GNAL_RAT
ID GNAL_RAT Reviewed; 381 AA.
AC P38406; Q64711;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 150.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2499043; DOI=10.1126/science.2499043;
RA Jones D.T., Reed R.R.;
RT "Golf: an olfactory neuron specific-G protein involved in odorant signal
RT transduction.";
RL Science 244:790-795(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7494450; DOI=10.1016/0169-328x(95)00070-9;
RA Herve D., Rogard M., Levi-Strauss M.;
RT "Molecular analysis of the multiple Golf alpha subunit mRNAs in the rat
RT brain.";
RL Brain Res. Mol. Brain Res. 32:125-134(1995).
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.
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 (By similarity). {ECO:0000250|UniProtKB:P38405}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
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DR EMBL; M26718; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; S80376; AAP32223.1; -; mRNA.
DR EMBL; S80330; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001178765.1; NM_001191836.2.
DR AlphaFoldDB; P38406; -.
DR SMR; P38406; -.
DR STRING; 10116.ENSRNOP00000025172; -.
DR PhosphoSitePlus; P38406; -.
DR jPOST; P38406; -.
DR PaxDb; P38406; -.
DR PRIDE; P38406; -.
DR GeneID; 24611; -.
DR KEGG; rno:24611; -.
DR UCSC; RGD:2715; rat.
DR CTD; 2774; -.
DR RGD; 2715; Gnal.
DR eggNOG; KOG0099; Eukaryota.
DR InParanoid; P38406; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P38406; -.
DR Reactome; R-RNO-170660; Adenylate cyclase activating pathway.
DR Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-RNO-381753; Olfactory Signaling Pathway.
DR PRO; PR:P38406; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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:0007190; P:activation of adenylate cyclase activity; ISO:RGD.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
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; IMP:RGD.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; IMP:RGD.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0031000; P:response to caffeine; ISO:RGD.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; ISO:RGD.
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 2: Evidence at transcript level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Nucleotide-binding;
KW Palmitate; Phosphoprotein; 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_0000203734"
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:0000250|UniProtKB:Q8CGK7"
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"
FT CONFLICT 70
FT /note="S -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="V -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 44248 MW; 1206E3659457994C CRC64;
MGCLGNSSKT AEDQGVDEKE RREANKKIEK QLQKERLAYK ATHRLLLLGA GESGKSTIVK
QMRILHVNGS 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
