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)

Q86SF2

- GALT7_HUMAN

UniProt

Q86SF2 - GALT7_HUMAN

Protein

N-acetylgalactosaminyltransferase 7

Gene

GALNT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers 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. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei247 – 2471SubstrateBy similarity
    Binding sitei277 – 2771SubstrateBy similarity
    Metal bindingi301 – 3011ManganeseBy similarity
    Metal bindingi303 – 3031ManganeseBy similarity
    Binding sitei412 – 4121SubstrateBy similarity
    Metal bindingi440 – 4401ManganeseBy similarity
    Binding sitei443 – 4431SubstrateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. O-glycan processing Source: Reactome
    4. post-translational protein modification Source: Reactome
    5. protein O-linked glycosylation Source: ProtInc

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_115606. 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:
    N-acetylgalactosaminyltransferase 7 (EC:2.4.1.-)
    Alternative name(s):
    Polypeptide GalNAc transferase 7
    Short name:
    GalNAc-T7
    Short name:
    pp-GaNTase 7
    Protein-UDP acetylgalactosaminyltransferase 7
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
    Gene namesi
    Name:GALNT7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4129. GALNT7.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28542.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 657657N-acetylgalactosaminyltransferase 7PRO_0000059116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi197 ↔ 435PROSITE-ProRule annotation
    Disulfide bondi426 ↔ 507PROSITE-ProRule annotation
    Disulfide bondi545 ↔ 562PROSITE-ProRule annotation
    Disulfide bondi585 ↔ 600PROSITE-ProRule annotation
    Disulfide bondi625 ↔ 640PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ86SF2.
    PaxDbiQ86SF2.
    PeptideAtlasiQ86SF2.
    PRIDEiQ86SF2.

    PTM databases

    PhosphoSiteiQ86SF2.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.1 Publication

    Gene expression databases

    ArrayExpressiQ86SF2.
    BgeeiQ86SF2.
    CleanExiHS_GALNT7.
    GenevestigatoriQ86SF2.

    Interactioni

    Protein-protein interaction databases

    BioGridi119735. 3 interactions.
    IntActiQ86SF2. 2 interactions.
    STRINGi9606.ENSP00000265000.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86SF2.
    SMRiQ86SF2. Positions 148-656.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 657628LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini532 – 652121Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 317112Catalytic subdomain AAdd
    BLAST
    Regioni381 – 44363Catalytic 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

    eggNOGiNOG248127.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ86SF2.
    KOiK00710.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ86SF2.
    TreeFamiTF352176.

    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.

    Q86SF2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP    50
    MPNRGGNGLA PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG 100
    GDSQKDIMQR QYLTFKPQTF TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG 150
    EKAKPLVLGP EFKQAIQASI KEFGFNMVAS DMISLDRSVN DLRQEECKYW 200
    HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA EIVLIDDFSN 250
    KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL 300
    DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG 350
    YARGAWDWSM LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF 400
    ELGLYDPGLQ IWGGENFEIS YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN 450
    PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF YASRPESQAL PYGDISELKK 500
    FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF ETAYCIDSMG 550
    KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC 600
    NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE 650
    MNNIHSV 657
    Length:657
    Mass (Da):75,389
    Last modified:June 1, 2003 - v1
    Checksum:iD78CB5CBDA4B02FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881S → N in CAB60270. (PubMed:10544240)Curated
    Sequence conflicti392 – 3921F → C in CAB60270. (PubMed:10544240)Curated
    Sequence conflicti408 – 4081G → S in CAB60270. (PubMed:10544240)Curated
    Sequence conflicti508 – 5081K → Q in CAB60270. (PubMed:10544240)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002744 mRNA. Translation: CAB60270.1.
    AK075488 mRNA. Translation: BAG52155.1.
    CH471056 Genomic DNA. Translation: EAX04761.1.
    BC035303 mRNA. Translation: AAH35303.1.
    BC046129 mRNA. Translation: AAH46129.1.
    BC047468 mRNA. Translation: AAH47468.1.
    CCDSiCCDS3815.1.
    RefSeqiNP_059119.2. NM_017423.2.
    UniGeneiHs.548088.

    Genome annotation databases

    EnsembliENST00000265000; ENSP00000265000; ENSG00000109586.
    GeneIDi51809.
    KEGGihsa:51809.
    UCSCiuc003isz.4. human.

    Polymorphism databases

    DMDMi51315961.

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    N-acetylgalactosaminyltransferase 7

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002744 mRNA. Translation: CAB60270.1 .
    AK075488 mRNA. Translation: BAG52155.1 .
    CH471056 Genomic DNA. Translation: EAX04761.1 .
    BC035303 mRNA. Translation: AAH35303.1 .
    BC046129 mRNA. Translation: AAH46129.1 .
    BC047468 mRNA. Translation: AAH47468.1 .
    CCDSi CCDS3815.1.
    RefSeqi NP_059119.2. NM_017423.2.
    UniGenei Hs.548088.

    3D structure databases

    ProteinModelPortali Q86SF2.
    SMRi Q86SF2. Positions 148-656.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119735. 3 interactions.
    IntActi Q86SF2. 2 interactions.
    STRINGi 9606.ENSP00000265000.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q86SF2.

    Polymorphism databases

    DMDMi 51315961.

    Proteomic databases

    MaxQBi Q86SF2.
    PaxDbi Q86SF2.
    PeptideAtlasi Q86SF2.
    PRIDEi Q86SF2.

    Protocols and materials databases

    DNASUi 51809.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265000 ; ENSP00000265000 ; ENSG00000109586 .
    GeneIDi 51809.
    KEGGi hsa:51809.
    UCSCi uc003isz.4. human.

    Organism-specific databases

    CTDi 51809.
    GeneCardsi GC04P174089.
    H-InvDB HIX0031463.
    HGNCi HGNC:4129. GALNT7.
    MIMi 605005. gene.
    neXtProti NX_Q86SF2.
    PharmGKBi PA28542.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248127.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q86SF2.
    KOi K00710.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q86SF2.
    TreeFami TF352176.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    GenomeRNAii 51809.
    NextBioi 55940.
    PROi Q86SF2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86SF2.
    Bgeei Q86SF2.
    CleanExi HS_GALNT7.
    Genevestigatori Q86SF2.

    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. "A novel human UDP-N-acetyl-D-galactosamine;polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates."
      Bennett E.P., Hassan H., Hollingsworth M.A., Clausen H.
      FEBS Lett. 460:226-230(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
    2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Placenta and Testis.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGALT7_HUMAN
    AccessioniPrimary (citable) accession number: Q86SF2
    Secondary accession number(s): B3KQU3, Q7Z5W7, Q9UJ28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3