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Q9D2N8

- GLT15_MOUSE

UniProt

Q9D2N8 - GLT15_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 15

Gene

Galnt15

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate 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 sitei231 – 2311SubstrateBy similarity
    Binding sitei260 – 2601SubstrateBy similarity
    Metal bindingi283 – 2831ManganeseBy similarity
    Metal bindingi285 – 2851ManganeseBy similarity
    Metal bindingi416 – 4161ManganeseBy similarity
    Binding sitei419 – 4191SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    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 15 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase-like protein 2
    Short name:
    GalNAc-T-like protein 2
    Short name:
    pp-GaNTase-like protein 2
    Polypeptide N-acetylgalactosaminyltransferase-like protein 2
    Protein-UDP acetylgalactosaminyltransferase-like protein 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
    Gene namesi
    Name:Galnt15
    Synonyms:Galntl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1926004. Galnt15.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. transport vesicle Source: Ensembl

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 638638Polypeptide N-acetylgalactosaminyltransferase 15PRO_0000059138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi181 ↔ 411PROSITE-ProRule annotation
    Disulfide bondi402 ↔ 481PROSITE-ProRule annotation
    Disulfide bondi516 ↔ 535PROSITE-ProRule annotation
    Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi602 ↔ 619PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9D2N8.

    PTM databases

    PhosphoSiteiQ9D2N8.

    Expressioni

    Tissue specificityi

    Specifically expressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9D2N8.
    BgeeiQ9D2N8.
    GenevestigatoriQ9D2N8.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D2N8.
    SMRiQ9D2N8. Positions 128-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 638603LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini503 – 630128Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 299110Catalytic subdomain AAdd
    BLAST
    Regioni357 – 41963Catalytic 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

    eggNOGiNOG282033.
    GeneTreeiENSGT00750000117451.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiA3KN88.
    KOiK00710.
    OMAiETWLGSF.
    OrthoDBiEOG7X3QQH.
    PhylomeDBiQ9D2N8.
    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.

    Q9D2N8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK    50
    HSPDTGYRLD FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA 100
    SPRARRSQSQ GRRQGSYQFI KHRSRRWDEE ALEKDWRTEE DGEESEEVLT 150
    PLGPDSDGLN KPLSARLPLR RVLPEVRHPL CLQQHPTSGL PTASVILCFH 200
    DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS ALSEYVARLE 250
    AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 300
    ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA 350
    LPSPISPVRS PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW 400
    LCGGSVEILP CSRVGHIYRS QDASSRPDPE VALKNKIIIA ETWLSSFKET 450
    FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG CRTFHWFLAN VYPELYPSDH 500
    RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ QQNLEHTGRK 550
    EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG 600
    KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER 638
    Length:638
    Mass (Da):72,321
    Last modified:June 1, 2001 - v1
    Checksum:i421617F0C8556976
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK019470 mRNA. Translation: BAB31741.1.
    BC133711 mRNA. Translation: AAI33712.1.
    CCDSiCCDS36859.1.
    RefSeqiNP_084442.1. NM_030166.3.
    UniGeneiMm.40681.

    Genome annotation databases

    EnsembliENSMUST00000022460; ENSMUSP00000022460; ENSMUSG00000021903.
    GeneIDi78754.
    KEGGimmu:78754.
    UCSCiuc007syb.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase-like protein 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK019470 mRNA. Translation: BAB31741.1 .
    BC133711 mRNA. Translation: AAI33712.1 .
    CCDSi CCDS36859.1.
    RefSeqi NP_084442.1. NM_030166.3.
    UniGenei Mm.40681.

    3D structure databases

    ProteinModelPortali Q9D2N8.
    SMRi Q9D2N8. Positions 128-631.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q9D2N8.

    Proteomic databases

    PRIDEi Q9D2N8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022460 ; ENSMUSP00000022460 ; ENSMUSG00000021903 .
    GeneIDi 78754.
    KEGGi mmu:78754.
    UCSCi uc007syb.1. mouse.

    Organism-specific databases

    CTDi 117248.
    MGIi MGI:1926004. Galnt15.

    Phylogenomic databases

    eggNOGi NOG282033.
    GeneTreei ENSGT00750000117451.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi A3KN88.
    KOi K00710.
    OMAi ETWLGSF.
    OrthoDBi EOG7X3QQH.
    PhylomeDBi Q9D2N8.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 349440.
    PROi Q9D2N8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D2N8.
    Bgeei Q9D2N8.
    Genevestigatori Q9D2N8.

    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. "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: Skin.
    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].
    3. "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 nameiGLT15_MOUSE
    AccessioniPrimary (citable) accession number: Q9D2N8
    Secondary accession number(s): A3KN88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 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