GNA13_RAT
ID GNA13_RAT Reviewed; 377 AA.
AC Q6Q7Y5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SHR, and Wistar Kyoto;
RA Jackson E.K., Zhu C.;
RT "Genetic similarity between spontaneously hypertensive rats and wistar-
RT kyoto rats in the coding regions of signal transduction proteins.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION, INTERACTION WITH PPP5C, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLN-226.
RX PubMed=12176367; DOI=10.1016/s0960-9822(02)01034-5;
RA Yamaguchi Y., Katoh H., Mori K., Negishi M.;
RT "Galpha(12) and Galpha(13) interact with Ser/Thr protein phosphatase type 5
RT and stimulate its phosphatase activity.";
RL Curr. Biol. 12:1353-1358(2002).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:12176367). Activates effector molecule RhoA by binding and
CC activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and
CC ARHGEF12/LARG) (By similarity). 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 (By similarity). Inhibits CDH1-
CC mediated cell adhesion in process independent from Rho activation (By
CC similarity). {ECO:0000250|UniProtKB:P27601,
CC ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:12176367}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma (By
CC similarity). The alpha chain contains the guanine nucleotide binding
CC site (By similarity). Interacts with UBXD5 (By similarity). Interacts
CC with HAX1 (By similarity). Interacts (in GTP-bound form) with PPP5C
CC (via TPR repeats); activates PPP5C phosphatase activity and
CC translocates PPP5C to the cell membrane (PubMed:12176367). Interacts
CC with RGS22 (By similarity). Interacts with ARHGEF1. Interacts (in GTP-
CC bound form) with ARHGEF11 (via RGS domain) (By similarity). Interacts
CC (in GTP-bound form) with ARHGEF12 (via RGS domain) (By similarity).
CC Interacts (in GTP-bound form) with CTNND1 (By similarity). Interacts
CC with GAS2L2 (By similarity). {ECO:0000250|UniProtKB:P27601,
CC ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:12176367}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12176367}; Lipid-
CC anchor {ECO:0000269|PubMed:12176367}. Melanosome
CC {ECO:0000250|UniProtKB:Q14344}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14344}. Nucleus {ECO:0000250|UniProtKB:Q14344}.
CC Note=Cytoplasmic in adult somatic cells, but mainly nuclear in
CC spermatids in the testes. Translocates from the cytoplasm to the
CC nucleus during spermatogenesis, hence predominantly observed in the
CC cytoplasm of round spermatids but localized in the nuclei of elongating
CC or elongated spermatids and testicular spermatozoa.
CC {ECO:0000250|UniProtKB:Q14344}.
CC -!- PTM: Palmitoylation is critical for proper membrane localization and
CC signaling. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of
CC alpha, beta and gamma, and inhibits Rho activation.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC {ECO:0000305}.
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DR EMBL; AY553631; AAS64389.1; -; mRNA.
DR EMBL; AY553632; AAS64390.1; -; mRNA.
DR EMBL; DQ120481; AAZ23820.1; -; mRNA.
DR EMBL; DQ120482; AAZ23821.1; -; mRNA.
DR RefSeq; NP_001013137.1; NM_001013119.1.
DR AlphaFoldDB; Q6Q7Y5; -.
DR SMR; Q6Q7Y5; -.
DR CORUM; Q6Q7Y5; -.
DR IntAct; Q6Q7Y5; 1.
DR STRING; 10116.ENSRNOP00000051938; -.
DR iPTMnet; Q6Q7Y5; -.
DR PhosphoSitePlus; Q6Q7Y5; -.
DR jPOST; Q6Q7Y5; -.
DR PaxDb; Q6Q7Y5; -.
DR PRIDE; Q6Q7Y5; -.
DR Ensembl; ENSRNOT00000118369; ENSRNOP00000076869; ENSRNOG00000063135.
DR GeneID; 303634; -.
DR KEGG; rno:303634; -.
DR CTD; 10672; -.
DR RGD; 1310221; Gna13.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000157054; -.
DR HOGENOM; CLU_014184_3_1_1; -.
DR OMA; TSRFACM; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q6Q7Y5; -.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q6Q7Y5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036745; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q6Q7Y5; RN.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031752; F:D5 dopamine receptor binding; IPI:RGD.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031584; P:activation of phospholipase D activity; IMP:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
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 Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Transducer.
FT CHAIN 1..377
FT /note="Guanine nucleotide-binding protein subunit alpha-13"
FT /id="PRO_0000424080"
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:0000250|UniProtKB:Q14344"
FT LIPID 14
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT LIPID 18
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT MUTAGEN 226
FT /note="Q->L: Constitutively active. Interacts with PPP5C,
FT activates its phosphatase activity and translocates PPP5C
FT to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:12176367"
SQ SEQUENCE 377 AA; 44012 MW; 076F9F65508E8416 CRC64;
MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG
KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQVHGD
KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWDDSGIQN AYDRRREFQL GESVKYFLDN
LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV
TSILFLVSSS EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR
DVKDTILHDN LKQLMLQ
