ID   KBRS1_MACFA             Reviewed;         192 AA.
AC   Q9BH04;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=QflA-10220;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (FEB-2001) 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. May act by blocking phosphorylation of NFKBIB
CC       and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It
CC       is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms
CC       block phosphorylation of NFKBIB (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA) and
CC       beta (NFKBIB) in vitro. However, it probably only interacts with NFKBIB
CC       in vivo. Forms a complex with NFKBIB and NF-kappa-B heterodimer
CC       (p50/NFKB1 and p65/RELA). Also interacts with c-Rel (REL) (By
CC       similarity). {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 Leu residues,
CC       and are therefore similar to the constitutively active forms of
CC       oncogenic forms of Ras. This suggests that members of this family are
CC       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; AB055252; BAB21876.1; -; mRNA.
DR   RefSeq; NP_001272051.1; NM_001285122.1.
DR   AlphaFoldDB; Q9BH04; -.
DR   SMR; Q9BH04; -.
DR   STRING; 9541.XP_005545709.1; -.
DR   Ensembl; ENSMFAT00000023650; ENSMFAP00000004981; ENSMFAG00000002166.
DR   GeneID; 102137307; -.
DR   CTD; 28512; -.
DR   VEuPathDB; HostDB:ENSMFAG00000002166; -.
DR   eggNOG; KOG3883; Eukaryota.
DR   GeneTree; ENSGT00940000159705; -.
DR   OMA; ADMAQQW; -.
DR   OrthoDB; 1382000at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000002166; Expressed in temporal lobe and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
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_0000225676"
FT   REGION          58..93
FT                   /note="Interactions with NFKBIA and NFKBIB"
FT                   /evidence="ECO:0000250"
FT   REGION          168..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"
SQ   SEQUENCE   192 AA;  21616 MW;  849484594E0853B0 CRC64;
     MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD RGVKEQLHLY
     DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN
     KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP
     GRKNKGNSSS EN