ID   Q4VAE6_MOUSE            Unreviewed;       193 AA.
AC   Q4VAE6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Transforming protein RhoA {ECO:0000256|ARBA:ARBA00039694};
GN   Name=Rhoa {ECO:0000313|EMBL:AAH96423.1, ECO:0000313|MGI:MGI:1096342};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH96423.1};
RN   [1] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:AAH96423.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II {ECO:0000313|EMBL:AAH96423.1};
RC   TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously
RC   {ECO:0000313|EMBL:AAH96423.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [7] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE29592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29592.1}, and NOD
RC   {ECO:0000313|EMBL:BAE42800.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE42800.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29592.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [11] {ECO:0000313|EMBL:AFR23588.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AFR23588.1};
RA   Suo L., Lu H., Wu Q.;
RT   "Pcdh clusters regulate dendritic complexity through CAKs and Rho
RT   GTPases.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000256|ARBA:ARBA00004510}. Cleavage furrow
CC       {ECO:0000256|ARBA:ARBA00004626}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004423}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000256|ARBA:ARBA00010142}.
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DR   EMBL; BC096423; AAH96423.1; -; mRNA.
DR   EMBL; JN971019; AFR23588.1; -; mRNA.
DR   EMBL; AK150475; BAE29592.1; -; mRNA.
DR   EMBL; AK152629; BAE31372.1; -; mRNA.
DR   EMBL; AK172051; BAE42800.1; -; mRNA.
DR   RefSeq; NP_001300890.1; NM_001313961.1.
DR   RefSeq; NP_001300891.1; NM_001313962.1.
DR   RefSeq; NP_058082.2; NM_016802.5.
DR   AlphaFoldDB; Q4VAE6; -.
DR   SMR; Q4VAE6; -.
DR   PeptideAtlas; Q4VAE6; -.
DR   TopDownProteomics; Q4VAE6; -.
DR   Antibodypedia; 30508; 839 antibodies from 39 providers.
DR   DNASU; 11848; -.
DR   GeneID; 11848; -.
DR   KEGG; mmu:11848; -.
DR   AGR; MGI:1096342; -.
DR   CTD; 387; -.
DR   MGI; MGI:1096342; Rhoa.
DR   VEuPathDB; HostDB:ENSMUSG00000007815; -.
DR   HOGENOM; CLU_041217_21_2_1; -.
DR   OMA; SKYSARC; -.
DR   OrthoDB; 20499at2759; -.
DR   BioGRID-ORCS; 11848; 18 hits in 76 CRISPR screens.
DR   ChiTaRS; Rhoa; mouse.
DR   ExpressionAtlas; Q4VAE6; baseline and differential.
DR   GO; GO:0043296; C:apical junction complex; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0017022; F:myosin binding; IEA:Ensembl.
DR   GO; GO:0003189; P:aortic valve formation; IEA:Ensembl.
DR   GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:1990869; P:cellular response to chemokine; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR   GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0097498; P:endothelial tube lumen extension; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR   GO; GO:1903673; P:mitotic cleavage furrow formation; IEA:Ensembl.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR   GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0035385; P:Roundabout signaling pathway; IEA:Ensembl.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR   CDD; cd01870; RhoA_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR   PANTHER; PTHR24072:SF153; TRANSFORMING PROTEIN RHOA; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   193 AA;  21782 MW;  C4C8BDC31FF858BC CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ
     ARRGKKKSGC LIL
//