GNAT2_BOVIN
ID GNAT2_BOVIN Reviewed; 354 AA.
AC P04696;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-2;
DE AltName: Full=Transducin alpha-2 chain;
GN Name=GNAT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3856323; DOI=10.1126/science.3856323;
RA Lochrie M.A., Hurley J.B., Simon M.I.;
RT "Sequence of the alpha subunit of photoreceptor G protein: homologies
RT between transducin, ras, and elongation factors.";
RL Science 228:96-99(1985).
RN [2]
RP FUNCTION.
RX PubMed=6586721; DOI=10.1016/s0021-9258(20)82197-8;
RA Navon S., Fung B.K.-K.;
RT "Characterization of transducin from bovine retinal rod outer segments.
RT Mechanism and effects of cholera toxin-catalyzed ADP-ribosylation.";
RL J. Biol. Chem. 259:6686-6693(1984).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Transducin is an amplifier and one of the transducers of a
CC visual impulse that performs the coupling between rhodopsin and cGMP-
CC phosphodiesterase. {ECO:0000269|PubMed:6586721}.
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: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:P50149}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P50149}. Note=Localizes mainly in the outer
CC segment in the dark-adapted state, whereas is translocated to the inner
CC part of the photoreceptors in the light-adapted state. During dark-
CC adapted conditions, in the presence of UNC119 mislocalizes from the
CC outer segment to the inner part of rod photoreceptors which leads to
CC decreased photoreceptor damage caused by light.
CC {ECO:0000250|UniProtKB:P50149}.
CC -!- TISSUE SPECIFICITY: Retinal rod outer segment.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; M11116; AAA30790.1; -; mRNA.
DR PIR; A94279; RGBOT2.
DR RefSeq; NP_776751.1; NM_174326.2.
DR PDB; 6PGS; X-ray; 2.90 A; B=344-354.
DR PDB; 6PH7; X-ray; 2.90 A; B=344-354.
DR PDBsum; 6PGS; -.
DR PDBsum; 6PH7; -.
DR AlphaFoldDB; P04696; -.
DR SMR; P04696; -.
DR STRING; 9913.ENSBTAP00000017305; -.
DR PaxDb; P04696; -.
DR PRIDE; P04696; -.
DR Ensembl; ENSBTAT00000017305; ENSBTAP00000017305; ENSBTAG00000013017.
DR GeneID; 281795; -.
DR KEGG; bta:281795; -.
DR CTD; 2780; -.
DR VEuPathDB; HostDB:ENSBTAG00000013017; -.
DR VGNC; VGNC:29455; GNAT2.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000158399; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P04696; -.
DR OMA; ICKPDYM; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000013017; Expressed in retina and 107 other tissues.
DR ExpressionAtlas; P04696; baseline.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA: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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:0046549; P:retinal cone cell development; 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 1: Evidence at protein level;
KW 3D-structure; Cell projection; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Myristate; Nucleotide-binding; Reference proteome;
KW Sensory transduction; Transducer; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(t) subunit
FT alpha-2"
FT /id="PRO_0000203739"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 175..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:6PH7"
SQ SEQUENCE 354 AA; 40144 MW; EE13B7B5A660A533 CRC64;
MGSGASAEDK ELAKRSKELE KKLQEDADKE AKTVKLLLLG AGESGKSTIV KQMKIIHQDG
YSPEECLEYK AIIYGNVLQS ILAIIRAMPT LGIDYAEVSC VDNGRQLNNL ADSIEEGTMP
PELVEVIRKL WKDGGVQACF DRAAEYQLND SASYYLNQLD RITAPDYLPN EQDVLRSRVK
TTGIIETKFS VKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDDEV
NRMHESLHLF NSICNHKFFA ATSIVLFLNK KDLFEEKIKK VHLSICFPEY DGNNSYEDAG
NYIKSQFLDL NMRKDVKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
