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Q8BVG5

- GLT14_MOUSE

UniProt

Q8BVG5 - GLT14_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 14

Gene

Galnt14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      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. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney 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 sitei151 – 1511SubstrateBy similarity
    Binding sitei176 – 1761SubstrateBy similarity
    Metal bindingi199 – 1991ManganeseBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Metal bindingi201 – 2011ManganeseBy similarity
    Binding sitei305 – 3051SubstrateBy similarity
    Metal bindingi333 – 3331ManganeseBy similarity
    Binding sitei336 – 3361SubstrateBy similarity
    Binding sitei339 – 3391SubstrateBy similarity
    Binding sitei341 – 3411SubstrateBy 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 14 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 14
    Short name:
    GalNAc-T14
    Short name:
    pp-GaNTase 14
    Protein-UDP acetylgalactosaminyltransferase 14
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
    Gene namesi
    Name:Galnt14
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1918935. Galnt14.

    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 – 550550Polypeptide N-acetylgalactosaminyltransferase 14PRO_0000059134Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi101 ↔ 328PROSITE-ProRule annotation
    Disulfide bondi319 ↔ 397PROSITE-ProRule annotation
    Disulfide bondi430 ↔ 447PROSITE-ProRule annotation
    Disulfide bondi474 ↔ 491PROSITE-ProRule annotation
    Disulfide bondi515 ↔ 536PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ8BVG5.

    PTM databases

    PhosphoSiteiQ8BVG5.

    Expressioni

    Gene expression databases

    BgeeiQ8BVG5.
    GenevestigatoriQ8BVG5.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BVG5.
    SMRiQ8BVG5. Positions 78-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini27 – 550524LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 548134Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 215106Catalytic subdomain AAdd
    BLAST
    Regioni274 – 33663Catalytic 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.
    InParanoidiQ8BVG5.
    KOiK00710.
    PhylomeDBiQ8BVG5.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. 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: Q8BVG5-1) [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

    MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD    50
    DLWEQFDERR YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR 100
    CSLLVYCTDL PPTSIIITFH NEARSTLLRT IRSVLNRTPM HLIQEIILVD 150
    DFSNDPEDCK QLIKLPKVKC LRNNERQGLV RSRMRGADIA QGTTLTFLDS 200
    HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE SASELRGGFD 250
    WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV 300
    DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT 350
    YIKNTKRTAE VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF 400
    KWNLENVYPE LRVPPDSSIQ KGNIRQRQKC LESQKQKKQE ILRLSPCAKV 450
    KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL FPGAPVVLAL CKNGDERQLW 500
    TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL MSQHWDIVSS 550
    Length:550
    Mass (Da):63,989
    Last modified:June 13, 2006 - v2
    Checksum:iD67054CFE6F332E1
    GO
    Isoform 2 (identifier: Q8BVG5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-429: IENRLNLRKN...QKGNIRQRQK → SHVTQCCRRR...SSPYYLSSSS
         430-550: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:429
    Mass (Da):50,057
    Checksum:iB14F4BE219C5B7B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121P → H in BAC37208. (PubMed:16141072)Curated
    Sequence conflicti173 – 1731N → H in BAD52069. 1 PublicationCurated
    Sequence conflicti260 – 2601L → I in BAB22325. (PubMed:16141072)Curated
    Sequence conflicti381 – 3811P → H in BAC37208. (PubMed:16141072)Curated
    Sequence conflicti403 – 4031N → Y in BAD52069. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei385 – 42945IENRL…RQRQK → SHVTQCCRRRILIRGTSFRG VVPPTNLPVESPTDPSSPYY LSSSS in isoform 2. 1 PublicationVSP_011225Add
    BLAST
    Alternative sequencei430 – 550121Missing in isoform 2. 1 PublicationVSP_011226Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB175681 mRNA. Translation: BAD52069.1.
    AK002747 mRNA. Translation: BAB22325.1.
    AK078292 mRNA. Translation: BAC37208.1.
    CCDSiCCDS28965.1. [Q8BVG5-1]
    RefSeqiNP_082140.2. NM_027864.2.
    XP_006525002.1. XM_006524939.1. [Q8BVG5-2]
    UniGeneiMm.271953.
    Mm.450771.

    Genome annotation databases

    EnsembliENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
    GeneIDi71685.
    KEGGimmu:71685.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 14

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB175681 mRNA. Translation: BAD52069.1 .
    AK002747 mRNA. Translation: BAB22325.1 .
    AK078292 mRNA. Translation: BAC37208.1 .
    CCDSi CCDS28965.1. [Q8BVG5-1 ]
    RefSeqi NP_082140.2. NM_027864.2.
    XP_006525002.1. XM_006524939.1. [Q8BVG5-2 ]
    UniGenei Mm.271953.
    Mm.450771.

    3D structure databases

    ProteinModelPortali Q8BVG5.
    SMRi Q8BVG5. Positions 78-545.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8BVG5.

    Proteomic databases

    PRIDEi Q8BVG5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112591 ; ENSMUSP00000108210 ; ENSMUSG00000024064 . [Q8BVG5-2 ]
    GeneIDi 71685.
    KEGGi mmu:71685.

    Organism-specific databases

    CTDi 79623.
    MGIi MGI:1918935. Galnt14.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q8BVG5.
    KOi K00710.
    PhylomeDBi Q8BVG5.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 334229.
    PROi Q8BVG5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BVG5.
    Genevestigatori Q8BVG5.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    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. "Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, mpp-GalNAc-T14."
      Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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: Kidney and Olfactory bulb.

    Entry informationi

    Entry nameiGLT14_MOUSE
    AccessioniPrimary (citable) accession number: Q8BVG5
    Secondary accession number(s): Q60GT2, Q8BTI6, Q9DCJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 98 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