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Q9GM01

- GALT9_MACFA

UniProt

Q9GM01 - GALT9_MACFA

Protein

Polypeptide N-acetylgalactosaminyltransferase 9

Gene

GALNT9

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. Does not glycosylate apomucin or SDC3 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 sitei194 – 1941SubstrateBy similarity
    Binding sitei225 – 2251SubstrateBy similarity
    Metal bindingi248 – 2481ManganeseBy similarity
    Metal bindingi250 – 2501ManganeseBy similarity
    Metal bindingi380 – 3801ManganeseBy similarity
    Binding sitei383 – 3831SubstrateBy similarity
    Binding sitei388 – 3881SubstrateBy 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 9 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 9
    Short name:
    GalNAc-T9
    Short name:
    pp-GaNTase 9
    Protein-UDP acetylgalactosaminyltransferase 9
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
    Gene namesi
    Name:GALNT9
    ORF Names:QnpA-13140
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    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 – 606606Polypeptide N-acetylgalactosaminyltransferase 9PRO_0000059121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi144 ↔ 375PROSITE-ProRule annotation
    Disulfide bondi366 ↔ 445PROSITE-ProRule annotation
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi480 ↔ 496PROSITE-ProRule annotation
    Disulfide bondi528 ↔ 543PROSITE-ProRule annotation
    Disulfide bondi570 ↔ 590PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GM01.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 606577LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini467 – 603137Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni153 – 264112Catalytic subdomain AAdd
    BLAST
    Regioni321 – 38363Catalytic 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

    HOVERGENiHBG051699.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    IPR001202. WW_dom.
    [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.

    Q9GM01-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRP LSGGCRPRPA    50
    TPAPGSPLRS GGPRAVVAGR AELVLKGQLP AEPCSPGRLM VPEAEAEAQG 100
    GLAATLRDDG QEAEGKYEEY GYNAQLSDRI SLDRSIPDYR PRKCRHMSYA 150
    QDLPQVSVVF IFVNEALSVI LRSVHSVVNH TPSQLLKEVI LVDDNSDNVE 200
    LKFNLDQYVN KRYPGLVKIV RNSRREGLIR ARLQGWKAAT APVVGFFDAH 250
    VEFNTGWAEP ALSRIREDRR RIVLPAIDNI KYSTFEVQQY ANAAHGYNWG 300
    LWCMYIIPPQ DWLDRGDESA PIRTPAMIGC SFVVDREYFG DIGLLDPGME 350
    VYGGENVELG MRVWQCGGSM EVLPCSRVAH IERTRKPYNN DIDYYAKRNA 400
    LRAAEVWMDD FKSHVYMAWN IPMTNPGVDF GDVSERLALR QRLKCRSFKW 450
    YLENVYPEMR IYNNTLTYGE VRNSKASGYC LDQGAEDGDR AILYPCHGMS 500
    SQLVRYSADG LLQLGPLGST AFLPDSKCLV DDGRGRTPTL RKCEDVARPT 550
    QRLWDFTQSG PIVSRATGRC LEVEMSKDAN FGLRLVVQRC SGQKWMIRNW 600
    IKHARH 606
    Length:606
    Mass (Da):68,318
    Last modified:March 1, 2001 - v1
    Checksum:iA00A97C02BD3BBBD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050509 mRNA. Translation: BAB17277.1.
    UniGeneiMfa.1709.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050509 mRNA. Translation: BAB17277.1 .
    UniGenei Mfa.1709.

    3D structure databases

    ProteinModelPortali Q9GM01.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG051699.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    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.
    IPR001202. WW_dom.
    [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. "Isolation of full-length cDNA clones from macaque brain cDNA libraries."
      Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Parietal cortex.

    Entry informationi

    Entry nameiGALT9_MACFA
    AccessioniPrimary (citable) accession number: Q9GM01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3