GNAL_MOUSE
ID GNAL_MOUSE Reviewed; 381 AA.
AC Q8CGK7; Q61020; Q61589;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Guanine nucleotide-binding protein G(olf) subunit alpha;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein, olfactory type;
GN Name=Gnal;
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=C57BL/6J;
RA Von Dannecker L.E.C., Malnic B.;
RT "The mouse G protein Golf alpha subunit full length coding sequence.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 45-55, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-373.
RC STRAIN=CF-1 / Harlan; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 216-276.
RC TISSUE=Brain;
RX PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA Strathmann M., Wilkie T.M., Simon M.I.;
RT "Diversity of the G-protein family: sequences from five additional alpha
RT subunits in the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH GAS2L2.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. G(olf) alpha mediates signal transduction within the olfactory
CC neuroepithelium and the basal ganglia. May be involved in some aspect
CC of visual transduction, and in mediating the effect of one or more
CC hormones/neurotransmitters (By similarity). {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. Interacts
CC with GAS2L2 (PubMed:23994616). {ECO:0000269|PubMed:23994616}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
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DR EMBL; AY179169; AAO03564.1; -; mRNA.
DR EMBL; U38503; AAB01734.1; -; mRNA.
DR EMBL; M57635; AAA63300.1; -; mRNA.
DR CCDS; CCDS29318.1; -.
DR PIR; A33833; A33833.
DR RefSeq; NP_034437.1; NM_010307.3.
DR AlphaFoldDB; Q8CGK7; -.
DR SMR; Q8CGK7; -.
DR BioGRID; 199969; 17.
DR IntAct; Q8CGK7; 2.
DR MINT; Q8CGK7; -.
DR STRING; 10090.ENSMUSP00000025402; -.
DR iPTMnet; Q8CGK7; -.
DR PhosphoSitePlus; Q8CGK7; -.
DR SwissPalm; Q8CGK7; -.
DR jPOST; Q8CGK7; -.
DR MaxQB; Q8CGK7; -.
DR PaxDb; Q8CGK7; -.
DR PRIDE; Q8CGK7; -.
DR ProteomicsDB; 263380; -.
DR Antibodypedia; 4227; 182 antibodies from 27 providers.
DR DNASU; 14680; -.
DR Ensembl; ENSMUST00000076605; ENSMUSP00000075908; ENSMUSG00000024524.
DR Ensembl; ENSMUST00000236771; ENSMUSP00000158245; ENSMUSG00000024524.
DR GeneID; 14680; -.
DR KEGG; mmu:14680; -.
DR UCSC; uc008flt.2; mouse.
DR CTD; 2774; -.
DR MGI; MGI:95774; Gnal.
DR VEuPathDB; HostDB:ENSMUSG00000024524; -.
DR eggNOG; KOG0099; Eukaryota.
DR GeneTree; ENSGT00940000155271; -.
DR HOGENOM; CLU_014184_3_0_1; -.
DR InParanoid; Q8CGK7; -.
DR OMA; KEFFEHA; -.
DR PhylomeDB; Q8CGK7; -.
DR Reactome; R-MMU-170660; Adenylate cyclase activating pathway.
DR Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-MMU-381753; Olfactory Signaling Pathway.
DR BioGRID-ORCS; 14680; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Gnal; mouse.
DR PRO; PR:Q8CGK7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CGK7; protein.
DR Bgee; ENSMUSG00000024524; Expressed in olfactory tubercle and 136 other tissues.
DR ExpressionAtlas; Q8CGK7; baseline and differential.
DR Genevisible; Q8CGK7; MM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISA: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; ISA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISA:MGI.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0031000; P:response to caffeine; IMP:MGI.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
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; PR00443; GPROTEINAS.
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 Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..381
FT /note="Guanine nucleotide-binding protein G(olf) subunit
FT alpha"
FT /id="PRO_0000203733"
FT DOMAIN 41..381
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..57
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 183..191
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 206..215
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 275..282
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 351..356
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 210..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 279..282
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-palmitoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 44308 MW; F707E668EC279033 CRC64;
MGCLGNSSKT AEDQGVDEKE RREANKKIEK QLQKERLAYK ATHRLLLLGA GESGKSTIVK
QMRILHVNGF NPEEKKQKIL DIRKNVKDAI VTIVSAMSTI IPPVPLANPE NQFRSDYIKS
IAPITDFEYS QEFFDHVKKL WDDEGVKACF ERSNEYQLID CAQYFLERID SVSLVDYTPT
DQDLLRCRVL TSGIFETRFQ VDKVNFHMFD VGGQRDERRK WIQCFNDVTA IIYVAACSSY
NMVIREDNNT NRLRESLDLF ESIWNNRWLR TISIILFLNK QDMLAEKVLA GKSKIEDYFP
EYANYTVPED ATPDAGEDPK VTRAKFFIRD LFLRISTATG DGKHYCYPHF TCAVDTENIR
RVFNDCRDII QRMHLKQYEL L
