GNA13_HUMAN
ID GNA13_HUMAN Reviewed; 377 AA.
AC Q14344; B2R977; B7Z7R0; F5H1G8; Q8TD70;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-13;
DE Short=G alpha-13;
DE Short=G-protein subunit alpha-13;
GN Name=GNA13;
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] (ISOFORM 1), AND VARIANT LEU-221.
RC TISSUE=Thymus;
RX PubMed=7791744; DOI=10.1007/bf00926739;
RA Kabouridis P.S., Waters S.T., Escobar S., Stanners J., Tsoukas C.D.;
RT "Expression of GTP-binding protein alpha subunits in human thymocytes.";
RL Mol. Cell. Biochem. 144:45-51(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
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 [6]
RP INTERACTION WITH ARHGEF11.
RX PubMed=10026210; DOI=10.1074/jbc.274.9.5868;
RA Fukuhara S., Murga C., Zohar M., Igishi T., Gutkind J.S.;
RT "A novel PDZ domain containing guanine nucleotide exchange factor links
RT heterotrimeric G proteins to Rho.";
RL J. Biol. Chem. 274:5868-5879(1999).
RN [7]
RP INTERACTION WITH ARHGEF12.
RX PubMed=11094164; DOI=10.1016/s0014-5793(00)02224-9;
RA Fukuhara S., Chikumi H., Gutkind J.S.;
RT "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links
RT heterotrimeric G proteins of the G(12) family to Rho.";
RL FEBS Lett. 485:183-188(2000).
RN [8]
RP INTERACTION WITH ARHGEF1, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-14
RP AND CYS-18, AND MUTAGENESIS OF CYS-14 AND CYS-18.
RX PubMed=10747909; DOI=10.1074/jbc.m000415200;
RA Bhattacharyya R., Wedegaertner P.B.;
RT "Galpha 13 requires palmitoylation for plasma membrane localization, Rho-
RT dependent signaling, and promotion of p115-RhoGEF membrane binding.";
RL J. Biol. Chem. 275:14992-14999(2000).
RN [9]
RP FUNCTION.
RX PubMed=11976333; DOI=10.1074/jbc.m201984200;
RA Meigs T.E., Fedor-Chaiken M., Kaplan D.D., Brackenbury R., Casey P.J.;
RT "Galpha12 and Galpha13 negatively regulate the adhesive functions of
RT cadherin.";
RL J. Biol. Chem. 277:24594-24600(2002).
RN [10]
RP SUBUNIT, PHOSPHORYLATION AT THR-203, AND MUTAGENESIS OF THR-203.
RX PubMed=12399457; DOI=10.1074/jbc.m209219200;
RA Manganello J.M., Huang J.-S., Kozasa T., Voyno-Yasenetskaya T.A.,
RA Le Breton G.C.;
RT "PKA-mediated phosphorylation of Galpha 13 switch I region alters the
RT Galpha beta gamma 13-GPCR complex and inhibits Rho activation.";
RL J. Biol. Chem. 278:124-130(2003).
RN [11]
RP FUNCTION.
RX PubMed=12515866; DOI=10.1073/pnas.0234057100;
RA Suzuki N., Nakamura S., Mano H., Kozasa T.;
RT "Galpha 12 activates Rho GTPase through tyrosine-phosphorylated leukemia-
RT associated RhoGEF.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:733-738(2003).
RN [12]
RP INTERACTION WITH HAX1.
RX PubMed=15339924; DOI=10.1074/jbc.m408836200;
RA Radhika V., Onesime D., Ha J.H., Dhanasekaran N.;
RT "Galpha13 stimulates cell migration through cortactin-interacting protein
RT Hax-1.";
RL J. Biol. Chem. 279:49406-49413(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH CTNND1.
RX PubMed=15240885; DOI=10.1073/pnas.0401366101;
RA Krakstad B.F., Ardawatia V.V., Aragay A.M.;
RT "A role for Galpha12/Galpha13 in p120ctn regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004).
RN [14]
RP INTERACTION WITH UBXD5.
RX PubMed=16202387; DOI=10.1016/j.bbrc.2005.09.097;
RA Tateiwa K., Katoh H., Negishi M.;
RT "Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-
RT induced RhoA activation.";
RL Biochem. Biophys. Res. Commun. 337:615-620(2005).
RN [15]
RP FUNCTION.
RX PubMed=16787920; DOI=10.1074/jbc.m604376200;
RA Kelly P., Stemmle L.N., Madden J.F., Fields T.A., Daaka Y., Casey P.J.;
RT "A role for the G12 family of heterotrimeric G proteins in prostate cancer
RT invasion.";
RL J. Biol. Chem. 281:26483-26490(2006).
RN [16]
RP FUNCTION.
RX PubMed=16705036; DOI=10.1073/pnas.0510254103;
RA Kelly P., Moeller B.J., Juneja J., Booden M.A., Der C.J., Daaka Y.,
RA Dewhirst M.W., Fields T.A., Casey P.J.;
RT "The G12 family of heterotrimeric G proteins promotes breast cancer
RT invasion and metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8173-8178(2006).
RN [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [18]
RP INTERACTION WITH RGS22, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18703424; DOI=10.1095/biolreprod.107.067504;
RA Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z.,
RA Sha J.;
RT "RGS22, a novel testis-specific regulator of G-protein signaling involved
RT in human and mouse spermiogenesis along with GNA12/13 subunits.";
RL Biol. Reprod. 79:1021-1029(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH GAS2L2.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
RN [21]
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).
RN [22]
RP FUNCTION.
RX PubMed=27084452; DOI=10.1016/j.bbrc.2016.04.048;
RA Yuan B., Cui J., Wang W., Deng K.;
RT "Galpha12/13 signaling promotes cervical cancer invasion through the
RT RhoA/ROCK-JNK signaling axis.";
RL Biochem. Biophys. Res. Commun. 473:1240-1246(2016).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:15240885, PubMed:16787920, PubMed:16705036, PubMed:27084452).
CC Activates effector molecule RhoA by binding and activating RhoGEFs
CC (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG)
CC (PubMed:15240885, PubMed:12515866). GNA13-dependent Rho signaling
CC subsequently regulates transcription factor AP-1 (activating protein-1)
CC (By similarity). Promotes tumor cell invasion and metastasis by
CC activating RhoA/ROCK signaling pathway (PubMed:16787920,
CC PubMed:16705036, PubMed:27084452). Inhibits CDH1-mediated cell adhesion
CC in process independent from Rho activation (PubMed:11976333).
CC {ECO:0000250|UniProtKB:P27601, ECO:0000269|PubMed:11976333,
CC ECO:0000269|PubMed:12515866, ECO:0000269|PubMed:15240885,
CC ECO:0000269|PubMed:16705036, ECO:0000269|PubMed:16787920,
CC ECO:0000269|PubMed:27084452}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma
CC (PubMed:12399457). The alpha chain contains the guanine nucleotide
CC binding site (By similarity). Interacts with UBXD5 (PubMed:16202387).
CC Interacts with HAX1 (PubMed:15339924). Interacts (in GTP-bound form)
CC with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and
CC translocates PPP5C to the cell membrane. Interacts with RGS22
CC (PubMed:18703424). Interacts (in GTP-bound form) with ARHGEF1
CC (PubMed:10747909). Interacts (in GTP-bound form) with ARHGEF11 (via RGS
CC domain) (PubMed:10026210). Interacts (in GTP-bound form) with ARHGEF12
CC (via RGS domain) (PubMed:11094164). Interacts with CTNND1
CC (PubMed:15240885). Interacts with GASL2L2 (PubMed:23994616).
CC {ECO:0000250|UniProtKB:P27601, ECO:0000269|PubMed:10026210,
CC ECO:0000269|PubMed:10747909, ECO:0000269|PubMed:11094164,
CC ECO:0000269|PubMed:12399457, ECO:0000269|PubMed:15240885,
CC ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16202387,
CC ECO:0000269|PubMed:18703424, ECO:0000269|PubMed:23994616}.
CC -!- INTERACTION:
CC Q14344; Q92888: ARHGEF1; NbExp=3; IntAct=EBI-465387, EBI-465400;
CC Q14344; P32302: CXCR5; NbExp=9; IntAct=EBI-465387, EBI-2835269;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747909};
CC Lipid-anchor {ECO:0000269|PubMed:10747909}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Cytoplasm {ECO:0000269|PubMed:10747909,
CC ECO:0000269|PubMed:18703424}. Nucleus {ECO:0000269|PubMed:18703424}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV (PubMed:17081065). Detected in the cytoplasm of Leydig
CC cells and in the seminiferous epithelium, including differentiating
CC cells from the spermatogonia to mature spermatozoa stages
CC (PubMed:18703424). In round spermatids, also present in the nuclei
CC (PubMed:18703424). {ECO:0000269|PubMed:17081065,
CC ECO:0000269|PubMed:18703424}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14344-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14344-2; Sequence=VSP_055140;
CC -!- TISSUE SPECIFICITY: Expressed in testis, including in Leydig cells and
CC in the seminiferous epithelium, in differentiating cells from the
CC spermatogonia to mature spermatozoa stages and round spermatids (at
CC protein level). Expressed in 99.2% of spermatozoa from healthy
CC individuals, but only in 28.6% of macrocephalic spermatozoa from
CC infertile patients (at protein level). {ECO:0000269|PubMed:18703424}.
CC -!- PTM: Palmitoylation is critical for proper membrane localization and
CC signaling. {ECO:0000269|PubMed:10747909}.
CC -!- PTM: Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of
CC alpha, beta and gamma, and inhibits Rho activation.
CC {ECO:0000269|PubMed:12399457}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22075; AAA74235.1; -; mRNA.
DR EMBL; AF493902; AAM12616.1; -; mRNA.
DR EMBL; AK302400; BAH13696.1; -; mRNA.
DR EMBL; AK313672; BAG36424.1; -; mRNA.
DR EMBL; AC037487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW88993.1; -; Genomic_DNA.
DR EMBL; BC036756; AAH36756.1; -; mRNA.
DR CCDS; CCDS11661.1; -. [Q14344-1]
DR CCDS; CCDS62302.1; -. [Q14344-2]
DR PIR; I57490; I57490.
DR RefSeq; NP_001269354.1; NM_001282425.1. [Q14344-2]
DR RefSeq; NP_006563.2; NM_006572.5. [Q14344-1]
DR PDB; 7T6B; EM; 3.19 A; A=17-377.
DR PDBsum; 7T6B; -.
DR AlphaFoldDB; Q14344; -.
DR SMR; Q14344; -.
DR BioGRID; 115914; 163.
DR CORUM; Q14344; -.
DR IntAct; Q14344; 28.
DR MINT; Q14344; -.
DR STRING; 9606.ENSP00000400717; -.
DR iPTMnet; Q14344; -.
DR MetOSite; Q14344; -.
DR PhosphoSitePlus; Q14344; -.
DR SwissPalm; Q14344; -.
DR BioMuta; GNA13; -.
DR DMDM; 38258936; -.
DR EPD; Q14344; -.
DR jPOST; Q14344; -.
DR MassIVE; Q14344; -.
DR MaxQB; Q14344; -.
DR PaxDb; Q14344; -.
DR PeptideAtlas; Q14344; -.
DR PRIDE; Q14344; -.
DR ProteomicsDB; 25652; -.
DR ProteomicsDB; 59969; -. [Q14344-1]
DR Antibodypedia; 31626; 271 antibodies from 30 providers.
DR DNASU; 10672; -.
DR Ensembl; ENST00000439174.7; ENSP00000400717.2; ENSG00000120063.10. [Q14344-1]
DR Ensembl; ENST00000541118.1; ENSP00000439647.1; ENSG00000120063.10. [Q14344-2]
DR GeneID; 10672; -.
DR KEGG; hsa:10672; -.
DR MANE-Select; ENST00000439174.7; ENSP00000400717.2; NM_006572.6; NP_006563.2.
DR UCSC; uc002jfc.4; human. [Q14344-1]
DR CTD; 10672; -.
DR DisGeNET; 10672; -.
DR GeneCards; GNA13; -.
DR HGNC; HGNC:4381; GNA13.
DR HPA; ENSG00000120063; Tissue enhanced (bone).
DR MIM; 604406; gene.
DR neXtProt; NX_Q14344; -.
DR OpenTargets; ENSG00000120063; -.
DR PharmGKB; PA28766; -.
DR VEuPathDB; HostDB:ENSG00000120063; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000157054; -.
DR HOGENOM; CLU_014184_3_1_1; -.
DR InParanoid; Q14344; -.
DR OMA; TSRFACM; -.
DR PhylomeDB; Q14344; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; Q14344; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q14344; -.
DR SIGNOR; Q14344; -.
DR BioGRID-ORCS; 10672; 39 hits in 1083 CRISPR screens.
DR ChiTaRS; GNA13; human.
DR GeneWiki; GNA13; -.
DR GenomeRNAi; 10672; -.
DR Pharos; Q14344; Tbio.
DR PRO; PR:Q14344; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14344; protein.
DR Bgee; ENSG00000120063; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; Q14344; baseline and differential.
DR Genevisible; Q14344; HS.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031752; F:D5 dopamine receptor binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031584; P:activation of phospholipase D activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000469; Gprotein_alpha_12/13.
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; PR00440; GPROTEINA12.
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 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Nucleus; Palmitate; Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..377
FT /note="Guanine nucleotide-binding protein subunit alpha-13"
FT /id="PRO_0000203773"
FT DOMAIN 47..377
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 50..63
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 195..203
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 218..227
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 287..294
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 347..352
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 58..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 197..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 291..294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT BINDING 349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27601"
FT MOD_RES 203
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:12399457"
FT LIPID 14
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10747909"
FT LIPID 18
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10747909"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055140"
FT VARIANT 221
FT /note="V -> L (in dbSNP:rs1062597)"
FT /evidence="ECO:0000269|PubMed:7791744"
FT /id="VAR_017160"
FT MUTAGEN 14
FT /note="C->S: Fails to localize to plasma membranes and
FT failed to activate Rho-dependent serum response factor-
FT mediated transcription and actin stress fiber formation."
FT /evidence="ECO:0000269|PubMed:10747909"
FT MUTAGEN 18
FT /note="C->S: Fails to localize to plasma membranes and
FT failed to activate Rho-dependent serum response factor-
FT mediated transcription and actin stress fiber formation."
FT /evidence="ECO:0000269|PubMed:10747909"
FT MUTAGEN 203
FT /note="T->A: Abolishes phosphorylation by PKA; disrupts
FT heterotrimer stability."
FT /evidence="ECO:0000269|PubMed:12399457"
FT CONFLICT 211
FT /note="F -> L (in Ref. 3; BAH13696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 44050 MW; 929B7B6473C54F2E CRC64;
MADFLPSRSV LSVCFPGCLL TSGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG
KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNSNQQHGD
KMMSFDTRAP MAAQGMVETR VFLQYLPAIR ALWADSGIQN AYDRRREFQL GESVKYFLDN
LDKLGEPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV
TSILFLVSSS EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
QIVSIKDYFL EFEGDPHCLR DVQKFLVECF RNKRRDQQQK PLYHHFTTAI NTENIRLVFR
DVKDTILHDN LKQLMLQ
