(data stored in ACNUC8465 zone)

SWISSPROT: RHOAA_DANRE

ID   RHOAA_DANRE             Reviewed;         193 AA.
AC   Q6NUX8;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 135.
DE   RecName: Full=Rho-related GTP-binding protein RhoA-A {ECO:0000305};
DE   Flags: Precursor;
GN   Name=rhoaa {ECO:0000303|PubMed:15894457,
GN   ECO:0000312|ZFIN:ZDB-GENE-040426-2150};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [2]
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.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   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.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH56556.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION), AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=26190758; DOI=10.1038/ncomms8807;
RA   Jank T., Eckerle S., Steinemann M., Trillhaase C., Schimpl M.,
RA   Wiese S., van Aalten D.M., Driever W., Aktories K.;
RT   "Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere
RT   cell 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
CC       stress 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
CC       ruckeri toxin Afp18. Mono-O-GlcNAcylation by Afp18 inhibits RhoA
CC       activation by guanine nucleotide exchange factors and blocks RhoA
CC       signaling. {ECO:0000305|PubMed:26190758}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
DR   EMBL; AY865555; AAX20127.1; -; mRNA.
DR   EMBL; BX004884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC056556; AAH56556.1; -; mRNA.
DR   EMBL; BC068390; AAH68390.1; -; mRNA.
DR   RefSeq; NP_998302.1; NM_213137.1.
DR   SMR; Q6NUX8; -.
DR   STRING; 7955.ENSDARP00000040644; -.
DR   PaxDb; Q6NUX8; -.
DR   PRIDE; Q6NUX8; -.
DR   Ensembl; ENSDART00000040645; ENSDARP00000040644; ENSDARG00000026845.
DR   Ensembl; ENSDART00000177931; ENSDARP00000144555; ENSDARG00000026845.
DR   GeneID; 406411; -.
DR   KEGG; dre:406411; -.
DR   CTD; 406411; -.
DR   ZFIN; ZDB-GENE-040426-2150; rhoaa.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00950000182945; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; Q6NUX8; -.
DR   KO; K04513; -.
DR   OMA; MSNRINA; -.
DR   OrthoDB; 1166960at2759; -.
DR   PhylomeDB; Q6NUX8; -.
DR   TreeFam; TF300837; -.
DR   PRO; PR:Q6NUX8; -.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000026845; Expressed in 26 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q6NUX8; baseline.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0051017; P:actin filament bundle assembly; 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:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
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   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q6NUX8.
DR   SWISS-2DPAGE; Q6NUX8.
KW   Cell membrane; Complete proteome; Glycoprotein; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome.
FT   CHAIN         1    190       Rho-related GTP-binding protein RhoA-A.
FT                                /FTId=PRO_0000434735.
FT   PROPEP      191    193       Removed in mature form.
FT                                {ECO:0000250|UniProtKB:P61586}.
FT                                /FTId=PRO_0000434736.
FT   NP_BIND      12     19       GTP. {ECO:0000250|UniProtKB:P61586}.
FT   NP_BIND      59     63       GTP. {ECO:0000250}.
FT   NP_BIND     117    120       GTP. {ECO:0000250|UniProtKB:P61586}.
FT   MOD_RES     190    190       Cysteine methyl ester.
FT                                {ECO:0000250|UniProtKB:P62745}.
FT   LIPID       190    190       S-geranylgeranyl cysteine.
FT                                {ECO:0000250|UniProtKB:P62745}.
FT   CARBOHYD     34     34       O-linked (GlcNAc) tyrosine; by Yersinia
FT                                Afp18. {ECO:0000305|PubMed:26190758}.
SQ   SEQUENCE   193 AA;  21893 MW;  1B7DD8BC9AF869C7 CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDS KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRNDEHTRRE LQKMKQEPVK PEEGRDMANR INAFGYLECS AKTKEGVREV FEMATRAALQ
     AKKRGKKNAC ALL
//

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