GNAT1_MOUSE
ID GNAT1_MOUSE Reviewed; 350 AA.
AC P20612; Q80X34;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-1;
DE AltName: Full=Transducin alpha-1 chain;
GN Name=Gnat1; Synonyms=Gnat-1;
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 [GENOMIC DNA].
RX PubMed=2708360; DOI=10.1016/s0021-9258(18)83210-0;
RA Raport C.J., Dere B., Hurley J.B.;
RT "Characterization of the mouse rod transducin alpha subunit gene.";
RL J. Biol. Chem. 264:7122-7128(1989).
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 PROTEIN SEQUENCE OF 32-42; 194-201; 267-273 AND 330-341, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-317.
RC STRAIN=CF-1 / Harlan; TISSUE=Retina;
RX PubMed=8858601;
RX DOI=10.1002/(sici)1098-2795(199607)44:3<315::aid-mrd5>3.0.co;2-p;
RA Williams C.J., Schultz R.M., Kopf G.S.;
RT "G protein gene expression during mouse oocyte growth and maturation, and
RT preimplantation embryo development.";
RL Mol. Reprod. Dev. 44:315-323(1996).
RN [5]
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: Functions as signal transducer for the rod photoreceptor RHO.
CC Required for normal RHO-mediated light perception by the retina (By
CC similarity). Guanine nucleotide-binding proteins (G proteins) function
CC as transducers downstream of G protein-coupled receptors (GPCRs), such
CC as the photoreceptor RHO. 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. Activated RHO promotes GDP
CC release and GTP binding. Signaling is mediated via downstream effector
CC proteins, such as cGMP-phosphodiesterase (By similarity).
CC {ECO:0000250|UniProtKB:P04695, ECO:0000250|UniProtKB:P11488}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 subunits alpha,
CC beta and gamma. The alpha chain contains the guanine nucleotide binding
CC site. Interacts with RHO. Interacts with RGS9 and PDE6G (By
CC similarity). Interacts (when myristoylated) with UNC119; interaction is
CC required for localization in sensory neurons (By similarity).
CC {ECO:0000250|UniProtKB:P04695, ECO:0000250|UniProtKB:P11488}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000269|PubMed:31696965}. Membrane
CC {ECO:0000250|UniProtKB:P04695}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04695}. 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; M25513; AAA40473.1; -; Genomic_DNA.
DR EMBL; M25506; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25507; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25508; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25509; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25510; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25511; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; M25512; AAA40473.1; JOINED; Genomic_DNA.
DR EMBL; BC022793; AAH22793.1; -; mRNA.
DR EMBL; BC051412; AAH51412.2; -; mRNA.
DR EMBL; BC058810; AAH58810.1; -; mRNA.
DR EMBL; U38504; AAB01735.1; -; mRNA.
DR CCDS; CCDS23504.1; -.
DR PIR; A33352; RGMST1.
DR RefSeq; NP_032166.1; NM_008140.2.
DR AlphaFoldDB; P20612; -.
DR SMR; P20612; -.
DR BioGRID; 199973; 3.
DR IntAct; P20612; 1.
DR STRING; 10090.ENSMUSP00000010205; -.
DR iPTMnet; P20612; -.
DR PhosphoSitePlus; P20612; -.
DR jPOST; P20612; -.
DR MaxQB; P20612; -.
DR PaxDb; P20612; -.
DR PRIDE; P20612; -.
DR ProteomicsDB; 271004; -.
DR Antibodypedia; 13896; 199 antibodies from 26 providers.
DR DNASU; 14685; -.
DR Ensembl; ENSMUST00000010205; ENSMUSP00000010205; ENSMUSG00000034837.
DR GeneID; 14685; -.
DR KEGG; mmu:14685; -.
DR UCSC; uc009rmr.1; mouse.
DR CTD; 2779; -.
DR MGI; MGI:95778; Gnat1.
DR VEuPathDB; HostDB:ENSMUSG00000034837; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160395; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P20612; -.
DR OMA; EFIVIIY; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P20612; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 14685; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gnat1; mouse.
DR PRO; PR:P20612; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P20612; protein.
DR Bgee; ENSMUSG00000034837; Expressed in retinal neural layer and 56 other tissues.
DR ExpressionAtlas; P20612; baseline and differential.
DR Genevisible; P20612; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; TAS:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; 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; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
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:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IMP:MGI.
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:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA: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:0007603; P:phototransduction, visible light; ISO:MGI.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:0009642; P:response to light intensity; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISO:MGI.
DR GO; GO:0050917; P:sensory perception of umami taste; 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 1: Evidence at protein level;
KW Cell projection; Direct protein sequencing; GTP-binding; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Sensory transduction; Transducer;
KW Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT CHAIN 2..350
FT /note="Guanine nucleotide-binding protein G(t) subunit
FT alpha-1"
FT /id="PRO_0000203738"
FT DOMAIN 28..350
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 169..177
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 192..201
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 261..268
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 320..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 340..350
FT /note="Interaction with RHO"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 171..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11488"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P04695"
SQ SEQUENCE 350 AA; 39967 MW; 3810BA8DEEFBD7D5 CRC64;
MGAGASAEEK HSRELEKKLK EDAEKDARTV KLLLLGAGES GKSTIVKQMK IIHQDGYSLE
ECLEFIAIIY GNTLQSILAI VRAMTTLNIQ YGDSARQDDA RKLMHMADTI EEGTMPKEMS
DIIQRLWKDS GIQACFDRAS EYQLNDSAGY YLSDLERLVT PGYVPTEQDV LRSRVKTTGI
IETQFSFKDL NFRMFDVGGQ RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH
ESLHLFNSIC NHRYFATTSI VLFLNKKDVF SEKIKKAHLS ICFPDYDGPN TYEDAGNYIK
VQFLELNMRR DVKEIYSHMT CATDTQNVKF VFDAVTDIII KENLKDCGLF
