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Q5JCT0

- GCNT3_MOUSE

UniProt

Q5JCT0 - GCNT3_MOUSE

Protein

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3

Gene

Gcnt3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    Functioni

    Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development By similarity.By similarity

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R.
    UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.

    Pathwayi

    GO - Molecular functioni

    1. acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Source: MGI
    2. beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
    3. N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. immunoglobulin production in mucosal tissue Source: MGI
    2. intestinal absorption Source: MGI
    3. kidney morphogenesis Source: MGI
    4. protein glycosylation Source: UniProtKB-UniPathway
    5. tissue morphogenesis Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_198517. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT14. Glycosyltransferase Family 14.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC:2.4.1.102, EC:2.4.1.150)
    Alternative name(s):
    C2GnT-mucin type
    Short name:
    C2GnT-M
    Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase
    Gene namesi
    Name:Gcnt3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1919327. Gcnt3.

    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 – 437437Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3PRO_0000288546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi70 ↔ 227By similarity
    Disulfide bondi161 ↔ 381By similarity
    Disulfide bondi182 ↔ 209By similarity
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi390 ↔ 422By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ5JCT0.
    PRIDEiQ5JCT0.

    PTM databases

    PhosphoSiteiQ5JCT0.

    Expressioni

    Gene expression databases

    BgeeiQ5JCT0.
    CleanExiMM_GCNT3.
    GenevestigatoriQ5JCT0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JCT0.
    SMRiQ5JCT0. Positions 67-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini31 – 437407LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3018Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 14 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG253565.
    GeneTreeiENSGT00750000117608.
    HOGENOMiHOG000293251.
    HOVERGENiHBG051711.
    InParanoidiQ5JCT0.
    KOiK09662.
    OMAiMTADCEH.
    OrthoDBiEOG74N5HW.
    PhylomeDBiQ5JCT0.
    TreeFamiTF315534.

    Family and domain databases

    InterProiIPR003406. Glyco_trans_14.
    [Graphical view]
    PfamiPF02485. Branch. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5JCT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSWQRLCWH YRLWTLGCYM LLAILALKLS LRLKCDFDAM DLDSEEFQSQ    50
    YCRDLLYKTL KLPAKSSINC SGVIRGEQKA VTQALLNNLE IKKKQQLFTE 100
    ADYLRMTADC EHFKTKRKFI QVPLSKEEAS FPIAYSMVVH EKIENFERLL 150
    RAVYTPQNVY CVHMDQKSSE PFKQAVRAIV SCFPNVFIAS KLVSVVYASW 200
    SRVQADLNCM EDLLQSPVPW KYLLNTCGTD FPIKTNAEMV KALKLLKGQN 250
    SMESEVPPPH KKSRWKYHYE VTDTLHMTSK RKTPPPNNLT MFTGNAYMVA 300
    SRDFIEHVFS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHRK 350
    FDLSDMRAIA RLTKWYDHEG DIENGAPYTS CSGIHQRAVC VYGSGDLHWI 400
    LQNHHLLANK FDPKVDDNVL QCLEEYLRHK AIYGTEL 437
    Length:437
    Mass (Da):50,698
    Last modified:May 29, 2007 - v2
    Checksum:iFF0C1EC8F25320F1
    GO

    Sequence cautioni

    The sequence AAH18297.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB25548.1 differs from that shown. Reason: Erroneous termination at position 35. Translated as Cys.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011A → G in AAK72480. 1 PublicationCurated
    Sequence conflicti353 – 3531L → M in BAB25548. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY039027 mRNA. Translation: AAK72480.1.
    EF202835 mRNA. Translation: ABM91120.1.
    AK008234 mRNA. Translation: BAB25548.1. Sequence problems.
    BC018297 mRNA. Translation: AAH18297.1. Different initiation.
    CCDSiCCDS40678.1.
    RefSeqiNP_082363.2. NM_028087.2.
    XP_006511526.1. XM_006511463.1.
    XP_006511527.1. XM_006511464.1.
    XP_006511528.1. XM_006511465.1.
    UniGeneiMm.195555.

    Genome annotation databases

    EnsembliENSMUST00000034751; ENSMUSP00000034751; ENSMUSG00000032226.
    GeneIDi72077.
    KEGGimmu:72077.
    UCSCiuc009qnt.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    core 2 beta 6 GlcNAc T3

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY039027 mRNA. Translation: AAK72480.1 .
    EF202835 mRNA. Translation: ABM91120.1 .
    AK008234 mRNA. Translation: BAB25548.1 . Sequence problems.
    BC018297 mRNA. Translation: AAH18297.1 . Different initiation.
    CCDSi CCDS40678.1.
    RefSeqi NP_082363.2. NM_028087.2.
    XP_006511526.1. XM_006511463.1.
    XP_006511527.1. XM_006511464.1.
    XP_006511528.1. XM_006511465.1.
    UniGenei Mm.195555.

    3D structure databases

    ProteinModelPortali Q5JCT0.
    SMRi Q5JCT0. Positions 67-432.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT14. Glycosyltransferase Family 14.

    PTM databases

    PhosphoSitei Q5JCT0.

    Proteomic databases

    MaxQBi Q5JCT0.
    PRIDEi Q5JCT0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034751 ; ENSMUSP00000034751 ; ENSMUSG00000032226 .
    GeneIDi 72077.
    KEGGi mmu:72077.
    UCSCi uc009qnt.1. mouse.

    Organism-specific databases

    CTDi 9245.
    MGIi MGI:1919327. Gcnt3.

    Phylogenomic databases

    eggNOGi NOG253565.
    GeneTreei ENSGT00750000117608.
    HOGENOMi HOG000293251.
    HOVERGENi HBG051711.
    InParanoidi Q5JCT0.
    KOi K09662.
    OMAi MTADCEH.
    OrthoDBi EOG74N5HW.
    PhylomeDBi Q5JCT0.
    TreeFami TF315534.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 335378.
    PROi Q5JCT0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5JCT0.
    CleanExi MM_GCNT3.
    Genevestigatori Q5JCT0.

    Family and domain databases

    InterProi IPR003406. Glyco_trans_14.
    [Graphical view ]
    Pfami PF02485. Branch. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Core 2 beta-1,6-N-acetylglucosaminyltransferase II (Core2-GlcNAcT-II)."
      Yeh J.-C., Ong E., Fukuda M.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Mucin biosynthesis: molecular cloning and expression of mouse mucus-type core 2 beta-1,6 N-acetylglucosaminyltransferase."
      Hashimoto M., Tan S., Mori N., Cheng H., Cheng P.-W.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Colon.
    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.
      Tissue: Small intestine.
    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: Colon.

    Entry informationi

    Entry nameiGCNT3_MOUSE
    AccessioniPrimary (citable) accession number: Q5JCT0
    Secondary accession number(s): A2TIK7, Q8VCX9, Q9D8A3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 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