RHOAB_DANRE
ID RHOAB_DANRE Reviewed; 193 AA.
AC Q6DHM9; Q52WZ2;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rho-related GTP-binding protein RhoA-B {ECO:0000305};
DE Flags: Precursor;
GN Name=rhoab {ECO:0000303|PubMed:15894457};
GN ORFNames=zgc:153713 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-193.
RX PubMed=15894457; DOI=10.1016/j.ygeno.2005.03.010;
RA Salas-Vidal E., Meijer A.H., Cheng X., Spaink H.P.;
RT "Genomic annotation and expression analysis of the zebrafish Rho small
RT GTPase family during development and bacterial infection.";
RL Genomics 86:25-37(2005).
RN [4]
RP GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=26190758; DOI=10.1038/ncomms8807;
RA Jank T., Eckerle S., Steinemann M., Trillhaase C., Schimpl M., Wiese S.,
RA van Aalten D.M., Driever W., Aktories K.;
RT "Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell
RT behaviour in zebrafish embryos.";
RL Nat. Commun. 6:7807-7807(2015).
CC -!- FUNCTION: Regulates a signal transduction pathway linking plasma
CC membrane receptors to the assembly of focal adhesions and actin stress
CC fibers. {ECO:0000250|UniProtKB:P61586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26190758};
CC Lipid-anchor {ECO:0000250|UniProtKB:P61586}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P61586}.
CC -!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Yersinia ruckeri
CC toxin Afp18. Mono-O-GlcNAcylation by Afp18 inhibits RhoA activation by
CC guanine nucleotide exchange factors and blocks RhoA signaling.
CC {ECO:0000305|PubMed:26190758}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; BX784025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC075938; AAH75938.1; -; mRNA.
DR EMBL; BC171417; AAI71417.1; -; mRNA.
DR EMBL; BC171421; AAI71421.1; -; mRNA.
DR EMBL; AY865556; AAX20128.1; -; mRNA.
DR RefSeq; NP_997914.2; NM_212749.2.
DR RefSeq; XP_005167037.1; XM_005166980.3.
DR AlphaFoldDB; Q6DHM9; -.
DR SMR; Q6DHM9; -.
DR STRING; 7955.ENSDARP00000109720; -.
DR PaxDb; Q6DHM9; -.
DR PRIDE; Q6DHM9; -.
DR Ensembl; ENSDART00000024009; ENSDARP00000018377; ENSDARG00000094673.
DR Ensembl; ENSDART00000124300; ENSDARP00000109720; ENSDARG00000094673.
DR Ensembl; ENSDART00000127618; ENSDARP00000111732; ENSDARG00000094673.
DR GeneID; 100006041; -.
DR KEGG; dre:100006041; -.
DR CTD; 100006041; -.
DR ZFIN; ZDB-GENE-040322-2; rhoab.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q6DHM9; -.
DR OMA; GADMANR; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; Q6DHM9; -.
DR TreeFam; TF300837; -.
DR Reactome; R-DRE-114604; GPVI-mediated activation cascade.
DR Reactome; R-DRE-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-DRE-198203; PI3K/AKT activation.
DR Reactome; R-DRE-209563; Axonal growth stimulation.
DR Reactome; R-DRE-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-DRE-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DRE-4086400; PCP/CE pathway.
DR Reactome; R-DRE-416482; G alpha (12/13) signalling events.
DR Reactome; R-DRE-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-DRE-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DRE-5625900; RHO GTPases activate CIT.
DR Reactome; R-DRE-5625970; RHO GTPases activate KTN1.
DR Reactome; R-DRE-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-DRE-5689896; Ovarian tumor domain proteases.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR PRO; PR:Q6DHM9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000094673; Expressed in granulocyte and 37 other tissues.
DR ExpressionAtlas; Q6DHM9; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:ZFIN.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ZFIN.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:ZFIN.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IGI:ZFIN.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:ZFIN.
DR GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR GO; GO:0043149; P:stress fiber assembly; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..190
FT /note="Rho-related GTP-binding protein RhoA-B"
FT /id="PRO_0000434737"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT /id="PRO_0000434738"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 190
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT LIPID 190
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT CARBOHYD 34
FT /note="(Microbial infection) O-linked (GlcNAc) tyrosine; by
FT Yersinia Afp18"
FT /evidence="ECO:0000305|PubMed:26190758"
SQ SEQUENCE 193 AA; 21863 MW; 522D6E93090D1C5C CRC64;
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDS KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRNDEHTRRE LTKMKQEPVK AEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ
ARRGKKSNKC CLL
