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Q8BGT9

- GLT12_MOUSE

UniProt

Q8BGT9 - GLT12_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 12

Gene

Galnt12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs 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 sitei171 – 1711SubstrateBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Metal bindingi223 – 2231ManganeseBy similarity
    Metal bindingi225 – 2251ManganeseBy similarity
    Binding sitei330 – 3301SubstrateBy similarity
    Metal bindingi358 – 3581ManganeseBy similarity
    Binding sitei366 – 3661SubstrateBy similarity

    GO - Molecular functioni

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

    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 12 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 12
    Short name:
    GalNAc-T12
    Short name:
    pp-GaNTase 12
    Protein-UDP acetylgalactosaminyltransferase 12
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
    Gene namesi
    Name:Galnt12
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2444664. Galnt12.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 576576Polypeptide N-acetylgalactosaminyltransferase 12PRO_0000059129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi120 ↔ 353PROSITE-ProRule annotation
    Disulfide bondi344 ↔ 417PROSITE-ProRule annotation
    Disulfide bondi453 ↔ 474PROSITE-ProRule annotation
    Disulfide bondi501 ↔ 516PROSITE-ProRule annotation
    Disulfide bondi542 ↔ 561PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ8BGT9.
    PRIDEiQ8BGT9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BGT9.
    BgeeiQ8BGT9.
    GenevestigatoriQ8BGT9.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000045721.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BGT9.
    SMRiQ8BGT9. Positions 83-569.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 576539LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini440 – 572133Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 239110Catalytic subdomain AAdd
    BLAST
    Regioni299 – 36163Catalytic 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.
    InParanoidiQ8BGT9.
    KOiK00710.
    OMAiKELYYHR.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8BGT9.
    TreeFamiTF352660.

    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.

    Q8BGT9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT    50
    PLPGRHEPVL PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI 100
    YLSDRISLHR RLPERWNPLC REVKYDYDNL PKTSVVIAFY NEAWSTLLRT 150
    VYSVLETSPD ILLEEVILVD DYSDREHLKE RLANELSQLP KVRLIRASRR 200
    EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI HEKESAVVCP 250
    VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI 300
    RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET 350
    HPCSHVGHVF PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE 400
    PFGDVTERKK LRAKLQCKDF KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR 450
    GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN QFFEYTTRKE IRYNTRQPEA 500
    CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR KCVEATEKVL 550
    DNGFAPYLRD CTNSDNQRWF FKERMS 576
    Length:576
    Mass (Da):66,541
    Last modified:March 1, 2003 - v1
    Checksum:i706310A99FCDACD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033638 mRNA. Translation: BAC28401.1.
    AK042133 mRNA. Translation: BAC31179.1.
    BC056425 mRNA. Translation: AAH56425.1.
    CCDSiCCDS18158.1.
    RefSeqiNP_766281.1. NM_172693.3.
    UniGeneiMm.132246.

    Genome annotation databases

    EnsembliENSMUST00000045041; ENSMUSP00000045721; ENSMUSG00000039774.
    GeneIDi230145.
    KEGGimmu:230145.
    UCSCiuc008suk.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 12

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033638 mRNA. Translation: BAC28401.1 .
    AK042133 mRNA. Translation: BAC31179.1 .
    BC056425 mRNA. Translation: AAH56425.1 .
    CCDSi CCDS18158.1.
    RefSeqi NP_766281.1. NM_172693.3.
    UniGenei Mm.132246.

    3D structure databases

    ProteinModelPortali Q8BGT9.
    SMRi Q8BGT9. Positions 83-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000045721.

    Protein family/group databases

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

    Proteomic databases

    MaxQBi Q8BGT9.
    PRIDEi Q8BGT9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045041 ; ENSMUSP00000045721 ; ENSMUSG00000039774 .
    GeneIDi 230145.
    KEGGi mmu:230145.
    UCSCi uc008suk.1. mouse.

    Organism-specific databases

    CTDi 79695.
    MGIi MGI:2444664. Galnt12.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117451.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q8BGT9.
    KOi K00710.
    OMAi KELYYHR.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8BGT9.
    TreeFami TF352660.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi GALNT12. mouse.
    NextBioi 379814.
    PROi Q8BGT9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BGT9.
    Bgeei Q8BGT9.
    Genevestigatori Q8BGT9.

    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. "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.
      Tissue: Cecum and Thymus.
    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/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiGLT12_MOUSE
    AccessioniPrimary (citable) accession number: Q8BGT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 101 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