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Q921L8

- GLT11_MOUSE

UniProt

Q921L8 - GLT11_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

Galnt11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO) 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 sitei191 – 1911SubstrateBy similarity
    Binding sitei222 – 2221SubstrateBy similarity
    Metal bindingi245 – 2451ManganeseBy similarity
    Binding sitei246 – 2461SubstrateBy similarity
    Metal bindingi247 – 2471ManganeseBy similarity
    Binding sitei350 – 3501SubstrateBy similarity
    Metal bindingi378 – 3781ManganeseBy similarity
    Binding sitei381 – 3811SubstrateBy similarity
    Binding sitei386 – 3861SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. determination of left/right symmetry Source: UniProtKB
    3. Notch receptor processing Source: UniProtKB
    4. Notch signaling involved in heart development Source: UniProtKB
    5. protein O-linked glycosylation via threonine Source: UniProtKB
    6. regulation of Notch signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Notch signaling pathway

    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 11 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 11
    Short name:
    GalNAc-T11
    Short name:
    pp-GaNTase 11
    Protein-UDP acetylgalactosaminyltransferase 11
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
    Gene namesi
    Name:Galnt11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2444392. Galnt11.

    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 – 608608Polypeptide N-acetylgalactosaminyltransferase 11PRO_0000059126Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi493 ↔ 512PROSITE-ProRule annotation
    Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
    Disulfide bondi578 ↔ 596PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ921L8.
    PRIDEiQ921L8.

    PTM databases

    PhosphoSiteiQ921L8.

    Expressioni

    Tissue specificityi

    Mainly expressed in kidney. Weakly expressed in other tissues.1 Publication

    Developmental stagei

    At E8.0, present in the left-right organiser (LRO) node, with enrichment in crown cells compared to pit cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ921L8.
    BgeeiQ921L8.
    GenevestigatoriQ921L8.

    Interactioni

    Subunit structurei

    Interacts with NOTCH1.By similarity

    Protein-protein interaction databases

    IntActiQ921L8. 2 interactions.
    MINTiMINT-4096164.

    Structurei

    3D structure databases

    ProteinModelPortaliQ921L8.
    SMRiQ921L8. Positions 130-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 608579LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini476 – 607132Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 261112Catalytic subdomain AAdd
    BLAST
    Regioni319 – 38163Catalytic 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.
    GeneTreeiENSGT00740000115054.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ921L8.
    KOiK00710.
    OMAiMIFNERD.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ921L8.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 2 hits.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q921L8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSITVRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP    50
    FPKKFYPRFT RGPGRVLDPQ FKANRIDRLM NNHIEDPDKG LSKSSSELGM 100
    IFNERDQELR DLGYQKHAFN MLISNRLGYH RDVPDTRNAE CRRKSYPTDL 150
    PTASIVICFY NEAFSALLRT VHSVVDRTPA HLLHEIILVD DSSDFDDLKG 200
    ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV LVFLDSHCEV 250
    NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF 300
    KWDLVPVSEL GGPDGATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW 350
    GGENLEISFR IWMCGGKLFI LPCSRVGHIF RKRRPYGSPE GQDTMTHNSL 400
    RLAHVWLDEY KEQYFSLRPD LKNKSFGNIS ERVELRKKLG CQSFKWYLDN 450
    IYPEMQIPGP NAKPQQPVLI NRGPKRPRVL QRGRLYHLQT NKCLVAQGRS 500
    SQKGGLVLLK TCDYGDPTQV WIYNEDHELI LNNLLCLDMS ETRSSDPPRL 550
    MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VMDLMDQKGY VGMAICDGSS 600
    SQQWRLEG 608
    Length:608
    Mass (Da):69,201
    Last modified:December 1, 2001 - v1
    Checksum:i0E452FDA1CA5668B
    GO

    Sequence cautioni

    The sequence AAH34184.1 differs from that shown. Reason: Erroneous termination at position 412. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti545 – 5451S → L in BAC40096. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12435 mRNA. Translation: CAC79626.1.
    AF495528 mRNA. Translation: AAQ06668.1.
    AK088014 mRNA. Translation: BAC40096.1.
    AK161524 mRNA. Translation: BAE36442.1.
    BC011428 mRNA. Translation: AAH11428.1.
    BC021504 mRNA. Translation: AAH21504.1.
    BC034184 mRNA. Translation: AAH34184.1. Sequence problems.
    BC034185 mRNA. Translation: AAH34185.1.
    BC036143 mRNA. Translation: AAH36143.1.
    BC036145 mRNA. Translation: AAH36145.1.
    CCDSiCCDS19133.1.
    RefSeqiNP_659157.1. NM_144908.3.
    XP_006535744.1. XM_006535681.1.
    UniGeneiMm.246718.

    Genome annotation databases

    EnsembliENSMUST00000045737; ENSMUSP00000036240; ENSMUSG00000038072.
    ENSMUST00000114950; ENSMUSP00000110600; ENSMUSG00000038072.
    ENSMUST00000114952; ENSMUSP00000110602; ENSMUSG00000038072.
    GeneIDi231050.
    KEGGimmu:231050.
    UCSCiuc008wss.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12435 mRNA. Translation: CAC79626.1 .
    AF495528 mRNA. Translation: AAQ06668.1 .
    AK088014 mRNA. Translation: BAC40096.1 .
    AK161524 mRNA. Translation: BAE36442.1 .
    BC011428 mRNA. Translation: AAH11428.1 .
    BC021504 mRNA. Translation: AAH21504.1 .
    BC034184 mRNA. Translation: AAH34184.1 . Sequence problems.
    BC034185 mRNA. Translation: AAH34185.1 .
    BC036143 mRNA. Translation: AAH36143.1 .
    BC036145 mRNA. Translation: AAH36145.1 .
    CCDSi CCDS19133.1.
    RefSeqi NP_659157.1. NM_144908.3.
    XP_006535744.1. XM_006535681.1.
    UniGenei Mm.246718.

    3D structure databases

    ProteinModelPortali Q921L8.
    SMRi Q921L8. Positions 130-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q921L8. 2 interactions.
    MINTi MINT-4096164.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q921L8.

    Proteomic databases

    PaxDbi Q921L8.
    PRIDEi Q921L8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045737 ; ENSMUSP00000036240 ; ENSMUSG00000038072 .
    ENSMUST00000114950 ; ENSMUSP00000110600 ; ENSMUSG00000038072 .
    ENSMUST00000114952 ; ENSMUSP00000110602 ; ENSMUSG00000038072 .
    GeneIDi 231050.
    KEGGi mmu:231050.
    UCSCi uc008wss.1. mouse.

    Organism-specific databases

    CTDi 63917.
    MGIi MGI:2444392. Galnt11.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00740000115054.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q921L8.
    KOi K00710.
    OMAi MIFNERD.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q921L8.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi GALNT11. mouse.
    NextBioi 380378.
    PROi Q921L8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q921L8.
    Bgeei Q921L8.
    Genevestigatori Q921L8.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 2 hits.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
      Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
      J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Characterization of a novel mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
      Shimoji S., Reynolds P.R., Ten Hagen K.G., Tabak L.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
    3. "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: Ovary and Thymus.
    4. "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: FVB/N.
      Tissue: Kidney and Mammary tumor.
    5. "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
      Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
      Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiGLT11_MOUSE
    AccessioniPrimary (citable) accession number: Q921L8
    Secondary accession number(s): Q3TT83, Q8BU26, Q8K032
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 113 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