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Q6P9S7

- GLT10_MOUSE

UniProt

Q6P9S7 - GLT10_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

Galnt10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 Muc5Ac and EA2 peptide substrates 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 sitei185 – 1851SubstrateBy similarity
    Binding sitei214 – 2141SubstrateBy similarity
    Metal bindingi237 – 2371ManganeseBy similarity
    Binding sitei238 – 2381SubstrateBy similarity
    Metal bindingi239 – 2391ManganeseBy similarity
    Binding sitei342 – 3421SubstrateBy similarity
    Metal bindingi370 – 3701ManganeseBy similarity
    Binding sitei373 – 3731SubstrateBy similarity
    Binding sitei378 – 3781SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein O-linked glycosylation Source: MGI

    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 10 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 10
    Short name:
    GalNAc-T10
    Short name:
    pp-GaNTase 10
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
    Gene namesi
    Name:Galnt10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1890480. Galnt10.

    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 – 603603Polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi135 ↔ 365PROSITE-ProRule annotation
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi356 ↔ 432PROSITE-ProRule annotation
    Disulfide bondi471 ↔ 488PROSITE-ProRule annotation
    Disulfide bondi523 ↔ 538PROSITE-ProRule annotation
    Disulfide bondi563 ↔ 578PROSITE-ProRule annotation
    Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ6P9S7.

    PTM databases

    PhosphoSiteiQ6P9S7.

    Expressioni

    Tissue specificityi

    Expressed at higher level than GALNT9. In the developing hindbrain region of E14.5 embryos it accumulates in the rapidly dividing, undifferentiated ventricular zone adjacent to the pons. It also accumulates in the regions immediately rostral and caudal to the dorsal rhombic lips differentiating into the cerebellum. Not expressed in the developing choroid plexus.1 Publication

    Gene expression databases

    ArrayExpressiQ6P9S7.
    BgeeiQ6P9S7.
    GenevestigatoriQ6P9S7.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P9S7.
    SMRiQ6P9S7. Positions 69-603.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 603572LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 590133Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 253110Catalytic subdomain AAdd
    BLAST
    Regioni311 – 37363Catalytic subdomain BAdd
    BLAST
    Regioni373 – 38412Flexible loopBy similarityAdd
    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.
    InParanoidiQ6P9S7.
    KOiK00710.
    OMAiHSRQKKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6P9S7.
    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.

    Q6P9S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGLGAAVAPA    50
    AVQELHSRQK KTFFLGAEQR LKDWHNKEAI RRDAQRVGYG EQGKPYPMTD 100
    AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKLY LETLPNTSII 150
    IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM 200
    ALFPSVRILR TKKREGLIRT RMLGASAATG DVVTFLDSHC EANVNWLPPL 250
    LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 300
    PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS 350
    FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE 400
    YAEYIYQRRP EYRHLSAGDV VAQKKLRVSL NCKSFKWFMT KIAWDLPKFY 450
    PPVEPPAAAW GEIRNVGTGL CTDTKLGTLG SPLRLETCIR GRGEAAWNSM 500
    QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS MKGNQLWKYR 550
    KDKTLYHPVS GSCMDCSESD HRVFMNTCNP SSLTQQWLFE HTNSTVLENF 600
    NKN 603
    Length:603
    Mass (Da):69,116
    Last modified:July 5, 2004 - v1
    Checksum:iFF55FBA7E1DD7544
    GO

    Sequence cautioni

    The sequence AAH16585.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD21405.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti233 – 2331V → I in BAD21405. (PubMed:15449545)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131155 mRNA. Translation: BAD21405.1. Different initiation.
    BC016585 mRNA. Translation: AAH16585.1. Different initiation.
    BC060617 mRNA. Translation: AAH60617.1.
    AK033515 mRNA. Translation: BAC28334.1.
    CCDSiCCDS24719.1.
    RefSeqiNP_598950.2. NM_134189.2.
    UniGeneiMm.271670.

    Genome annotation databases

    EnsembliENSMUST00000066987; ENSMUSP00000065096; ENSMUSG00000020520.
    GeneIDi171212.
    KEGGimmu:171212.
    UCSCiuc007jab.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 10

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131155 mRNA. Translation: BAD21405.1 . Different initiation.
    BC016585 mRNA. Translation: AAH16585.1 . Different initiation.
    BC060617 mRNA. Translation: AAH60617.1 .
    AK033515 mRNA. Translation: BAC28334.1 .
    CCDSi CCDS24719.1.
    RefSeqi NP_598950.2. NM_134189.2.
    UniGenei Mm.271670.

    3D structure databases

    ProteinModelPortali Q6P9S7.
    SMRi Q6P9S7. Positions 69-603.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q6P9S7.

    Proteomic databases

    PRIDEi Q6P9S7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000066987 ; ENSMUSP00000065096 ; ENSMUSG00000020520 .
    GeneIDi 171212.
    KEGGi mmu:171212.
    UCSCi uc007jab.1. mouse.

    Organism-specific databases

    CTDi 55568.
    MGIi MGI:1890480. Galnt10.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00740000115054.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q6P9S7.
    KOi K00710.
    OMAi HSRQKKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6P9S7.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi GALNT10. mouse.
    NextBioi 370706.
    PROi Q6P9S7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P9S7.
    Bgeei Q6P9S7.
    Genevestigatori Q6P9S7.

    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. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
      DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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 and FVB/N.
      Tissue: Brain and Mammary tumor.
    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] OF 76-603.
      Strain: C57BL/6J.
      Tissue: Colon.
    4. "Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9."
      Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K., Balys M.M., Beres T.M., Degand P., Tabak L.A.
      J. Biol. Chem. 276:17395-17404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGLT10_MOUSE
    AccessioniPrimary (citable) accession number: Q6P9S7
    Secondary accession number(s): Q6KAQ2, Q8BZU8, Q91YJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.Curated

    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