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)

Q6UE39

- GLT13_RAT

UniProt

Q6UE39 - GLT13_RAT

Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

Galnt13

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells 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 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: 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 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi735044. 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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059132Add
    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

    Expressioni

    Gene expression databases

    GenevestigatoriQ6UE39.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000042772.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UE39.
    SMRiQ6UE39. Positions 94-552.
    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.
    HOVERGENiHBG051699.
    KOiK00710.
    OMAiETFEYMA.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6UE39.

    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.

    Q6UE39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRLVYCKVV 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):63,949
    Last modified:July 5, 2004 - v1
    Checksum:i5AEEB9F0F4ECD148
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY371923 mRNA. Translation: AAQ75749.1.
    RefSeqiNP_954537.1. NM_199106.1.
    XP_006234262.1. XM_006234200.1.
    UniGeneiRn.39371.

    Genome annotation databases

    EnsembliENSRNOT00000048804; ENSRNOP00000042772; ENSRNOG00000005335.
    GeneIDi311039.
    KEGGirno:311039.
    UCSCiRGD:735044. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY371923 mRNA. Translation: AAQ75749.1 .
    RefSeqi NP_954537.1. NM_199106.1.
    XP_006234262.1. XM_006234200.1.
    UniGenei Rn.39371.

    3D structure databases

    ProteinModelPortali Q6UE39.
    SMRi Q6UE39. Positions 94-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000042772.

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000048804 ; ENSRNOP00000042772 ; ENSRNOG00000005335 .
    GeneIDi 311039.
    KEGGi rno:311039.
    UCSCi RGD:735044. rat.

    Organism-specific databases

    CTDi 114805.
    RGDi 735044. Galnt13.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOVERGENi HBG051699.
    KOi K00710.
    OMAi ETFEYMA.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6UE39.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 662923.

    Gene expression databases

    Genevestigatori Q6UE39.

    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. Huang C.Q., Wu S.L., Liu S.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiGLT13_RAT
    AccessioniPrimary (citable) accession number: Q6UE39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 77 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3