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O88422

- GALT5_RAT

UniProt

O88422 - GALT5_RAT

Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

Galnt5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2, Muc1b, rMuc-2 or mG-Muc 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 sitei526 – 5261SubstrateBy similarity
    Binding sitei555 – 5551SubstrateBy similarity
    Metal bindingi578 – 5781ManganeseBy similarity
    Binding sitei579 – 5791SubstrateBy similarity
    Metal bindingi580 – 5801ManganeseBy similarity
    Binding sitei685 – 6851SubstrateBy similarity
    Metal bindingi713 – 7131ManganeseBy similarity
    Binding sitei716 – 7161SubstrateBy similarity
    Binding sitei721 – 7211SubstrateBy 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

    BRENDAi2.4.1.41. 5301.
    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 5 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 5
    Short name:
    GalNAc-T5
    Short name:
    pp-GaNTase 5
    Protein-UDP acetylgalactosaminyltransferase 5
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
    Gene namesi
    Name:Galnt5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi620361. Galnt5.

    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 – 930930Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059112Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi476 ↔ 708PROSITE-ProRule annotation
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi699 ↔ 779PROSITE-ProRule annotation
    Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi812 ↔ 825PROSITE-ProRule annotation
    Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi848 ↔ 863PROSITE-ProRule annotation
    Disulfide bondi898 ↔ 913PROSITE-ProRule annotation
    Glycosylationi902 – 9021N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO88422.
    PRIDEiO88422.

    Expressioni

    Tissue specificityi

    Predominantly expressed in sublingual gland. Expressed at lower level in stomach and small intestine. Weakly or not expressed in submandibular gland, parotid gland, kidney, liver, heart, brain, spleen, lung, skeletal muscle, testis, ovary, cervix and uterus.1 Publication

    Gene expression databases

    GenevestigatoriO88422.

    Interactioni

    Subunit structurei

    Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000006319.

    Structurei

    3D structure databases

    ProteinModelPortaliO88422.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 930895LumenalSequence 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
    Domaini794 – 925132Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni485 – 594110Catalytic subdomain AAdd
    BLAST
    Regioni654 – 71663Catalytic 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

    eggNOGiNOG307550.
    GeneTreeiENSGT00740000115054.
    HOGENOMiHOG000231869.
    HOVERGENiHBG051698.
    InParanoidiO88422.
    KOiK00710.
    OMAiSHVVIIT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiO88422.
    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.

    O88422-1 [UniParc]FASTAAdd to Basket

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    MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTGILKEDIM    50
    RREQTGFRVE ADQMTILSPS SRGMRPPRNG AGGKESFRKA ENRVLKVEEN 100
    VDQVQRKGKM QFLLGRGKAV SLWHRTHVQT LPVTLPMQKT QGRDSKPEVS 150
    SLHMMSKQTT VLGSEKDSFT VSRGVPLNKT AEHTETLDKK QEAPENYNLS 200
    SDTSKQASQR ALNVTISVRT DRSKQQSQTV TKSSIQFASL PILKPEEVTV 250
    TKKTEAQGKD LKYEAHKARP LLKFTADVGH LKKQSTNETG LGVLPEADGA 300
    KVAPGKKLNF SESQIVIITK EEGQKTDTKE VPNSKIQTVF PKLLGESQGK 350
    HIPRSQSQTL SSPLAPKRAV SQSKPTLAEE LHTARSNLTA KATTVGHQQS 400
    HANISENPGK HHVLRIDVTL SPRDLNAPGQ FGRPVVVPPG KKKEAEQRWK 450
    EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS 500
    ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK DYLKANLDKY MSQFPKVRIL 550
    RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 600
    KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWRTIP PDVIAKNGIK 650
    ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG 700
    GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF 750
    YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCQ SFKWYLDNVF PDLKAPVVRA 800
    SGVFINLALG KCVSIKNITV VLEDCDGSSE LQQFNYTWVR LIKHGEWCVA 850
    PIPDKGSLTL YPCDNRNNRL KWLHRSASAF HPELVDHIVF ESYQQLLCME 900
    GNFSQKTLKL AACNPTEPQQ KWKFEKYYDV 930
    Length:930
    Mass (Da):105,120
    Last modified:November 1, 1998 - v1
    Checksum:i1C906A76F320A225
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049344 mRNA. Translation: AAC69708.1.
    RefSeqiNP_113984.1. NM_031796.1.
    UniGeneiRn.30048.

    Genome annotation databases

    EnsembliENSRNOT00000006319; ENSRNOP00000006319; ENSRNOG00000004645.
    GeneIDi83627.
    KEGGirno:83627.
    UCSCiRGD:620361. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049344 mRNA. Translation: AAC69708.1 .
    RefSeqi NP_113984.1. NM_031796.1.
    UniGenei Rn.30048.

    3D structure databases

    ProteinModelPortali O88422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000006319.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi O88422.
    PRIDEi O88422.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000006319 ; ENSRNOP00000006319 ; ENSRNOG00000004645 .
    GeneIDi 83627.
    KEGGi rno:83627.
    UCSCi RGD:620361. rat.

    Organism-specific databases

    CTDi 11227.
    RGDi 620361. Galnt5.

    Phylogenomic databases

    eggNOGi NOG307550.
    GeneTreei ENSGT00740000115054.
    HOGENOMi HOG000231869.
    HOVERGENi HBG051698.
    InParanoidi O88422.
    KOi K00710.
    OMAi SHVVIIT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi O88422.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 5301.
    Reactomei REACT_196259. O-linked glycosylation of mucins.

    Miscellaneous databases

    NextBioi 616203.
    PROi O88422.

    Gene expression databases

    Genevestigatori O88422.

    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 expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family."
      Ten Hagen K.G., Hagen F.K., Balys M.M., Beres T.M., Van Wuyckhuyse B., Tabak L.A.
      J. Biol. Chem. 273:27749-27754(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Sublingual gland.

    Entry informationi

    Entry nameiGALT5_RAT
    AccessioniPrimary (citable) accession number: O88422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 101 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