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P09606

- GLNA_RAT

UniProt

P09606 - GLNA_RAT

Protein

Glutamine synthetase

Gene

Glul

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential for proliferation of fetal skin fibroblasts. This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner By similarity.By similarity

    Catalytic activityi

    ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Biotin.By similarity
    Magnesium or manganese.By similarity

    GO - Molecular functioni

    1. ATP binding Source: RGD
    2. dynein light chain binding Source: RGD
    3. glutamate-ammonia ligase activity Source: RGD
    4. glutamate binding Source: RGD
    5. glutamate decarboxylase activity Source: UniProtKB-EC
    6. magnesium ion binding Source: RGD
    7. manganese ion binding Source: RGD

    GO - Biological processi

    1. ammonia assimilation cycle Source: RGD
    2. cell proliferation Source: Ensembl
    3. glutamate metabolic process Source: RGD
    4. glutamine biosynthetic process Source: RGD
    5. neurotransmitter metabolic process Source: RGD
    6. positive regulation of epithelial cell proliferation Source: RGD
    7. positive regulation of insulin secretion Source: RGD
    8. positive regulation of synaptic transmission, glutamatergic Source: RGD
    9. protein homooligomerization Source: RGD
    10. response to glucose Source: Ensembl

    Keywords - Molecular functioni

    Ligase, Lyase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_214662. Amino acid synthesis and interconversion (transamination).
    REACT_219617. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Short name:
    GS
    Alternative name(s):
    Glutamate decarboxylase (EC:4.1.1.15)
    Glutamate--ammonia ligase
    Gene namesi
    Name:Glul
    Synonyms:Glns
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 13

    Organism-specific databases

    RGDi2710. Glul.

    Subcellular locationi

    Cytoplasm. Mitochondrion By similarity

    GO - Cellular componenti

    1. axon terminus Source: RGD
    2. cell projection Source: RGD
    3. cytoplasm Source: RGD
    4. intracellular membrane-bounded organelle Source: RGD
    5. mitochondrion Source: UniProtKB-SubCell
    6. neuron projection Source: RGD
    7. perikaryon Source: RGD
    8. protein complex Source: RGD
    9. rough endoplasmic reticulum Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 373372Glutamine synthetasePRO_0000153143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei104 – 1041PhosphotyrosineBy similarity

    Post-translational modificationi

    Ubiquitinated by ZNRF1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP09606.

    2D gel databases

    World-2DPAGE0004:P09606.

    PTM databases

    PhosphoSiteiP09606.

    Expressioni

    Inductioni

    By glucocorticoids. Stimulated by the N-methyl-D-aspartate (NMDA) type glutamate receptor antagonist MK801. Vitamin D and the Wnt signaling pathway inhibit its expression and activity. Down-regulated during osteoblast mineralization.1 Publication

    Gene expression databases

    GenevestigatoriP09606.

    Interactioni

    Subunit structurei

    Homooctamer and homotetramer. Interacts with PALMD By similarity.By similarity

    Protein-protein interaction databases

    BioGridi247058. 2 interactions.
    IntActiP09606. 1 interaction.
    MINTiMINT-4578083.

    Structurei

    3D structure databases

    ProteinModelPortaliP09606.
    SMRiP09606. Positions 3-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000010047.
    HOVERGENiHBG005847.
    KOiK01915.
    OMAiRIPRNVG.
    OrthoDBiEOG7CZK5G.
    PhylomeDBiP09606.

    Family and domain databases

    Gene3Di3.30.590.10. 1 hit.
    InterProiIPR008147. Gln_synt_beta.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    IPR008146. Gln_synth_cat_dom.
    IPR027303. Gln_synth_gly_rich_site.
    IPR027302. Gln_synth_N_conserv_site.
    [Graphical view]
    PfamiPF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF54368. SSF54368. 1 hit.
    PROSITEiPS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09606-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSASSHLN KGIKQMYMNL PQGEKIQLMY IWVDGTGEGL RCKTRTLDCD    50
    PKCVEELPEW NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR RDPNKLVFCE 100
    VFKYNRKPAE TNLRHSCKRI MDMVSSQHPW FGMEQEYTLM GTDGHPFGWP 150
    SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI TGTNAEVMPA 200
    QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA 250
    GCHTNFSTKA MREENGLRCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 300
    TGFHETSNIN DFSAGVANRS ASIRIPRIVG QEKKGYFEDR RPSANCDPYA 350
    VTEAIVRTCL LNETGDEPFQ YKN 373
    Length:373
    Mass (Da):42,268
    Last modified:January 23, 2007 - v3
    Checksum:iA7C12D9C5959BCA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741N → D in AAH61559. (PubMed:15489334)Curated
    Sequence conflicti128 – 1281H → R in AAC42038. (PubMed:1674354)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07921 mRNA. Translation: CAA30754.1.
    M29599
    , M29595, M29596, M29597, M29598 Genomic DNA. Translation: AAA65096.1.
    M29579 mRNA. Translation: AAA65095.1.
    M91652 mRNA. Translation: AAC42038.1.
    BC061559 mRNA. Translation: AAH61559.1.
    BC072694 mRNA. Translation: AAH72694.1.
    PIRiS01242. AJRTQ.
    RefSeqiNP_058769.4. NM_017073.3.
    UniGeneiRn.2204.

    Genome annotation databases

    EnsembliENSRNOT00000075480; ENSRNOP00000065890; ENSRNOG00000049560.
    GeneIDi24957.
    KEGGirno:24957.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07921 mRNA. Translation: CAA30754.1 .
    M29599
    , M29595 , M29596 , M29597 , M29598 Genomic DNA. Translation: AAA65096.1 .
    M29579 mRNA. Translation: AAA65095.1 .
    M91652 mRNA. Translation: AAC42038.1 .
    BC061559 mRNA. Translation: AAH61559.1 .
    BC072694 mRNA. Translation: AAH72694.1 .
    PIRi S01242. AJRTQ.
    RefSeqi NP_058769.4. NM_017073.3.
    UniGenei Rn.2204.

    3D structure databases

    ProteinModelPortali P09606.
    SMRi P09606. Positions 3-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247058. 2 interactions.
    IntActi P09606. 1 interaction.
    MINTi MINT-4578083.

    PTM databases

    PhosphoSitei P09606.

    2D gel databases

    World-2DPAGE 0004:P09606.

    Proteomic databases

    PRIDEi P09606.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000075480 ; ENSRNOP00000065890 ; ENSRNOG00000049560 .
    GeneIDi 24957.
    KEGGi rno:24957.

    Organism-specific databases

    CTDi 2752.
    RGDi 2710. Glul.

    Phylogenomic databases

    GeneTreei ENSGT00390000010047.
    HOVERGENi HBG005847.
    KOi K01915.
    OMAi RIPRNVG.
    OrthoDBi EOG7CZK5G.
    PhylomeDBi P09606.

    Enzyme and pathway databases

    Reactomei REACT_214662. Amino acid synthesis and interconversion (transamination).
    REACT_219617. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

    Miscellaneous databases

    NextBioi 604985.
    PROi P09606.

    Gene expression databases

    Genevestigatori P09606.

    Family and domain databases

    Gene3Di 3.30.590.10. 1 hit.
    InterProi IPR008147. Gln_synt_beta.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    IPR008146. Gln_synth_cat_dom.
    IPR027303. Gln_synth_gly_rich_site.
    IPR027302. Gln_synth_N_conserv_site.
    [Graphical view ]
    Pfami PF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54368. SSF54368. 1 hit.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "Cloning and functional characterization of the rat glutamine synthetase gene."
      Mill J.F., Mearow K.M., Purohit H.J., Haleem-Smith H., King R., Freese E.
      Brain Res. Mol. Brain Res. 9:197-207(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Strain: Brown Norway.
      Tissue: Heart and Pituitary.
    5. Lubec G., Afjehi-Sadat L.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-41; 92-103; 190-213; 299-319 AND 341-357, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.
    6. "Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells."
      Olkku A., Mahonen A.
      Bone 43:483-493(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiGLNA_RAT
    AccessioniPrimary (citable) accession number: P09606
    Secondary accession number(s): Q6P7Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3