ID   GNA15_HUMAN             Reviewed;         374 AA.
AC   P30679; E9KL40; E9KL47; O75247; Q53XK2;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2023, sequence version 3.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-15;
DE            Short=G alpha-15;
DE            Short=G-protein subunit alpha-15;
DE   AltName: Full=Epididymis tissue protein Li 17E;
DE   AltName: Full=Guanine nucleotide-binding protein subunit alpha-16;
DE            Short=G alpha-16;
DE            Short=G-protein subunit alpha-16;
GN   Name=GNA15; Synonyms=GNA16;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1905813; DOI=10.1073/pnas.88.13.5587;
RA   Amatruda T.T. III, Steele D.A., Slepak V.Z., Simon M.I.;
RT   "G alpha 16, a G protein alpha subunit specifically expressed in
RT   hematopoietic cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5587-5591(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA   Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA   Jin S., Liu J., Zhu P., Liu Y.;
RT   "Systematic mapping and functional analysis of a family of human epididymal
RT   secretory sperm-located proteins.";
RL   Mol. Cell. Proteomics 9:2517-2528(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-147.
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
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: Specifically expressed in hematopoietic cells.
CC       Expressed in epididymis (at protein level).
CC       {ECO:0000269|PubMed:20736409}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M63904; AAA35860.1; -; mRNA.
DR   EMBL; GU727637; ADU87639.1; -; mRNA.
DR   EMBL; GU727645; ADU87646.1; -; mRNA.
DR   EMBL; AF493904; AAM12618.1; -; mRNA.
DR   EMBL; BT009850; AAP88852.1; -; mRNA.
DR   EMBL; AC005264; AAC25612.1; -; Genomic_DNA.
DR   EMBL; AC005262; AAC25616.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69338.1; -; Genomic_DNA.
DR   EMBL; BC013585; AAH13585.1; -; mRNA.
DR   CCDS; CCDS12104.1; -.
DR   PIR; A41096; A41096.
DR   RefSeq; NP_002059.3; NM_002068.3.
DR   AlphaFoldDB; P30679; -.
DR   EMDB; EMD-33022; -.
DR   EMDB; EMD-34301; -.
DR   SMR; P30679; -.
DR   BioGRID; 109031; 12.
DR   IntAct; P30679; 15.
DR   STRING; 9606.ENSP00000262958; -.
DR   BindingDB; P30679; -.
DR   iPTMnet; P30679; -.
DR   PhosphoSitePlus; P30679; -.
DR   SwissPalm; P30679; -.
DR   BioMuta; GNA15; -.
DR   DMDM; 311033388; -.
DR   EPD; P30679; -.
DR   jPOST; P30679; -.
DR   MassIVE; P30679; -.
DR   MaxQB; P30679; -.
DR   PaxDb; 9606-ENSP00000262958; -.
DR   PeptideAtlas; P30679; -.
DR   ProteomicsDB; 54731; -.
DR   Pumba; P30679; -.
DR   Antibodypedia; 23159; 300 antibodies from 29 providers.
DR   DNASU; 2769; -.
DR   Ensembl; ENST00000262958.4; ENSP00000262958.2; ENSG00000060558.4.
DR   GeneID; 2769; -.
DR   KEGG; hsa:2769; -.
DR   MANE-Select; ENST00000262958.4; ENSP00000262958.2; NM_002068.4; NP_002059.3.
DR   UCSC; uc002lxf.3; human.
DR   AGR; HGNC:4383; -.
DR   CTD; 2769; -.
DR   DisGeNET; 2769; -.
DR   GeneCards; GNA15; -.
DR   HGNC; HGNC:4383; GNA15.
DR   HPA; ENSG00000060558; Tissue enhanced (bone marrow, esophagus).
DR   MIM; 139314; gene.
DR   neXtProt; NX_P30679; -.
DR   OpenTargets; ENSG00000060558; -.
DR   PharmGKB; PA28768; -.
DR   VEuPathDB; HostDB:ENSG00000060558; -.
DR   eggNOG; KOG0085; Eukaryota.
DR   GeneTree; ENSGT00940000161736; -.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P30679; -.
DR   OMA; NIFVSMQ; -.
DR   OrthoDB; 2897309at2759; -.
DR   PhylomeDB; P30679; -.
DR   TreeFam; TF300673; -.
DR   BRENDA; 3.6.5.1; 2681.
DR   PathwayCommons; P30679; -.
DR   Reactome; R-HSA-112043; PLC beta mediated events.
DR   Reactome; R-HSA-202040; G-protein activation.
DR   Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   SignaLink; P30679; -.
DR   SIGNOR; P30679; -.
DR   BioGRID-ORCS; 2769; 11 hits in 1144 CRISPR screens.
DR   ChiTaRS; GNA15; human.
DR   GenomeRNAi; 2769; -.
DR   Pharos; P30679; Tbio.
DR   PRO; PR:P30679; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P30679; Protein.
DR   Bgee; ENSG00000060558; Expressed in lower esophagus mucosa and 137 other cell types or tissues.
DR   ExpressionAtlas; P30679; baseline and differential.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
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; TAS:Reactome.
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:0007202; P:activation of phospholipase C activity; TAS:ProtInc.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IPI:UniProtKB.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF217; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT ALPHA-15; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00442; GPROTEINAQ.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
DR   Genevisible; P30679; HS.
PE   1: Evidence at protein level;
KW   ADP-ribosylation; GTP-binding; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transducer.
FT   CHAIN           1..374
FT                   /note="Guanine nucleotide-binding protein subunit alpha-15"
FT                   /id="PRO_0000203755"
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"
FT   MOD_RES         186
FT                   /note="ADP-ribosylarginine; by cholera toxin"
FT                   /evidence="ECO:0000250"
FT   VARIANT         147
FT                   /note="C -> Y (in dbSNP:rs310680)"
FT                   /evidence="ECO:0000269|PubMed:15057824"
FT                   /id="VAR_028000"
SQ   SEQUENCE   374 AA;  43508 MW;  8127AC16FC212507 CRC64;
     MARSLTWRCC PWCLTEDEKA AARVDQEINR ILLEQKKQDR GELKLLLLGP GESGKSTFIK
     QMRIIHGAGY SEEERKGFRP LVYQNIFVSM RAMIEAMERL QIPFSRPESK HHASLVMSQD
     PYKVTTFEKR YAAAMQWLWR DAGIRACYER RREFHLLDSA VYYLSHLERI TEEGYVPTAQ
     DVLRSRMPTT GINEYCFSVQ KTNLRIVDVG GQKSERKKWI HCFENVIALI YLASLSEYDQ
     CLEENNQENR MKESLALFGT ILELPWFKST SVILFLNKTD ILEEKIPTSH LATYFPSFQG
     PKQDAEAAKR FILDMYTRMY TGCVDGPEGS KKGARSRRLF SHYTCATDTQ NIRKVFKDVR
     DSVLARYLDE INLL
//