KBRAS_DROME
ID KBRAS_DROME Reviewed; 201 AA.
AC Q9V4L4; Q86P69; Q9NH91;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NF-kappa-B inhibitor-interacting Ras-like protein;
DE Short=Kappa B-Ras;
DE Short=KappaB-Ras;
GN Name=kappaB-Ras; ORFNames=CG1669;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INTERACTION WITH CACT.
RX PubMed=10657303; DOI=10.1126/science.287.5454.869;
RA Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.;
RT "A subclass of Ras proteins that regulate the degradation of IkappaB.";
RL Science 287:869-873(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Atypical Ras-like protein that may act as a regulator of NF-
CC kappa-B activity, possibly by preventing the degradation of NF-kappa-B
CC inhibitor cactus. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NF-kappa-B inhibitor cactus.
CC {ECO:0000269|PubMed:10657303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9V4L4-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V4L4-2; Sequence=VSP_017413;
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 18 and 71, which are replaced by Lys 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF229841; AAF35000.1; -; mRNA.
DR EMBL; AE013599; AAF59256.1; -; Genomic_DNA.
DR EMBL; AY061054; AAL28602.1; -; mRNA.
DR EMBL; BT003452; AAO39455.1; ALT_INIT; mRNA.
DR RefSeq; NP_001137613.1; NM_001144141.3. [Q9V4L4-1]
DR RefSeq; NP_001260770.1; NM_001273841.1. [Q9V4L4-1]
DR RefSeq; NP_610278.1; NM_136434.5. [Q9V4L4-1]
DR AlphaFoldDB; Q9V4L4; -.
DR SMR; Q9V4L4; -.
DR IntAct; Q9V4L4; 2.
DR STRING; 7227.FBpp0088074; -.
DR PaxDb; Q9V4L4; -.
DR DNASU; 35667; -.
DR EnsemblMetazoa; FBtr0089002; FBpp0088074; FBgn0040513. [Q9V4L4-1]
DR EnsemblMetazoa; FBtr0299801; FBpp0289079; FBgn0040513. [Q9V4L4-1]
DR EnsemblMetazoa; FBtr0336926; FBpp0307863; FBgn0040513. [Q9V4L4-1]
DR GeneID; 35667; -.
DR KEGG; dme:Dmel_CG1669; -.
DR UCSC; CG1669-RA; d. melanogaster. [Q9V4L4-1]
DR CTD; 35667; -.
DR FlyBase; FBgn0040513; kappaB-Ras.
DR VEuPathDB; VectorBase:FBgn0040513; -.
DR eggNOG; KOG3883; Eukaryota.
DR GeneTree; ENSGT00940000168563; -.
DR HOGENOM; CLU_041217_17_0_1; -.
DR InParanoid; Q9V4L4; -.
DR OMA; HPPQTKS; -.
DR PhylomeDB; Q9V4L4; -.
DR SignaLink; Q9V4L4; -.
DR BioGRID-ORCS; 35667; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35667; -.
DR PRO; PR:Q9V4L4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0040513; Expressed in saliva-secreting gland and 10 other tissues.
DR Genevisible; Q9V4L4; DM.
DR GO; GO:0005525; F:GTP binding; ISM:FlyBase.
DR GO; GO:0032794; F:GTPase activating protein binding; IBA:GO_Central.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:FlyBase.
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; IPR001806; Small_GTPase.
DR PANTHER; PTHR46152; PTHR46152; 1.
DR Pfam; PF00071; Ras; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..201
FT /note="NF-kappa-B inhibitor-interacting Ras-like protein"
FT /id="PRO_0000225685"
FT REGION 3..201
FT /note="Small GTPase-like"
FT MOTIF 40..48
FT /note="Effector region"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 38
FT /note="T -> TV (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10657303"
FT /id="VSP_017413"
SQ SEQUENCE 201 AA; 22807 MW; 74F4AE5FBCC776BC CRC64;
MLNAKIGKVG KVLVCGMKGV GKTALIEQLV YGHVNPETEL HPTIEDIYVA SVDTGRGGAR
ETLRIYDTAG LQGEQQQLPR HYLQFPDAFV LVYDPMDPRS LDMLADIKAD IEKHKEKKEI
PVVVLANVRA RAAPNPVEKV MDRANIWCQR ERIKHYTVNA MERPSLYEPF TTLCARLHPM
QTKSTFPQLR QVMQNRQKSE A
