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 27-MAR-2024, entry version 209. 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). RN [23] {ECO:0007744|PDB:8H8J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 34-377, AND RP INTERACTION WITH GPR35. RX PubMed=36543774; DOI=10.1038/s41421-022-00499-8; RA Duan J., Liu Q., Yuan Q., Ji Y., Zhu S., Tan Y., He X., Xu Y., Shi J., RA Cheng X., Jiang H., Eric Xu H., Jiang Y.; RT "Insights into divalent cation regulation and G13-coupling of orphan RT receptor GPR35."; RL Cell Discov. 8:135-135(2022). 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). Interacts CC with GPR35 (PubMed:36543774). Interacts with GPR174 (By similarity). 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 ECO:0000269|PubMed:36543774}. 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; 7SF7; EM; 2.90 A; B=17-377. DR PDB; 7SF8; EM; 2.70 A; B=17-377. DR PDB; 7T6B; EM; 3.19 A; A=17-377. DR PDB; 7YDH; EM; 3.10 A; A=17-377. DR PDB; 8H8J; EM; 3.20 A; A=34-377. DR PDBsum; 7SF7; -. DR PDBsum; 7SF8; -. DR PDBsum; 7T6B; -. DR PDBsum; 7YDH; -. DR PDBsum; 8H8J; -. DR AlphaFoldDB; Q14344; -. DR EMDB; EMD-25076; -. DR EMDB; EMD-25077; -. DR EMDB; EMD-25712; -. DR EMDB; EMD-32883; -. DR EMDB; EMD-33747; -. DR EMDB; EMD-34549; -. DR SMR; Q14344; -. DR BioGRID; 115914; 172. DR CORUM; Q14344; -. DR IntAct; Q14344; 30. DR MINT; Q14344; -. DR STRING; 9606.ENSP00000400717; -. DR GlyGen; Q14344; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000400717; -. DR PeptideAtlas; Q14344; -. DR ProteomicsDB; 25652; -. DR ProteomicsDB; 59969; -. [Q14344-1] DR Pumba; Q14344; -. DR Antibodypedia; 31626; 304 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 AGR; HGNC:4381; -. 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; RFACMRC; -. DR OrthoDB; 2897309at2759; -. 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; 46 hits in 1174 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 196 other cell types or tissues. DR ExpressionAtlas; Q14344; baseline and differential. 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: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: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: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; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF85; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT ALPHA-13; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00440; GPROTEINA12. 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; Q14344; HS. 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 FT factor-mediated transcription and actin stress fiber FT 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 FT factor-mediated transcription and actin stress fiber FT 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" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:7SF7" FT HELIX 28..40 FT /evidence="ECO:0007829|PDB:7SF8" FT HELIX 42..46 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 49..54 FT /evidence="ECO:0007829|PDB:7SF8" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:7SF7" FT HELIX 61..66 FT /evidence="ECO:0007829|PDB:7SF8" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 206..215 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 217..223 FT /evidence="ECO:0007829|PDB:7SF8" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:7SF8" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:8H8J" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:7T6B" FT HELIX 265..276 FT /evidence="ECO:0007829|PDB:7SF8" FT TURN 280..283 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:7SF8" FT HELIX 296..299 FT /evidence="ECO:0007829|PDB:7SF8" FT TURN 300..302 FT /evidence="ECO:0007829|PDB:7SF8" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:7SF8" FT HELIX 319..331 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:8H8J" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:7SF8" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:7SF7" FT HELIX 354..374 FT /evidence="ECO:0007829|PDB:7SF8" 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 //