KBRS1_DANRE
ID KBRS1_DANRE Reviewed; 192 AA.
AC Q6DGQ1; A5PMZ9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NF-kappa-B inhibitor-interacting Ras-like protein 1;
DE AltName: Full=I-kappa-B-interacting Ras-like protein 1;
DE Short=Kappa B-Ras protein 1;
DE Short=KappaB-Ras1;
GN Name=nkiras1; ORFNames=si:dkey-126a1.3, zgc:92823;
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].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Atypical Ras-like protein that acts as a potent regulator of
CC NF-kappa-B activity by preventing the degradation of NF-kappa-B
CC inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more
CC resistant to degradation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: In contrast to other members of the Ras family, the members of
CC the KappaB-Ras subfamily do not contain the conserved Gly and Gln
CC residues in positions 13 and 65, which are replaced by Ala and Leu
CC residues, respectively, and are therefore similar to the constitutively
CC active forms of oncogenic forms of Ras. This suggests that members of
CC this family are clearly different from other small GTPases proteins.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC KappaB-Ras subfamily. {ECO:0000305}.
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DR EMBL; BX927163; CAN87987.1; -; Genomic_DNA.
DR EMBL; BC076289; AAH76289.1; -; mRNA.
DR RefSeq; NP_001093546.1; NM_001100076.1.
DR AlphaFoldDB; Q6DGQ1; -.
DR SMR; Q6DGQ1; -.
DR STRING; 7955.ENSDARP00000043219; -.
DR PaxDb; Q6DGQ1; -.
DR Ensembl; ENSDART00000162383; ENSDARP00000135507; ENSDARG00000099527.
DR GeneID; 100002175; -.
DR KEGG; dre:100002175; -.
DR CTD; 28512; -.
DR ZFIN; ZDB-GENE-040718-215; nkiras1.
DR eggNOG; KOG3883; Eukaryota.
DR GeneTree; ENSGT00940000159705; -.
DR HOGENOM; CLU_041217_17_0_1; -.
DR InParanoid; Q6DGQ1; -.
DR OMA; ADMAQQW; -.
DR OrthoDB; 1382000at2759; -.
DR PhylomeDB; Q6DGQ1; -.
DR TreeFam; TF314483; -.
DR Reactome; R-DRE-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-DRE-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-DRE-933542; TRAF6 mediated NF-kB activation.
DR PRO; PR:Q6DGQ1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000099527; Expressed in ovary and 21 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032794; F:GTPase activating protein binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR GO; GO:0032484; P:Ral protein signal transduction; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR042227; KBRS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46152; PTHR46152; 1.
DR Pfam; PF00071; Ras; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..192
FT /note="NF-kappa-B inhibitor-interacting Ras-like protein 1"
FT /id="PRO_0000225678"
FT REGION 1..192
FT /note="Small GTPase-like"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 70
FT /note="D -> G (in Ref. 2; AAH76289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21546 MW; 800040B9E0A15CDF CRC64;
MGKGCKVVVC GMASVGKTAI LEQLLYGSHT VGAETSDTQE DIYVASVETD RGVREQLRLY
DTRGLREGLD LPKHFFSVAD GFVLVYSVDC LESFKKVEVL KKEIDRSRDK KEVMVMVLGN
KCELRERRQV DQDTAQQWAR GEKVKLWEVT VTDRSTLIEP FTSLTSRLTQ PQSKSAFPLP
GRKSKGTPSN DI
