GNAT2_MOUSE
ID GNAT2_MOUSE Reviewed; 354 AA.
AC P50149;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Retina;
RX PubMed=8013366; DOI=10.1210/endo.135.1.8013366;
RA Zigman J.M., Westermark G.T., LaMendola J., Steiner D.F.;
RT "Expression of cone transducin, Gz alpha, and other G-protein alpha-subunit
RT messenger ribonucleic acids in pancreatic islets.";
RL Endocrinology 135:31-37(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31696965; DOI=10.15252/embj.2018101409;
RA Chaya T., Tsutsumi R., Varner L.R., Maeda Y., Yoshida S., Furukawa T.;
RT "Cul3-Klhl18 ubiquitin ligase modulates rod transducin translocation during
RT light-dark adaptation.";
RL EMBO J. 2019:E101409-E101409(2019).
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.
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:0000269|PubMed:31696965}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:31696965}. 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:0000269|PubMed:31696965}.
CC -!- TISSUE SPECIFICITY: In the retina, expressed in the rod photoreceptors.
CC {ECO:0000269|PubMed:31696965}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; L10666; AAC37650.1; -; mRNA.
DR EMBL; BC016272; AAH16272.1; -; mRNA.
DR CCDS; CCDS17750.1; -.
DR RefSeq; NP_032167.1; NM_008141.3.
DR RefSeq; XP_006501071.1; XM_006501008.2.
DR AlphaFoldDB; P50149; -.
DR SMR; P50149; -.
DR BioGRID; 199974; 1.
DR IntAct; P50149; 2.
DR STRING; 10090.ENSMUSP00000053818; -.
DR iPTMnet; P50149; -.
DR PhosphoSitePlus; P50149; -.
DR EPD; P50149; -.
DR jPOST; P50149; -.
DR MaxQB; P50149; -.
DR PaxDb; P50149; -.
DR PRIDE; P50149; -.
DR ProteomicsDB; 271005; -.
DR Antibodypedia; 33764; 178 antibodies from 25 providers.
DR DNASU; 14686; -.
DR Ensembl; ENSMUST00000058669; ENSMUSP00000053818; ENSMUSG00000009108.
DR GeneID; 14686; -.
DR KEGG; mmu:14686; -.
DR UCSC; uc008qyc.2; mouse.
DR CTD; 2780; -.
DR MGI; MGI:95779; Gnat2.
DR VEuPathDB; HostDB:ENSMUSG00000009108; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000158399; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P50149; -.
DR OMA; ICKPDYM; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P50149; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 14686; 2 hits in 71 CRISPR screens.
DR PRO; PR:P50149; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P50149; protein.
DR Bgee; ENSMUSG00000009108; Expressed in retinal neural layer and 95 other tissues.
DR ExpressionAtlas; P50149; baseline and differential.
DR Genevisible; P50149; MM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; ISO:MGI.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; TAS:MGI.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0009642; P:response to light intensity; ISO:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
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 projection; GTP-binding; Lipoprotein; Magnesium; Metal-binding;
KW Myristate; Nucleotide-binding; Reference proteome; Sensory transduction;
KW 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_0000203741"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..28
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..28
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"
SQ SEQUENCE 354 AA; 40118 MW; 6A14B9B152F14F4E CRC64;
MGSGISAEDK ELARRSKELE KKLQEDADKE AKTVKLLLLG AGESGKSTIV KQMKIIHQDG
YSPEECLEFK SVIYGNVLQS ILAIIRAMST LGIDYAEPSC ADAGRQLNNL ADSTEEGTMP
PELVDVIRKL WKDGGVQACF DRAAEFQLND SASYYLNQLD RITDPNYLPN EQDVLRSRVK
TTGIIETKFS VKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDDEV
NRMHESLHLF NSICNHKFFA ATSIVLFLNK KDLFEEKIKK VHLSICFPEY DGNNSYEDAG
NYIKSQFLDL NMRKDVKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
