KBRAS_CAEEL
ID KBRAS_CAEEL Reviewed; 199 AA.
AC Q19143; Q1NZ24; Q20640; Q95QF4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NF-kappa-B inhibitor-interacting Ras-like protein;
DE Short=Kappa B-Ras;
DE Short=KappaB-Ras;
GN Name=kbrl-1 {ECO:0000312|WormBase:F52A8.6c};
GN ORFNames=F52A8.6 {ECO:0000312|WormBase:F52A8.6c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Atypical Ras-like protein that may act as a regulator of NF-
CC kappa-B activity. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=c {ECO:0000312|WormBase:F52A8.6c};
CC IsoId=Q19143-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F52A8.6a};
CC IsoId=Q19143-2; Sequence=VSP_038728;
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 Lys and Val
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; Z71263; CAA95826.1; -; Genomic_DNA.
DR EMBL; Z72506; CAA95826.1; JOINED; Genomic_DNA.
DR EMBL; Z72506; CAC42277.1; -; Genomic_DNA.
DR PIR; T20540; T20540.
DR RefSeq; NP_001040668.1; NM_001047203.2. [Q19143-1]
DR RefSeq; NP_492076.1; NM_059675.6. [Q19143-2]
DR AlphaFoldDB; Q19143; -.
DR SMR; Q19143; -.
DR STRING; 6239.F52A8.6a; -.
DR EPD; Q19143; -.
DR PaxDb; Q19143; -.
DR EnsemblMetazoa; F52A8.6a.1; F52A8.6a.1; WBGene00009919. [Q19143-2]
DR EnsemblMetazoa; F52A8.6c.1; F52A8.6c.1; WBGene00009919. [Q19143-1]
DR GeneID; 172487; -.
DR KEGG; cel:CELE_F52A8.6; -.
DR UCSC; F52A8.6b; c. elegans.
DR CTD; 172487; -.
DR WormBase; F52A8.6a; CE20840; WBGene00009919; kbrl-1. [Q19143-2]
DR WormBase; F52A8.6c; CE28028; WBGene00009919; kbrl-1. [Q19143-1]
DR eggNOG; KOG3883; Eukaryota.
DR GeneTree; ENSGT00940000168563; -.
DR HOGENOM; CLU_070670_0_0_1; -.
DR InParanoid; Q19143; -.
DR OMA; ACIEDIT; -.
DR OrthoDB; 1382000at2759; -.
DR PhylomeDB; Q19143; -.
DR PRO; PR:Q19143; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009919; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q19143; baseline and differential.
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 SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Alternative splicing; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..199
FT /note="NF-kappa-B inhibitor-interacting Ras-like protein"
FT /id="PRO_0000225684"
FT REGION 1..199
FT /note="Small GTPase-like"
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 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MLKLKNKHVKTGKCANTPTRFHRRCIRVGDNLTNKRVRFFGSASNSC
FT EFLYYLFKENWIRPSSRKFSLGVTPRALSRIDATSTPSLDVPQKATNRRFSLAATFFDA
FT AKADRKTSLCVEKDYLNHQGRYRTVADPDLERPLFVERSEEKGVRTFRSDSIKPARSRR
FT M (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_038728"
SQ SEQUENCE 199 AA; 22569 MW; B24841EAB04B550A CRC64;
MGRAMRVVVV GGKKVGKTAI LRQVACVEDV TNKPYEPTIE DTYQVLLEEP DKAREILILH
DTAGVSNYGP IELKKAYVQA ADAFVLVYSS ADYESFNRVD LLKKWIDRQF GKDKKEVPIV
VLANMRDRPA TVDSAFAHSW AAREKVKLFE VTAKDRQSLV DFIHYVGHRH FHPTKESKFS
LSKKLKSEKS SNPAILMDF