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GNAI3_CAVPO
ID   GNAI3_CAVPO             Reviewed;         354 AA.
AC   P38403;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-3;
DE   AltName: Full=G(i) alpha-3;
GN   Name=GNAI3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Hartley; TISSUE=Lung;
RX   PubMed=1482697; DOI=10.1016/0167-4889(92)90009-z;
RA   Sakanaka C., Izumi T., Nakamura M., Honda Z., Watanabe T., Minami M.,
RA   Mutoh H., Bito H., Seyama Y., Ui M., Shimizu T.;
RT   "Three types of Gi alpha protein of the guinea-pig lung: cDNA cloning and
RT   analysis of their tissue distribution.";
RL   Biochim. Biophys. Acta 1175:61-66(1992).
CC   -!- FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G
CC       proteins) function as transducers downstream of G protein-coupled
CC       receptors (GPCRs) in numerous signaling cascades. The alpha chain
CC       contains the guanine nucleotide binding site and alternates between an
CC       active, GTP-bound state and an inactive, GDP-bound state. Signaling by
CC       an activated GPCR promotes GDP release and GTP binding. The alpha
CC       subunit has a low GTPase activity that converts bound GTP to GDP,
CC       thereby terminating the signal. Both GDP release and GTP hydrolysis are
CC       modulated by numerous regulatory proteins. Signaling is mediated via
CC       effector proteins, such as adenylate cyclase. Inhibits adenylate
CC       cyclase activity, leading to decreased intracellular cAMP levels.
CC       Stimulates the activity of receptor-regulated K(+) channels. The active
CC       GTP-bound form prevents the association of RGS14 with centrosomes and
CC       is required for the translocation of RGS14 from the cytoplasm to the
CC       plasma membrane. May play a role in cell division.
CC       {ECO:0000250|UniProtKB:P08754}.
CC   -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC       and gamma. The alpha subunit contains the guanine nucleotide binding
CC       site. GTP binding causes dissociation of the heterotrimer, liberating
CC       the individual subunits so that they can interact with downstream
CC       effector proteins. Forms a complex with CCDC88A/GIV and EGFR which
CC       leads to enhanced EGFR signaling and triggering of cell migration;
CC       ligand stimulation is required for recruitment of GNAI3 to the complex
CC       (By similarity). Interacts (inactive GDP-bound form) with CCDC88A/GIV
CC       (via GBA motif); the interaction leads to activation of GNAI3 (By
CC       similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE
CC       (via GBA motif); the interaction leads to activation of GNAI3 (By
CC       similarity). Interacts (inactive GDP-bound form) with NUCB1 (via GBA
CC       motif) and NUCB2 (via GBA motif); the interaction leads to activation
CC       of GNAI3 (By similarity). Interacts (inactive GDP-bound form) with
CC       PLCD4 (via GBA motif); the interaction leads to activation of GNAI3 (By
CC       similarity). Interacts with INSR; the interaction is probably mediated
CC       by CCDC88A/GIV (By similarity). Interacts with GPSM1. Interacts (GDP-
CC       bound form) with GPSM2 (via GoLoco domains). Does not interact with
CC       RGS2. Interacts with RGS8 and RGS10; this strongly enhances the
CC       intrinsic GTPase activity. Interacts with RGS12. Interacts with RGS16;
CC       this strongly enhances the intrinsic GTPase activity. Interacts (via
CC       active GTP- or inactive GDP-bound form) with RGS14.
CC       {ECO:0000250|UniProtKB:P08753, ECO:0000250|UniProtKB:P08754,
CC       ECO:0000250|UniProtKB:Q9DC51}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell
CC       membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of
CC       interphase and mitotic cells. Detected at the cleavage furrow and/or
CC       the midbody. {ECO:0000250|UniProtKB:P08754}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:1482697}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D21234; BAA04766.1; -; mRNA.
DR   PIR; S28159; S28159.
DR   RefSeq; NP_001166426.1; NM_001172955.1.
DR   RefSeq; XP_005007809.1; XM_005007752.2.
DR   AlphaFoldDB; P38403; -.
DR   BMRB; P38403; -.
DR   SMR; P38403; -.
DR   STRING; 10141.ENSCPOP00000010346; -.
DR   Ensembl; ENSCPOT00000011611; ENSCPOP00000010346; ENSCPOG00000011504.
DR   GeneID; 100135530; -.
DR   KEGG; cpoc:100135530; -.
DR   CTD; 2773; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   GeneTree; ENSGT00940000153567; -.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P38403; -.
DR   OMA; MRIIHDV; -.
DR   OrthoDB; 754573at2759; -.
DR   TreeFam; TF300673; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000011504; Expressed in zone of skin and 13 other tissues.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW   GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW   Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(i) subunit
FT                   alpha-3"
FT                   /id="PRO_0000203690"
FT   DOMAIN          32..354
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          173..181
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          196..205
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         43..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         150..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         175..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P08754"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  40604 MW;  CE913BFF010C5C30 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG
     YSEEECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEPAR ADDARQLFVL AGSAEEGLMT
     SELAGVIRRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQTNYIPT QQDVLRTRVK
     TTGIVETHFT FKDLYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
     AYIQCQFEDL NRRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY
 
 
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