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Q9JJ61

- GLT16_MOUSE

UniProt

Q9JJ61 - GLT16_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 16

Gene

Galnt16

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (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.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 sitei163 – 1631SubstrateBy similarity
    Binding sitei188 – 1881SubstrateBy similarity
    Metal bindingi211 – 2111ManganeseBy similarity
    Binding sitei212 – 2121SubstrateBy similarity
    Metal bindingi213 – 2131ManganeseBy similarity
    Binding sitei317 – 3171SubstrateBy similarity
    Metal bindingi345 – 3451ManganeseBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Binding sitei351 – 3511SubstrateBy similarity
    Binding sitei353 – 3531SubstrateBy 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

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 16 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 16
    Short name:
    GalNAc-T16
    Polypeptide GalNAc transferase-like protein 1
    Short name:
    GalNAc-T-like protein 1
    Short name:
    pp-GaNTase-like protein 1
    Polypeptide N-acetylgalactosaminyltransferase-like protein 1
    Protein-UDP acetylgalactosaminyltransferase-like protein 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1
    Gene namesi
    Name:Galnt16
    Synonyms:Galntl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1917754. Galnt16.

    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 – 558558Polypeptide N-acetylgalactosaminyltransferase 16PRO_0000059136Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi113 ↔ 340PROSITE-ProRule annotation
    Disulfide bondi331 ↔ 409PROSITE-ProRule annotation
    Disulfide bondi441 ↔ 460PROSITE-ProRule annotation
    Disulfide bondi486 ↔ 506PROSITE-ProRule annotation
    Disulfide bondi530 ↔ 543PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9JJ61.
    PRIDEiQ9JJ61.

    PTM databases

    PhosphoSiteiQ9JJ61.

    Expressioni

    Tissue specificityi

    In the CNS, it is predominantly expressed in several distinct hypothalamic, thalamic and amygdaloid nuclei. The most abundant level of expression is in the paraventricular, ventromedial and arcuate nuclei of the hypothalamus, the anterodorsal and parafascicular nuclei of the thalamus and the central, basomedial and medial nuclei of the amygdala. Also expressed in cerebral cortex, lateral septum, habenula and hippocampus.1 Publication

    Gene expression databases

    ArrayExpressiQ9JJ61.
    BgeeiQ9JJ61.
    GenevestigatoriQ9JJ61.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000021558.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJ61.
    SMRiQ9JJ61. Positions 90-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini27 – 558532LumenalSequence 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
    Domaini428 – 555128Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 227106Catalytic subdomain AAdd
    BLAST
    Regioni286 – 34863Catalytic 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.
    HOVERGENiHBG051699.
    InParanoidiQ60GT0.
    KOiK00710.
    OMAiPEDCQLL.
    OrthoDBiEOG7J9VP2.
    TreeFamiTF313267.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q9JJ61-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSSGRGA QRAGGRPEQL    50
    REDRTIPLIV TGTPSKGFDE KAYLSAKQLK PGEDPYRQHA FNQLESDKLS 100
    SDRPIRDTRH YSCPSLSYSS DLPATSVIIT FHNEARSTLL RTVKSVLNRT 150
    PASLIQEIIL VDDFSSDPED CLLLTRIPKV KCLRNDKREG LIRSRVRGAD 200
    VAGATVLTFL DSHCEVNVEW LQPMLQRVME DHTRVVSPII DVISLDNFAY 250
    LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTKPIRTP VIAGGIFVID 300
    KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR 350
    HPYNFPEGNA LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR 400
    IEQRKKMDCK SFRWYLENVY PELTVPVKEV LPGVIKQGVN CLESQGQNTA 450
    GDLLLGMGIC RGSAKSPPPA QAWLFSDHLI QQQGKCLAAT STLMSSPGSP 500
    VILQTCNPKE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT SKCQTDAQAQ 550
    QWQLLPHT 558
    Length:558
    Mass (Da):62,875
    Last modified:July 27, 2011 - v2
    Checksum:i1B59DBE8EDDD5C63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711K → E in BAA97985. 1 PublicationCurated
    Sequence conflicti198 – 1981G → R in BAA97985. 1 PublicationCurated
    Sequence conflicti283 – 2831P → L in BAA97985. 1 PublicationCurated
    Sequence conflicti518 – 5181K → R in BAA97985. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045325 mRNA. Translation: BAA97985.1.
    AB175683 mRNA. Translation: BAD52071.1.
    AK138883 mRNA. Translation: BAE23810.1.
    BC110634 mRNA. Translation: AAI10635.1.
    BC125015 mRNA. Translation: AAI25016.1.
    CCDSiCCDS36482.1.
    RefSeqiNP_001074890.1. NM_001081421.1.
    UniGeneiMm.308296.

    Genome annotation databases

    EnsembliENSMUST00000021558; ENSMUSP00000021558; ENSMUSG00000021130.
    GeneIDi108760.
    KEGGimmu:108760.
    UCSCiuc007oaw.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045325 mRNA. Translation: BAA97985.1 .
    AB175683 mRNA. Translation: BAD52071.1 .
    AK138883 mRNA. Translation: BAE23810.1 .
    BC110634 mRNA. Translation: AAI10635.1 .
    BC125015 mRNA. Translation: AAI25016.1 .
    CCDSi CCDS36482.1.
    RefSeqi NP_001074890.1. NM_001081421.1.
    UniGenei Mm.308296.

    3D structure databases

    ProteinModelPortali Q9JJ61.
    SMRi Q9JJ61. Positions 90-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000021558.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q9JJ61.

    Proteomic databases

    PaxDbi Q9JJ61.
    PRIDEi Q9JJ61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021558 ; ENSMUSP00000021558 ; ENSMUSG00000021130 .
    GeneIDi 108760.
    KEGGi mmu:108760.
    UCSCi uc007oaw.1. mouse.

    Organism-specific databases

    CTDi 57452.
    MGIi MGI:1917754. Galnt16.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOVERGENi HBG051699.
    InParanoidi Q60GT0.
    KOi K00710.
    OMAi PEDCQLL.
    OrthoDBi EOG7J9VP2.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 361295.
    PROi Q9JJ61.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JJ61.
    Bgeei Q9JJ61.
    Genevestigatori Q9JJ61.

    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. Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, mpp-GalNAc-T16."
      Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Strain: C57BL/6J.
      Tissue: Thymus.
    4. "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].
    5. "A new UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase mRNA exhibits predominant expression in the hypothalamus, thalamus and amygdala of mouse forebrain."
      Nelson P.A., Sutcliffe J.G., Thomas E.A.
      Gene Expr. Patterns 1:95-99(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGLT16_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJ61
    Secondary accession number(s): Q60GT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally termed Galnt10/pp-GaNTase 10.1 Publication

    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