ID   GNA15_RABIT             Reviewed;         374 AA.
AC   Q9TU29;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Spleen;
RX   PubMed=10571060; DOI=10.1016/s0014-5793(99)01317-4;
RA   Feild J.A., Foley J.J., Testa T.T., Nuthulaganti P., Ellis C., Sarau H.M.,
RA   Ames R.S.;
RT   "Cloning and characterization of a rabbit ortholog of human Galpha16 and
RT   mouse Galpha15.";
RL   FEBS Lett. 460:53-56(1999).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. {ECO:0000269|PubMed:10571060}.
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; AF169627; AAF06740.1; -; mRNA.
DR   RefSeq; NP_001076184.1; NM_001082715.1.
DR   AlphaFoldDB; Q9TU29; -.
DR   SMR; Q9TU29; -.
DR   GeneID; 100009469; -.
DR   KEGG; ocu:100009469; -.
DR   CTD; 2769; -.
DR   InParanoid; Q9TU29; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; NAS:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_0000203757"
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;  42933 MW;  630B2920A208CA1E CRC64;
     MARSLAWRCC PWCLSEDEKA AARVDQEITR LLLEHRRQVR GELKLLLLGT GESGKSTFIK
     QMRIIHGAGY SEEDRKGFRP LVFQNIFLSV QAIIEAMDRL QIPYSRPESK LHASLVMSQD
     PYKVNTFETR YALAVQSLWR DAGVRACYER RREFHLLDSA VYYLSHLERI AEEGYVPTAQ
     DVLRSRMPTT GINEYCFSVQ KTNLRIVDVG GQKSERRKWI HCFEDVTALI FLASLSEYDQ
     CLEENGQENR MQESLALFGT VLALPWFRAT SVILFLNKTD ILEDKVRTSH LATYFPGFRG
     PPQDPEAAKR FILELYTRVY AGAAAGPDGA SKGPRSRRLF SHYTCATDTQ NIRKVFKDVR
     DSVLARYLDE INLL