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P70419

- GALT3_MOUSE

UniProt

P70419 - GALT3_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

Galnt3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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 HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Glycosylates FGF23 By similarity. Probably glycosylates fibronectin in vivo. May be involved in phosphate homeostasis.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei225 – 2251SubstrateBy similarity
    Binding sitei254 – 2541SubstrateBy similarity
    Metal bindingi277 – 2771ManganeseBy similarity
    Metal bindingi279 – 2791ManganeseBy similarity
    Binding sitei387 – 3871SubstrateBy similarity
    Metal bindingi415 – 4151ManganeseBy similarity
    Binding sitei418 – 4181SubstrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. manganese ion binding Source: Ensembl
    3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein O-linked glycosylation via serine Source: Ensembl
    2. protein O-linked glycosylation via threonine Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.41. 3474.
    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 3 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 3
    Short name:
    GalNAc-T3
    Short name:
    pp-GaNTase 3
    Protein-UDP acetylgalactosaminyltransferase 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
    Gene namesi
    Name:Galnt3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:894695. Galnt3.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane By similarity; Single-pass type II membrane protein By similarity
    Note: Resides preferentially in the trans and medial parts of the Golgi stack.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3PRO_0000059107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 410PROSITE-ProRule annotation
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi401 ↔ 482PROSITE-ProRule annotation
    Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi517 ↔ 535PROSITE-ProRule annotation
    Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
    Disulfide bondi605 ↔ 618PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP70419.
    PaxDbiP70419.
    PRIDEiP70419.

    PTM databases

    PhosphoSiteiP70419.

    Expressioni

    Tissue specificityi

    Highly expressed in the reproductive tract, principally in the testis and uterus, and to a lesser degree in the cervix with only trace levels in the ovary. Also expressed at high level in sublingual gland, stomach and colon, with more moderate amounts present in the submandibular and parotid gland as well as the kidney.1 Publication

    Gene expression databases

    BgeeiP70419.
    GenevestigatoriP70419.

    Interactioni

    Protein-protein interaction databases

    IntActiP70419. 1 interaction.
    MINTiMINT-4095534.
    STRINGi10090.ENSMUSP00000028378.

    Structurei

    3D structure databases

    ProteinModelPortaliP70419.
    SMRiP70419. Positions 122-633.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 633596LumenalSequence 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
    Domaini504 – 630127Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 293110Catalytic subdomain AAdd
    BLAST
    Regioni356 – 41863Catalytic 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.
    InParanoidiQ3UXL2.
    KOiK00710.
    OMAiQYFEYSA.
    OrthoDBiEOG7J9VP2.
    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.

    P70419-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHLKRLVKL HIKRHYHRKF WKLGAVIFFF LVVLILMQRE VSVQYSKEES    50
    KMERNLKNKN KMLDFMLEAV NNIKDAMPKM QIGAPIKENI DVRERPCLQG 100
    YYTAAELKPV FDRPPQDSNA PGASGKPFKI THLSPEEQKE KERGETKHCF 150
    NAFASDRISL HRDLGPDTRP PECIEQKFKR CPPLPTTSVI IVFHNEAWST 200
    LLRTVHSVLY SSPAILLKEI ILVDDASVDD YLHEKLEEYI KQFSIVKIVR 250
    QQERKGLITA RLLGAAVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA 300
    VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR 350
    KDETYPIKTP TFAGGLFSIS KKYFEHIGSY DEEMEIWGGE NIEMSFRVWQ 400
    CGGQLEIMPC SVVGHVFRSK SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI 450
    FYRRNTDAAK IVKQKSFGDL SKRFEIKKRL QCKNFTWYLN TIYPEAYVPD 500
    LNPVISGYIK SVGQPLCLDV GENNQGGKPL ILYTCHGLGG NQYFEYSAQR 550
    EIRHNIQKEL CLHATQGVVQ LKACVYKGHR TIAPGEQIWE IRKDQLLYNP 600
    LFKMCLSSNG EHPNLVPCDA TDLLQKWIFS QND 633
    Length:633
    Mass (Da):72,932
    Last modified:July 27, 2011 - v3
    Checksum:i8BEE7CDDBCF56428
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti324 – 3241S → N in AAH43331. (PubMed:15489334)Curated
    Sequence conflicti633 – 6331D → E in AAB09579. (PubMed:8912633)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70538 mRNA. Translation: AAB09579.1.
    AK135489 mRNA. Translation: BAE22551.1.
    AL929230, AL928586 Genomic DNA. Translation: CAM20333.1.
    AL928586, AL929230 Genomic DNA. Translation: CAM21878.1.
    CH466519 Genomic DNA. Translation: EDL27008.1.
    BC043331 mRNA. Translation: AAH43331.1.
    CCDSiCCDS16075.1.
    PIRiJC5247.
    RefSeqiNP_056551.2. NM_015736.2.
    UniGeneiMm.439760.

    Genome annotation databases

    EnsembliENSMUST00000028378; ENSMUSP00000028378; ENSMUSG00000026994.
    GeneIDi14425.
    KEGGimmu:14425.
    UCSCiuc008jwu.2. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 3

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70538 mRNA. Translation: AAB09579.1 .
    AK135489 mRNA. Translation: BAE22551.1 .
    AL929230 , AL928586 Genomic DNA. Translation: CAM20333.1 .
    AL928586 , AL929230 Genomic DNA. Translation: CAM21878.1 .
    CH466519 Genomic DNA. Translation: EDL27008.1 .
    BC043331 mRNA. Translation: AAH43331.1 .
    CCDSi CCDS16075.1.
    PIRi JC5247.
    RefSeqi NP_056551.2. NM_015736.2.
    UniGenei Mm.439760.

    3D structure databases

    ProteinModelPortali P70419.
    SMRi P70419. Positions 122-633.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P70419. 1 interaction.
    MINTi MINT-4095534.
    STRINGi 10090.ENSMUSP00000028378.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei P70419.

    Proteomic databases

    MaxQBi P70419.
    PaxDbi P70419.
    PRIDEi P70419.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028378 ; ENSMUSP00000028378 ; ENSMUSG00000026994 .
    GeneIDi 14425.
    KEGGi mmu:14425.
    UCSCi uc008jwu.2. mouse.

    Organism-specific databases

    CTDi 2591.
    MGIi MGI:894695. Galnt3.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117451.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q3UXL2.
    KOi K00710.
    OMAi QYFEYSA.
    OrthoDBi EOG7J9VP2.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 3474.
    Reactomei REACT_198517. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT3. mouse.
    NextBioi 286025.
    PROi P70419.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70419.
    Genevestigatori P70419.

    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 expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3."
      Zara J., Hagen F.K., Ten Hagen K.G., Van Wuyckhuyse B.C., Tabak L.A.
      Biochem. Biophys. Res. Commun. 228:38-44(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Strain: CD-1.
      Tissue: Testis.
    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.
      Tissue: Muellerian duct.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Mammary tumor.

    Entry informationi

    Entry nameiGALT3_MOUSE
    AccessioniPrimary (citable) accession number: P70419
    Secondary accession number(s): Q3UXL2, Q80V55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 118 of the entry and version 3 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