GNAI1_CHICK
ID GNAI1_CHICK Reviewed; 354 AA.
AC P50146;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7821803; DOI=10.1016/0378-1119(94)90449-9;
RA Kilbourne E.J., Galper J.B.;
RT "Cloning of cDNAs coding for the G alpha i1 and G alpha i2 G-proteins from
RT chick brain.";
RL Gene 150:341-344(1994).
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). Required for cortical dynein-dynactin complex recruitment
CC during metaphase (By similarity). {ECO:0000250|UniProtKB:P10824,
CC 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. Identified in complex with
CC the beta subunit GNB1 and the gamma subunit GNG1. Identified in complex
CC with the beta subunit GNB1 and the gamma subunit GNG2. GTP binding
CC causes dissociation of the heterotrimer, liberating the individual
CC subunits so that they can interact with downstream effector proteins
CC (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}.
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; L24548; AAA65066.1; -; mRNA.
DR PIR; I50237; I50237.
DR RefSeq; NP_990734.1; NM_205403.1.
DR AlphaFoldDB; P50146; -.
DR SMR; P50146; -.
DR STRING; 9031.ENSGALP00000013640; -.
DR PaxDb; P50146; -.
DR GeneID; 396368; -.
DR KEGG; gga:396368; -.
DR CTD; 2770; -.
DR VEuPathDB; HostDB:geneid_396368; -.
DR eggNOG; KOG0082; Eukaryota.
DR InParanoid; P50146; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P50146; -.
DR PRO; PR:P50146; -.
DR Proteomes; UP000000539; 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:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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:0031821; F:G protein-coupled serotonin receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
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; IBA:GO_Central.
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:AgBase.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:AgBase.
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_0000203674"
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; 40378 MW; CA03F97E4EF534F2 CRC64;
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDPTR ADDARQLFVL AGAAEEGFMT
ADVAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQTSYIPT QQDVLRTRVK
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY AGSNTYEEAA
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
