GNA15_MOUSE
ID GNA15_MOUSE Reviewed; 374 AA.
AC P30678; Q8K1S0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 177.
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; Synonyms=Gna-15;
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].
RX PubMed=1946421; DOI=10.1073/pnas.88.22.10049;
RA Wilkie T.M., Scherle P.A., Strathmann M.P., Slepak V.Z., Simon M.I.;
RT "Characterization of G-protein alpha subunits in the Gq class: expression
RT in murine tissues and in stromal and hematopoietic cell lines.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10049-10053(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8838318; DOI=10.1006/geno.1996.0059;
RA Davignon I., Barnard M., Gavrilova O., Sweet K.K., Wilkie T.M.;
RT "Gene structure of murine Gna11 and Gna15: tandemly duplicated Gq class G
RT protein alpha subunit genes.";
RL Genomics 31:359-366(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE OF 301-374, AND TISSUE SPECIFICITY.
RX PubMed=12401211; DOI=10.1016/s0014-5793(02)03409-9;
RA Contos J.J.A., Ye X., Sah V.P., Chun J.;
RT "Tandem genomic arrangement of a G protein (Gna15) and G protein-coupled
RT receptor (s1p(4)/lp(C1)/Edg6) gene.";
RL FEBS Lett. 531:99-102(2002).
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 -!- TISSUE SPECIFICITY: Expressed primarily in hematopoietic cells.
CC Coexpressed with EDG6 at the same relative levels in all tissues
CC examined, with the highest levels in adult spleen and lung.
CC {ECO:0000269|PubMed:12401211}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; M80632; AAA37713.1; -; mRNA.
DR EMBL; U37419; AAB36840.1; -; Genomic_DNA.
DR EMBL; U37414; AAB36840.1; JOINED; Genomic_DNA.
DR EMBL; U37415; AAB36840.1; JOINED; Genomic_DNA.
DR EMBL; U37416; AAB36840.1; JOINED; Genomic_DNA.
DR EMBL; U37417; AAB36840.1; JOINED; Genomic_DNA.
DR EMBL; U37418; AAB36840.1; JOINED; Genomic_DNA.
DR EMBL; BC005439; AAH05439.1; -; mRNA.
DR EMBL; BC011098; AAH11098.1; -; mRNA.
DR EMBL; AJ489247; CAD33253.1; -; Genomic_DNA.
DR CCDS; CCDS24060.1; -.
DR PIR; B41534; B41534.
DR RefSeq; NP_034434.1; NM_010304.3.
DR AlphaFoldDB; P30678; -.
DR SMR; P30678; -.
DR STRING; 10090.ENSMUSP00000049175; -.
DR iPTMnet; P30678; -.
DR PhosphoSitePlus; P30678; -.
DR EPD; P30678; -.
DR MaxQB; P30678; -.
DR PaxDb; P30678; -.
DR PRIDE; P30678; -.
DR ProteomicsDB; 267638; -.
DR Antibodypedia; 23159; 266 antibodies from 29 providers.
DR DNASU; 14676; -.
DR Ensembl; ENSMUST00000043709; ENSMUSP00000049175; ENSMUSG00000034792.
DR GeneID; 14676; -.
DR KEGG; mmu:14676; -.
DR UCSC; uc007gij.1; mouse.
DR CTD; 2769; -.
DR MGI; MGI:95770; Gna15.
DR VEuPathDB; HostDB:ENSMUSG00000034792; -.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000161736; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P30678; -.
DR OMA; NIFVSMQ; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P30678; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-112043; PLC beta mediated events.
DR Reactome; R-MMU-202040; G-protein activation.
DR Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 14676; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Gna15; mouse.
DR PRO; PR:P30678; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P30678; protein.
DR Bgee; ENSMUSG00000034792; Expressed in granulocyte and 58 other tissues.
DR Genevisible; P30678; MM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
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:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IPI:UniProtKB.
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_0000203756"
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; 43536 MW; 44F15DC52C8C233E CRC64;
MARSLTWGCC PWCLTEEEKT AARIDQEINR ILLEQKKQER EELKLLLLGP GESGKSTFIK
QMRIIHGVGY SEEDRRAFRL LIYQNIFVSM QAMIDAMDRL QIPFSRPDSK QHASLVMTQD
PYKVSTFEKP YAVAMQYLWR DAGIRACYER RREFHLLDSA VYYLSHLERI SEDSYIPTAQ
DVLRSRMPTT GINEYCFSVK KTKLRIVDVG GQRSERRKWI HCFENVIALI YLASLSEYDQ
CLEENDQENR MEESLALFST ILELPWFKST SVILFLNKTD ILEDKIHTSH LATYFPSFQG
PRRDAEAAKS FILDMYARVY ASCAEPQDGG RKGSRARRFF AHFTCATDTQ SVRSVFKDVR
DSVLARYLDE INLL
