GNAI2_ORYLA
ID GNAI2_ORYLA Reviewed; 355 AA.
AC O13055;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-2;
DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
DE AltName: Full=Gi alpha c;
DE AltName: Full=Gi2 subunit alpha;
GN Name=gnai2;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=9395335; DOI=10.1111/j.1432-1033.1997.00846.x;
RA Oba Y., Yoshikuni M., Tanaka M., Mita M., Nagahama Y.;
RT "Inhibitory guanine-nucleotide-binding-regulatory protein alpha subunits in
RT medaka (Oryzias latipes) oocytes -- cDNA cloning and decreased expression
RT of proteins during oocyte maturation.";
RL Eur. J. Biochem. 249:846-853(1997).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. The G(i) proteins are involved in hormonal regulation of
CC adenylate cyclase: they inhibit the cyclase in response to beta-
CC adrenergic stimuli. May play a role in cell division (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cell membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; AB001742; BAA20073.1; -; mRNA.
DR RefSeq; NP_001098562.1; NM_001105092.1.
DR RefSeq; XP_011472915.1; XM_011474613.1.
DR AlphaFoldDB; O13055; -.
DR SMR; O13055; -.
DR Ensembl; ENSORLT00000001334; ENSORLP00000001333; ENSORLG00000001082.
DR Ensembl; ENSORLT00000029245; ENSORLP00000032440; ENSORLG00000001082.
DR Ensembl; ENSORLT00015011631; ENSORLP00015002033; ENSORLG00015002725.
DR Ensembl; ENSORLT00020005845; ENSORLP00020005706; ENSORLG00020006604.
DR Ensembl; ENSORLT00020005880; ENSORLP00020005681; ENSORLG00020006604.
DR GeneID; 100125814; -.
DR KEGG; ola:100125814; -.
DR CTD; 2771; -.
DR GeneTree; ENSGT00940000155125; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; O13055; -.
DR OMA; GDYIPTQ; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000001038; Chromosome 5.
DR Proteomes; UP000265180; Chromosome 5.
DR Proteomes; UP000265200; Chromosome 5.
DR Bgee; ENSORLG00000001082; Expressed in pharyngeal gill and 14 other tissues.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
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"
FT CHAIN 2..355
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-2"
FT /id="PRO_0000203684"
FT DOMAIN 32..355
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 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 355 AA; 40993 MW; 15DD95FC8A2C08F4 CRC64;
MGCTVSQEDK AAADRSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG
YSEDECKQYR AVVYSNTVQS IMAIIKAMTI LHLDYERPER EEDAKRLFKM AAEAEERGDL
PEELANIIKD LWADSGIQHC LTRAREYQLN DSAAYYLKDL ERISKPDYIP TQQDVLRTRV
KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVAMSA YDLVLAEDEE
MNRMHESMKL FDSICNNKWF TETSIILFLN KKDLFEQKIA HSPLTICFPE YEGPNTYQEA
QAYIQTKFED LNKKKETKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF
