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P10824

- GNAI1_RAT

UniProt

P10824 - GNAI1_RAT

Protein

Guanine nucleotide-binding protein G(i) subunit alpha-1

Gene

Gnai1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471MagnesiumBy similarity
    Metal bindingi181 – 1811MagnesiumBy similarity
    Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi40 – 478GTPBy similarity
    Nucleotide bindingi43 – 486GTP
    Nucleotide bindingi175 – 1817GTPBy similarity
    Nucleotide bindingi175 – 1784GTP
    Nucleotide bindingi200 – 2045GTPBy similarity
    Nucleotide bindingi269 – 2724GTP

    GO - Molecular functioni

    1. GDP binding Source: RGD
    2. G-protein beta/gamma-subunit complex binding Source: RefGenome
    3. G-protein coupled serotonin receptor binding Source: RGD
    4. GTPase activating protein binding Source: RGD
    5. GTPase activity Source: RefGenome
    6. GTP binding Source: UniProtKB-KW
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: UniProtKB
    9. signal transducer activity Source: RefGenome

    GO - Biological processi

    1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB
    4. G-protein coupled receptor signaling pathway Source: RGD
    5. negative regulation of synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP10824.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(i) subunit alpha-1
    Alternative name(s):
    Adenylate cyclase-inhibiting G alpha protein
    Gene namesi
    Name:Gnai1
    Synonyms:Gnai-1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2713. Gnai1.

    Subcellular locationi

    Nucleus. Cytoplasm. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody By similarity. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. heterotrimeric G-protein complex Source: RefGenome
    4. membrane Source: RGD
    5. membrane raft Source: RGD
    6. midbody Source: UniProtKB
    7. nucleus Source: UniProtKB-SubCell
    8. plasma membrane Source: UniProtKB
    9. protein complex Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. 1 Publication
    Mutagenesisi204 – 2041Q → L: Does not inhibit interaction with GNAI1 in the centrosomes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1PRO_0000203673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate

    Proteomic databases

    PaxDbiP10824.
    PRIDEiP10824.

    2D gel databases

    World-2DPAGE0004:P10824.

    PTM databases

    PhosphoSiteiP10824.

    Expressioni

    Gene expression databases

    GenevestigatoriP10824.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus). Interacts with DRD2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi247715. 1 interaction.
    DIPiDIP-6073N.
    IntActiP10824. 2 interactions.
    MINTiMINT-1795581.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 167
    Helixi20 – 234
    Helixi27 – 293
    Beta strandi33 – 397
    Helixi46 – 5712
    Helixi63 – 686
    Helixi70 – 9122
    Helixi100 – 11011
    Helixi111 – 1166
    Helixi121 – 13212
    Helixi134 – 1407
    Helixi141 – 1455
    Helixi152 – 1565
    Helixi159 – 1624
    Beta strandi164 – 1663
    Helixi171 – 1755
    Beta strandi183 – 1919
    Beta strandi194 – 2018
    Helixi205 – 21410
    Beta strandi219 – 2268
    Helixi227 – 2315
    Beta strandi237 – 2415
    Helixi242 – 25413
    Helixi257 – 2593
    Beta strandi262 – 2698
    Helixi271 – 2788
    Helixi283 – 2853
    Helixi296 – 30813
    Turni314 – 3163
    Beta strandi319 – 3235
    Helixi329 – 34618
    Helixi348 – 3503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AGRX-ray2.80A/D2-354[»]
    1AS0X-ray2.00A2-354[»]
    1AS2X-ray2.80A2-354[»]
    1AS3X-ray2.40A2-354[»]
    1BH2X-ray2.10A32-346[»]
    1BOFX-ray2.20A2-354[»]
    1CIPX-ray1.50A2-354[»]
    1GDDX-ray2.20A2-354[»]
    1GFIX-ray2.20A2-354[»]
    1GG2X-ray2.40A2-354[»]
    1GIAX-ray2.00A2-354[»]
    1GILX-ray2.30A2-354[»]
    1GITX-ray2.60A2-354[»]
    1GP2X-ray2.30A2-354[»]
    1SHZX-ray2.85A/D22-354[»]
    1SVKX-ray2.00A2-354[»]
    1SVSX-ray1.50A2-354[»]
    2BCJX-ray3.06Q-[»]
    2ZJYX-ray2.80A1-354[»]
    2ZJZX-ray2.60A/B1-354[»]
    3AH8X-ray2.90A2-28[»]
    3D7MX-ray2.90A1-354[»]
    3FFAX-ray2.30A1-348[»]
    3FFBX-ray2.57A1-354[»]
    3V00X-ray2.90A/B/C220-298[»]
    4N0DX-ray1.55A1-354[»]
    4N0EX-ray2.10A1-354[»]
    DisProtiDP00035.
    ProteinModelPortaliP10824.
    SMRiP10824. Positions 5-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10824.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG322962.
    HOGENOMiHOG000038730.
    HOVERGENiHBG063184.
    InParanoidiP10824.
    KOiK04630.
    PhylomeDBiP10824.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR001408. Gprotein_alpha_I.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00441. GPROTEINAI.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P10824-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV    50
    KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR 100
    ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND 150
    SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD 200
    VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF 250
    DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA 300
    AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD 350
    CGLF 354
    Length:354
    Mass (Da):40,345
    Last modified:January 23, 2007 - v3
    Checksum:i99E9D11B485C2DE3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17527 mRNA. Translation: AAA40825.1.
    DQ120469 mRNA. Translation: AAZ23808.1.
    DQ120470 mRNA. Translation: AAZ23809.1.
    PIRiA35377.
    C27423. RGRTI1.
    RefSeqiNP_037277.1. NM_013145.1.
    UniGeneiRn.11391.

    Genome annotation databases

    GeneIDi25686.
    KEGGirno:25686.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17527 mRNA. Translation: AAA40825.1 .
    DQ120469 mRNA. Translation: AAZ23808.1 .
    DQ120470 mRNA. Translation: AAZ23809.1 .
    PIRi A35377.
    C27423. RGRTI1.
    RefSeqi NP_037277.1. NM_013145.1.
    UniGenei Rn.11391.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AGR X-ray 2.80 A/D 2-354 [» ]
    1AS0 X-ray 2.00 A 2-354 [» ]
    1AS2 X-ray 2.80 A 2-354 [» ]
    1AS3 X-ray 2.40 A 2-354 [» ]
    1BH2 X-ray 2.10 A 32-346 [» ]
    1BOF X-ray 2.20 A 2-354 [» ]
    1CIP X-ray 1.50 A 2-354 [» ]
    1GDD X-ray 2.20 A 2-354 [» ]
    1GFI X-ray 2.20 A 2-354 [» ]
    1GG2 X-ray 2.40 A 2-354 [» ]
    1GIA X-ray 2.00 A 2-354 [» ]
    1GIL X-ray 2.30 A 2-354 [» ]
    1GIT X-ray 2.60 A 2-354 [» ]
    1GP2 X-ray 2.30 A 2-354 [» ]
    1SHZ X-ray 2.85 A/D 22-354 [» ]
    1SVK X-ray 2.00 A 2-354 [» ]
    1SVS X-ray 1.50 A 2-354 [» ]
    2BCJ X-ray 3.06 Q - [» ]
    2ZJY X-ray 2.80 A 1-354 [» ]
    2ZJZ X-ray 2.60 A/B 1-354 [» ]
    3AH8 X-ray 2.90 A 2-28 [» ]
    3D7M X-ray 2.90 A 1-354 [» ]
    3FFA X-ray 2.30 A 1-348 [» ]
    3FFB X-ray 2.57 A 1-354 [» ]
    3V00 X-ray 2.90 A/B/C 220-298 [» ]
    4N0D X-ray 1.55 A 1-354 [» ]
    4N0E X-ray 2.10 A 1-354 [» ]
    DisProti DP00035.
    ProteinModelPortali P10824.
    SMRi P10824. Positions 5-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247715. 1 interaction.
    DIPi DIP-6073N.
    IntActi P10824. 2 interactions.
    MINTi MINT-1795581.

    PTM databases

    PhosphoSitei P10824.

    2D gel databases

    World-2DPAGE 0004:P10824.

    Proteomic databases

    PaxDbi P10824.
    PRIDEi P10824.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25686.
    KEGGi rno:25686.

    Organism-specific databases

    CTDi 2770.
    RGDi 2713. Gnai1.

    Phylogenomic databases

    eggNOGi NOG322962.
    HOGENOMi HOG000038730.
    HOVERGENi HBG063184.
    InParanoidi P10824.
    KOi K04630.
    PhylomeDBi P10824.

    Enzyme and pathway databases

    SABIO-RK P10824.

    Miscellaneous databases

    EvolutionaryTracei P10824.
    NextBioi 607673.
    PROi P10824.

    Gene expression databases

    Genevestigatori P10824.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR001408. Gprotein_alpha_I.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00441. GPROTEINAI.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium."
      Jones D.T., Reed R.R.
      J. Biol. Chem. 262:14241-14249(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genetic similarity between spontaneously hypertensive rats and Wistar-Kyoto rats in the coding regions of signal transduction proteins."
      Jackson E.K., Zhu C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SHR and Wistar Kyoto.
    3. "Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits."
      de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B., Siderovski D.P., Farquhar M.G.
      Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPSM1.
    4. "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity."
      Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Gist Farquhar M., Siderovski D.P.
      J. Biol. Chem. 276:29275-29281(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS12 AND RGS14.
    5. "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization."
      Shu F.J., Ramineni S., Amyot W., Hepler J.R.
      Cell. Signal. 19:163-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RGS14, SUBCELLULAR LOCATION.
    6. "Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division."
      Cho H., Kehrl J.H.
      J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RGS14, MUTAGENESIS OF GLN-204.
    7. "Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A."
      Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.
      Biochemistry 50:752-762(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS14 AND RIC8A, MUTAGENESIS OF ASN-149, SUBCELLULAR LOCATION.
    8. "Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis."
      Coleman D.E., Berghuis A.M., Lee E., Linder M.E., Gilman A.G., Sprang S.R.
      Science 265:1405-1412(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    9. "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."
      Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R.
      Cell 83:1047-1058(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER IN COMPLEX WITH GDP, SUBUNIT.
    10. "Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis."
      Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.
      Cell 89:251-261(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RGS4 AND GDP.
    11. "Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment."
      Coleman D.E., Sprang S.R.
      Biochemistry 37:14376-14385(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GDP.
    12. "The A326S mutant of Gialpha1 as an approximation of the receptor-bound state."
      Posner B.A., Mixon M.B., Wall M.A., Sprang S.R., Gilman A.G.
      J. Biol. Chem. 273:21752-21758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-346 IN COMPLEX WITH GDP.

    Entry informationi

    Entry nameiGNAI1_RAT
    AccessioniPrimary (citable) accession number: P10824
    Secondary accession number(s): Q45QN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3