Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q925R7

- GLT10_RAT

UniProt

Q925R7 - GLT10_RAT

Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

Galnt10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    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: UniProtKB-EC

    GO - Biological processi

    1. protein O-linked glycosylation Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196259. 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 10

    Organism-specific databases

    RGDi69409. 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_0000059124Add
    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

    PaxDbiQ925R7.
    PRIDEiQ925R7.

    Expressioni

    Tissue specificityi

    Highly expressed in the sublingual gland, testis, small intestine, colon and ovary. Expressed at intermediate level in heart, brain, spleen, lung, stomach, cervix and uterus.1 Publication

    Gene expression databases

    GenevestigatoriQ925R7.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000003447.

    Structurei

    3D structure databases

    ProteinModelPortaliQ925R7.
    SMRiQ925R7. 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.
    InParanoidiQ925R7.
    KOiK00710.
    OMAiHSRQKKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ925R7.
    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.

    Q925R7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGSGAAVAPE    50
    AIQELHSRQK KTLFLGAEQR LKDWHNKEAI RRDAQRVGNG EQGKPYPMTD 100
    AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKLY LETLPNTSII 150
    IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM 200
    ALFPSVRILR TKKREGLIRT RMLGASAATG DVITFLDSHC EANVNWLPPL 250
    LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 300
    PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS 350
    FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE 400
    YAEYIYQRRP EYRHLSAGDV VAQKKLRGSL NCKSFKWFMT KIAWDLPKFY 450
    PPVEPPAAAW GEIRNVGTGL CTDTKHGTLG SPLRLETCIR GRGEAAWNSM 500
    QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS MKGNQLWKYR 550
    KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLENF 600
    NRN 603
    Length:603
    Mass (Da):69,117
    Last modified:December 1, 2001 - v1
    Checksum:i194EDEAA626A4BBF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241241 mRNA. Translation: AAK54498.1.
    RefSeqiNP_570098.1. NM_130742.1.
    UniGeneiRn.60224.

    Genome annotation databases

    EnsembliENSRNOT00000003447; ENSRNOP00000003447; ENSRNOG00000002488.
    GeneIDi170501.
    KEGGirno:170501.
    UCSCiRGD:69409. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241241 mRNA. Translation: AAK54498.1 .
    RefSeqi NP_570098.1. NM_130742.1.
    UniGenei Rn.60224.

    3D structure databases

    ProteinModelPortali Q925R7.
    SMRi Q925R7. Positions 69-603.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000003447.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q925R7.
    PRIDEi Q925R7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000003447 ; ENSRNOP00000003447 ; ENSRNOG00000002488 .
    GeneIDi 170501.
    KEGGi rno:170501.
    UCSCi RGD:69409. rat.

    Organism-specific databases

    CTDi 55568.
    RGDi 69409. Galnt10.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00740000115054.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q925R7.
    KOi K00710.
    OMAi HSRQKKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q925R7.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_196259. O-linked glycosylation of mucins.

    Miscellaneous databases

    NextBioi 621001.
    PROi Q925R7.

    Gene expression databases

    Genevestigatori Q925R7.

    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 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: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Sublingual gland.

    Entry informationi

    Entry nameiGLT10_RAT
    AccessioniPrimary (citable) accession number: Q925R7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 93 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 PubMed:11278534, 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
    Was originally termed Galnt9/pp-GaNTase 9.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3