV PDLNPTFYGA 500
    IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS QRDLRHNIGK 550
    QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS 600
    QDKKPAMAPC NPRDPYQLWL FV 622
    Length:622
    Mass (Da):71,537
    Last modified:March 1, 2003 - v1
    Checksum:i6DBCA3A2CCFDBDAA
    GO

    Sequence cautioni

    The sequence CAB55352.1 differs from that shown. Reason: Frameshift at position 622.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141A → T in CAB55352. (PubMed:10464263)Curated
    Sequence conflicti100 – 1001K → R in CAB55352. (PubMed:10464263)Curated
    Sequence conflicti210 – 2101K → N in BAC25984. (PubMed:16141072)Curated
    Sequence conflicti215 – 2151V → M in BAC25984. (PubMed:16141072)Curated
    Sequence conflicti247 – 2471K → G in BAC25984. (PubMed:16141072)Curated
    Sequence conflicti263 – 27513EVLTF…HCECF → KGAHVSWTPTVSVS(PubMed:10464263)CuratedAdd
    BLAST
    Sequence conflicti292 – 2921A → P in CAB55352. (PubMed:10464263)Curated
    Sequence conflicti336 – 3361E → Q in CAB55352. (PubMed:10464263)Curated
    Sequence conflicti398 – 3981E → G in BAC25984. (PubMed:16141072)Curated
    Sequence conflicti467 – 4671R → Q in CAB55352. (PubMed:10464263)Curated
    Sequence conflicti562 – 5621G → S in CAB55352. (PubMed:10464263)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133523 mRNA. Translation: CAB55352.1. Frameshift.
    AK028506 mRNA. Translation: BAC25984.1.
    AK049222 mRNA. Translation: BAC33618.1.
    AK155008 mRNA. Translation: BAE32989.1.
    AK159721 mRNA. Translation: BAE35316.1.
    BC119324 mRNA. Translation: AAI19325.1.
    BC119326 mRNA. Translation: AAI19327.1.
    CCDSiCCDS27843.1.
    RefSeqiNP_001155239.1. NM_001161767.1.
    NP_001155240.1. NM_001161768.1.
    NP_766039.2. NM_172451.3.
    UniGeneiMm.22969.

    Genome annotation databases

    EnsembliENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
    ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
    ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
    GeneIDi207839.
    KEGGimmu:207839.
    UCSCiuc007xrz.2. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 6

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133523 mRNA. Translation: CAB55352.1 . Frameshift.
    AK028506 mRNA. Translation: BAC25984.1 .
    AK049222 mRNA. Translation: BAC33618.1 .
    AK155008 mRNA. Translation: BAE32989.1 .
    AK159721 mRNA. Translation: BAE35316.1 .
    BC119324 mRNA. Translation: AAI19325.1 .
    BC119326 mRNA. Translation: AAI19327.1 .
    CCDSi CCDS27843.1.
    RefSeqi NP_001155239.1. NM_001161767.1.
    NP_001155240.1. NM_001161768.1.
    NP_766039.2. NM_172451.3.
    UniGenei Mm.22969.

    3D structure databases

    ProteinModelPortali Q8C7U7.
    SMRi Q8C7U7. Positions 117-621.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000056705.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8C7U7.

    Proteomic databases

    MaxQBi Q8C7U7.
    PaxDbi Q8C7U7.
    PRIDEi Q8C7U7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052069 ; ENSMUSP00000056705 ; ENSMUSG00000037280 .
    ENSMUST00000159715 ; ENSMUSP00000123848 ; ENSMUSG00000037280 .
    ENSMUST00000161514 ; ENSMUSP00000124793 ; ENSMUSG00000037280 .
    GeneIDi 207839.
    KEGGi mmu:207839.
    UCSCi uc007xrz.2. mouse.

    Organism-specific databases

    CTDi 11226.
    MGIi MGI:1891640. Galnt6.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117451.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q0VE84.
    KOi K00710.
    OMAi NQCLDVG.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8C7U7.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 372071.
    PROi Q8C7U7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C7U7.
    Genevestigatori Q8C7U7.

    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 characterization of a close homologue of human UDP-N-acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy."
      Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N., Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.
      J. Biol. Chem. 274:25362-25370(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Gastric carcinoma.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Skin.
    3. "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].
      Tissue: Brain.

    Entry informationi

    Entry nameiGALT6_MOUSE
    AccessioniPrimary (citable) accession number: Q8C7U7
    Secondary accession number(s): Q0VE84
    , Q3TWF0, Q8CED2, Q9QZ16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 106 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3