GNA15_RAT
ID GNA15_RAT Reviewed; 374 AA.
AC O88302;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-15;
DE Short=G alpha-15;
DE Short=G-protein subunit alpha-15;
GN Name=Gna15;
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 [MRNA].
RX PubMed=9685675; DOI=10.1016/s0167-4889(98)00062-7;
RA Kusakabe Y., Yamaguchi E., Tanemura K., Kameyama K., Chiba N., Arai S.,
RA Emori Y., Abe K.;
RT "Identification of two alpha-subunit species of GTP-binding proteins, G
RT alpha 15 and G alpha q, expressed in rat taste buds.";
RL Biochim. Biophys. Acta 1403:265-272(1998).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; AB015308; BAA28827.1; -; mRNA.
DR RefSeq; NP_445994.1; NM_053542.1.
DR AlphaFoldDB; O88302; -.
DR SMR; O88302; -.
DR STRING; 10116.ENSRNOP00000007202; -.
DR iPTMnet; O88302; -.
DR PhosphoSitePlus; O88302; -.
DR PaxDb; O88302; -.
DR GeneID; 89788; -.
DR KEGG; rno:89788; -.
DR UCSC; RGD:619751; rat.
DR CTD; 2769; -.
DR RGD; 619751; Gna15.
DR eggNOG; KOG0085; Eukaryota.
DR InParanoid; O88302; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; O88302; -.
DR Reactome; R-RNO-112043; PLC beta mediated events.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR PRO; PR:O88302; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
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:0001508; P:action potential; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:RGD.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
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; PR00442; GPROTEINAQ.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transducer.
FT CHAIN 1..374
FT /note="Guanine nucleotide-binding protein subunit alpha-15"
FT /id="PRO_0000203758"
FT DOMAIN 41..374
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 44..57
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 181..189
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 204..213
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 273..280
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 344..349
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 183..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 208..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 277..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 43332 MW; E5E65D32D41EC0EB CRC64;
MARSLTWGCC PWCLTEEEKT AARIDQEINK ILLEQKKQER GELKLLLLGP GESGKSTFIK
QMRIIHGAGY SEEDRRAFRL LVYQNIFVSM QAMIEAMDRL QIPFSRPDSK QHASLVMTQD
PYKVSSFEKP YAVAMQYLWR DAGIRACYER RREFHLLDSA VYYLSHLERI AEDDYIPTAQ
DVLRSRMPTT GINEYCFSVQ KTKLRIVDAG GQKSERKKWI HCFENVIALI YLASLSEYDQ
CLEENSQENR MKESLALFST ILELPWFKST SVILFLNKTD ILEDKIHTSH LASYFPSFQG
PRRDAEAAKR FILDMYARVY ASCAEPHDGG RKGSRARRLF AHFTCATDTH SVRSVFKDVR
DSVLARYLDE INLL
