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Q8CF93

- GLT13_MOUSE

UniProt

Q8CF93 - GLT13_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

Galnt13

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (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 a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. Probably responsible for the synthesis of Tn antigen in neuronal cells.2 Publications

    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 sitei155 – 1551SubstrateBy similarity
    Binding sitei185 – 1851SubstrateBy similarity
    Metal bindingi208 – 2081ManganeseBy similarity
    Metal bindingi210 – 2101ManganeseBy similarity
    Binding sitei315 – 3151SubstrateBy similarity
    Metal bindingi343 – 3431ManganeseBy similarity
    Binding sitei346 – 3461SubstrateBy similarity
    Binding sitei351 – 3511SubstrateBy 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 13 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 13
    Short name:
    GalNAc-T13
    Short name:
    pp-GaNTase 13
    Protein-UDP acetylgalactosaminyltransferase 13
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
    Gene namesi
    Name:Galnt13
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2139447. Galnt13.

    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

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. It however abolishes Tn antigen in neuronal cells.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi105 ↔ 338PROSITE-ProRule annotation
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi329 ↔ 407PROSITE-ProRule annotation
    Disulfide bondi441 ↔ 458PROSITE-ProRule annotation
    Disulfide bondi481 ↔ 496PROSITE-ProRule annotation
    Disulfide bondi522 ↔ 539PROSITE-ProRule annotation
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8CF93.

    PTM databases

    PhosphoSiteiQ8CF93.

    Expressioni

    Tissue specificityi

    Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level.2 Publications

    Gene expression databases

    ArrayExpressiQ8CF93.
    BgeeiQ8CF93.
    GenevestigatoriQ8CF93.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CF93.
    SMRiQ8CF93. Positions 56-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini28 – 556529LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini428 – 550123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni114 – 224111Catalytic subdomain AAdd
    BLAST
    Regioni284 – 34663Catalytic 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.
    GeneTreeiENSGT00750000117385.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    KOiK00710.
    OMAiETFEYMA.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CF93-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI    50
    SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV 100
    RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV 150
    ILVDDASERD FLKLTLENYV KTLEVPVKII RMEERSGLIR ARLRGAAASK 200
    GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG 250
    SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 300
    YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP 350
    YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT 400
    LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN 450
    EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLSGP VIMLKCHHMR 500
    GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR 550
    NMTLGT 556
    Length:556
    Mass (Da):63,983
    Last modified:March 1, 2003 - v1
    Checksum:i593934CFD0AED148
    GO
    Isoform 2 (identifier: Q8CF93-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         466-466: V → VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV

    Note: No experimental confirmation available.

    Show »
    Length:592
    Mass (Da):67,796
    Checksum:i54A13935542D268C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti457 – 4571N → K in BAC32353. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei466 – 4661V → VHDLCLSAPSLGVGAEECCS NHPLYGLVYTPTINEQV in isoform 2. 1 PublicationVSP_011220

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB082928 mRNA. Translation: BAC54546.1.
    AK038387 mRNA. Translation: BAC29981.1.
    AK045417 mRNA. Translation: BAC32353.1.
    CCDSiCCDS16041.1. [Q8CF93-1]
    RefSeqiNP_766618.2. NM_173030.2. [Q8CF93-1]
    XP_006498154.1. XM_006498091.1. [Q8CF93-1]
    XP_006498155.1. XM_006498092.1. [Q8CF93-1]
    UniGeneiMm.330227.

    Genome annotation databases

    EnsembliENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
    ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
    ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
    ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
    GeneIDi271786.
    KEGGimmu:271786.
    UCSCiuc008jrq.1. mouse. [Q8CF93-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 13

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB082928 mRNA. Translation: BAC54546.1 .
    AK038387 mRNA. Translation: BAC29981.1 .
    AK045417 mRNA. Translation: BAC32353.1 .
    CCDSi CCDS16041.1. [Q8CF93-1 ]
    RefSeqi NP_766618.2. NM_173030.2. [Q8CF93-1 ]
    XP_006498154.1. XM_006498091.1. [Q8CF93-1 ]
    XP_006498155.1. XM_006498092.1. [Q8CF93-1 ]
    UniGenei Mm.330227.

    3D structure databases

    ProteinModelPortali Q8CF93.
    SMRi Q8CF93. Positions 56-552.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8CF93.

    Proteomic databases

    PRIDEi Q8CF93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000068595 ; ENSMUSP00000063464 ; ENSMUSG00000060988 . [Q8CF93-1 ]
    ENSMUST00000112634 ; ENSMUSP00000108253 ; ENSMUSG00000060988 . [Q8CF93-2 ]
    ENSMUST00000112635 ; ENSMUSP00000108254 ; ENSMUSG00000060988 . [Q8CF93-1 ]
    ENSMUST00000112636 ; ENSMUSP00000108255 ; ENSMUSG00000060988 . [Q8CF93-1 ]
    GeneIDi 271786.
    KEGGi mmu:271786.
    UCSCi uc008jrq.1. mouse. [Q8CF93-1 ]

    Organism-specific databases

    CTDi 114805.
    MGIi MGI:2139447. Galnt13.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    KOi K00710.
    OMAi ETFEYMA.
    OrthoDBi EOG7J9VP2.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi GALNT13. mouse.
    NextBioi 393497.
    PROi Q8CF93.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CF93.
    Bgeei Q8CF93.
    Genevestigatori Q8CF93.

    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 characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
      Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
      J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina and Hypothalamus.
    3. "T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination."
      Hennet T., Hagen F.K., Tabak L.A., Marth J.D.
      Proc. Natl. Acad. Sci. U.S.A. 92:12070-12074(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    4. "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family."
      Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.
      Glycobiology 13:549-557(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGLT13_MOUSE
    AccessioniPrimary (citable) accession number: Q8CF93
    Secondary accession number(s): Q8BLE4, Q8BYT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 108 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