ID   RSLBL_DANRE             Reviewed;         253 AA.
AC   A1DZY4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Ras-like protein family member 11A-like;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
GN   ORFNames=zgc:110179;
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] {ECO:0000305, ECO:0000312|EMBL:ABK96901.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pezeron G., Lambert G., Rosa F.M., Mourrain P.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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., 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).
CC   -!- FUNCTION: Regulator of rDNA transcription. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P01116};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Associates
CC       with rDNA transcription unit throughout the cell cycle. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000255}.
CC   -!- CAUTION: Although highly related to the Ras family, lacks the conserved
CC       prenylation motif at the C-terminus, which serves to target Ras
CC       proteins to membrane compartments. {ECO:0000305}.
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DR   EMBL; EF088669; ABK96901.1; -; mRNA.
DR   EMBL; CR381676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001017840.2; NM_001017840.2.
DR   AlphaFoldDB; A1DZY4; -.
DR   SMR; A1DZY4; -.
DR   STRING; 7955.ENSDARP00000067646; -.
DR   PaxDb; A1DZY4; -.
DR   PRIDE; A1DZY4; -.
DR   Ensembl; ENSDART00000067647; ENSDARP00000067646; ENSDARG00000046013.
DR   GeneID; 550538; -.
DR   KEGG; dre:550538; -.
DR   CTD; 387496; -.
DR   ZFIN; ZDB-GENE-050417-384; rasl11a.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000164592; -.
DR   HOGENOM; CLU_041217_9_7_1; -.
DR   InParanoid; A1DZY4; -.
DR   OMA; LTHRFIG; -.
DR   OrthoDB; 1384728at2759; -.
DR   PhylomeDB; A1DZY4; -.
DR   TreeFam; TF318030; -.
DR   PRO; PR:A1DZY4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000046013; Expressed in spleen and 28 other tissues.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
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   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..253
FT                   /note="Ras-like protein family member 11A-like"
FT                   /id="PRO_0000308363"
FT   REGION          213..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43..50
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A58"
FT   BINDING         90..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A58"
FT   BINDING         157..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A58"
SQ   SEQUENCE   253 AA;  28052 MW;  04F31124694D6D67 CRC64;
     MRLLIEQPRT MSSGSSNFLL VPIPEYPVLD CVPNKNVKIV VLGASNVGKT ALIVRFLTKR
     FIGDYEANTG ALYSRKINLD GEQVSLQVQD TPCVSLQDDA DGLYCQEQIN RSIYWADGYV
     LVFSITDLNS YRTIQPLYQH VRRIHPSGNI PVIIVGNKSD LLRARQVSDP EGKALADELG
     GLYFEASARE NHESVQAAFL HLCQEVSRAL GGGNGEKRKG GLHLARPKSP NMQELKRRFR
     QVLSSKVKSA TAL