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GNAI1_PONAB
ID   GNAI1_PONAB             Reviewed;         354 AA.
AC   Q5RAD4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1;
DE   AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN   Name=GNAI1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC       transducers downstream of G protein-coupled receptors (GPCRs) in
CC       numerous signaling cascades. The alpha chain contains the guanine
CC       nucleotide binding site and alternates between an active, GTP-bound
CC       state and an inactive, GDP-bound state. Signaling by an activated GPCR
CC       promotes GDP release and GTP binding. The alpha subunit has a low
CC       GTPase activity that converts bound GTP to GDP, thereby terminating the
CC       signal. Both GDP release and GTP hydrolysis are modulated by numerous
CC       regulatory proteins (By similarity). Signaling is mediated via effector
CC       proteins, such as adenylate cyclase. Inhibits adenylate cyclase
CC       activity, leading to decreased intracellular cAMP levels (By
CC       similarity). The inactive GDP-bound form prevents the association of
CC       RGS14 with centrosomes and is required for the translocation of RGS14
CC       from the cytoplasm to the plasma membrane. Required for normal
CC       cytokinesis during mitosis (By similarity). Required for cortical
CC       dynein-dynactin complex recruitment during metaphase (By similarity).
CC       {ECO:0000250|UniProtKB:P10824, ECO:0000250|UniProtKB:P63096}.
CC   -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC       and gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Part of a spindle orientation complex at least composed of GNAI1,
CC       GPSM2 and NUMA1. Identified in complex with the beta subunit GNB1 and
CC       the gamma subunit GNG1. Identified in complex with the beta subunit
CC       GNB1 and the gamma subunit GNG2. GTP binding causes dissociation of the
CC       heterotrimer, liberating the individual subunits so that they can
CC       interact with downstream effector proteins. Interacts (GDP-bound form)
CC       with GPSM1; this inhibits guanine nucleotide exchange and GTP binding.
CC       Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this
CC       inhibits guanine nucleotide exchange. Interacts with RGS10; this
CC       strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16; this
CC       strongly enhances GTPase activity. Interacts with RGS4. Interacts with
CC       RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with
CC       RGS14 (via RGS and GoLoco domains). Interacts with RGS3, RGS6, RGS7,
CC       RGS8, RGS17, RGS18 and RGS20 (in vitro). Interacts (GDP-bound form)
CC       with RIC8A (via C-terminus). Interacts (inactive GDP-bound form) with
CC       NUCB1 (via GBA motif); the interaction leads to activation of GNAI1 (By
CC       similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE
CC       (via GBA motif); the interaction leads to activation of GNAI1 (By
CC       similarity). Interacts (inactive GDP-bound form) with CCDC8A/GIV (via
CC       GBA motif) (By similarity). {ECO:0000250|UniProtKB:P10824,
CC       ECO:0000250|UniProtKB:P63096}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P10824}. Cell membrane
CC       {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P10824}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane
CC       {ECO:0000250|UniProtKB:P10824}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P10824}. Note=Localizes in the centrosomes of
CC       interphase and mitotic cells, but not in centrosomes during
CC       cytokinesis. Detected at the cleavage furrow or the midbody. Localized
CC       at the plasma membrane throughout mitosis. Colocalizes with RIC8A and
CC       RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824}.
CC   -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before
CC       palmitoylation. {ECO:0000250|UniProtKB:P10824}.
CC   -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition.
CC       {ECO:0000250|UniProtKB:P10824}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR859084; CAH91276.1; -; mRNA.
DR   RefSeq; NP_001125754.1; NM_001132282.1.
DR   AlphaFoldDB; Q5RAD4; -.
DR   SMR; Q5RAD4; -.
DR   STRING; 9601.ENSPPYP00000001241; -.
DR   GeneID; 100172679; -.
DR   KEGG; pon:100172679; -.
DR   CTD; 2770; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   InParanoid; Q5RAD4; -.
DR   OrthoDB; 754573at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; 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; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR   GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
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; Mitosis;
KW   Myristate; Nucleotide-binding; Nucleus; Palmitate; Reference proteome;
KW   Transducer; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63096"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(i) subunit
FT                   alpha-1"
FT                   /id="PRO_0000203672"
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:P10824"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         150..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         175..178
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P63096"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
SQ   SEQUENCE   354 AA;  40349 MW;  15A0938AFFF6D303 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
     YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT
     AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK
     TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSTCNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
     AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
 
 
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