RHOAC_DANRE
ID RHOAC_DANRE Reviewed; 193 AA.
AC Q7T2E8; F1R5L0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Rho-related GTP-binding protein RhoA-C {ECO:0000305};
DE Flags: Precursor;
GN Name=rhoac {ECO:0000303|PubMed:15894457,
GN ECO:0000312|ZFIN:ZDB-GENE-040426-2665};
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 {ECO:0000312|EMBL:AAH54576.1};
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].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH54576.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NOMENCLATURE.
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; CABZ01063935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01063936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054576; AAH54576.1; -; mRNA.
DR RefSeq; NP_998515.1; NM_213350.1.
DR AlphaFoldDB; Q7T2E8; -.
DR SMR; Q7T2E8; -.
DR STRING; 7955.ENSDARP00000072903; -.
DR PaxDb; Q7T2E8; -.
DR Ensembl; ENSDART00000192851; ENSDARP00000151463; ENSDARG00000116058.
DR GeneID; 406659; -.
DR KEGG; dre:406659; -.
DR CTD; 406659; -.
DR ZFIN; ZDB-GENE-040426-2665; rhoac.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; Q7T2E8; -.
DR TreeFam; TF300837; -.
DR Reactome; R-DRE-416482; G alpha (12/13) signalling events.
DR Reactome; R-DRE-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DRE-5625900; RHO GTPases activate CIT.
DR Reactome; R-DRE-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR PRO; PR:Q7T2E8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000116058; Expressed in mature ovarian follicle and 27 other tissues.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; 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:0043005; C:neuron projection; 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:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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-C"
FT /id="PRO_0000434739"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT /id="PRO_0000434740"
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; 21851 MW; 0066D253A34998C7 CRC64;
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDS KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR INAFGYLECS AKTKDGVREV FEMATRAALQ
ARKRGKKSGC LLL
