GNA15_HUMAN
ID GNA15_HUMAN Reviewed; 374 AA.
AC P30679; E9KL40; E9KL47; O75247; Q53XK2;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 205.
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], AND VARIANT CYS-147.
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], TISSUE SPECIFICITY, AND VARIANT CYS-147.
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], AND VARIANT CYS-147.
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], AND VARIANT CYS-147.
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].
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], AND VARIANT CYS-147.
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], AND VARIANT CYS-147.
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 SMR; P30679; -.
DR BioGRID; 109031; 11.
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; P30679; -.
DR PeptideAtlas; P30679; -.
DR PRIDE; P30679; -.
DR ProteomicsDB; 54731; -.
DR Antibodypedia; 23159; 266 antibodies from 29 providers.
DR DNASU; 2769; -.
DR Ensembl; ENST00000262958.4; ENSP00000262958.2; ENSG00000060558.4.
DR GeneID; 2769; -.
DR KEGG; hsa:2769; -.
DR UCSC; uc002lxf.3; human.
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 PharmGKB; PA28768; -.
DR VEuPathDB; HostDB:ENSG00000060558; -.
DR eggNOG; KOG0085; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P30679; -.
DR OrthoDB; 754573at2759; -.
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; 10 hits in 1063 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 136 other tissues.
DR ExpressionAtlas; P30679; baseline and differential.
DR Genevisible; P30679; HS.
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: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 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 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="Y -> C (in dbSNP:rs310680)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1905813, ECO:0000269|PubMed:20736409,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT /id="VAR_028000"
SQ SEQUENCE 374 AA; 43568 MW; F32F8C9198FDC26A CRC64;
MARSLTWRCC PWCLTEDEKA AARVDQEINR ILLEQKKQDR GELKLLLLGP GESGKSTFIK
QMRIIHGAGY SEEERKGFRP LVYQNIFVSM RAMIEAMERL QIPFSRPESK HHASLVMSQD
PYKVTTFEKR YAAAMQWLWR DAGIRAYYER RREFHLLDSA VYYLSHLERI TEEGYVPTAQ
DVLRSRMPTT GINEYCFSVQ KTNLRIVDVG GQKSERKKWI HCFENVIALI YLASLSEYDQ
CLEENNQENR MKESLALFGT ILELPWFKST SVILFLNKTD ILEEKIPTSH LATYFPSFQG
PKQDAEAAKR FILDMYTRMY TGCVDGPEGS KKGARSRRLF SHYTCATDTQ NIRKVFKDVR
DSVLARYLDE INLL
