RALA_DROME
ID RALA_DROME Reviewed; 201 AA.
AC P48555; Q540X1; Q9W4Q6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras-related protein Ral-a;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P11233};
DE Flags: Precursor;
GN Name=Rala; ORFNames=CG2849;
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].
RC TISSUE=Eye imaginal disk;
RA Winge P., Fleming J.T., Settleman J., Hariharan I.K.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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].
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).
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:P11233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P11233};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11233};
CC Lipid-anchor {ECO:0000250|UniProtKB:P11233}; Cytoplasmic side. Cleavage
CC furrow {ECO:0000250|UniProtKB:P11233}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:P11233}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; U23800; AAC34902.1; -; mRNA.
DR EMBL; AE014298; AAF45889.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45890.1; -; Genomic_DNA.
DR EMBL; AY118912; AAM50772.1; -; mRNA.
DR RefSeq; NP_525063.1; NM_080324.4.
DR RefSeq; NP_726882.1; NM_166986.3.
DR PDB; 5CM8; X-ray; 2.60 A; B=1-201.
DR PDB; 5CM9; X-ray; 2.60 A; C/D=1-201.
DR PDBsum; 5CM8; -.
DR PDBsum; 5CM9; -.
DR AlphaFoldDB; P48555; -.
DR SMR; P48555; -.
DR BioGRID; 57853; 41.
DR DIP; DIP-19199N; -.
DR IntAct; P48555; 3.
DR STRING; 7227.FBpp0070558; -.
DR SwissPalm; P48555; -.
DR PaxDb; P48555; -.
DR PRIDE; P48555; -.
DR DNASU; 31332; -.
DR EnsemblMetazoa; FBtr0070583; FBpp0070558; FBgn0015286.
DR EnsemblMetazoa; FBtr0070584; FBpp0070559; FBgn0015286.
DR GeneID; 31332; -.
DR KEGG; dme:Dmel_CG2849; -.
DR CTD; 5898; -.
DR FlyBase; FBgn0015286; Rala.
DR VEuPathDB; VectorBase:FBgn0015286; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000168700; -.
DR InParanoid; P48555; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P48555; -.
DR SignaLink; P48555; -.
DR BioGRID-ORCS; 31332; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rala; fly.
DR GenomeRNAi; 31332; -.
DR PRO; PR:P48555; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0015286; Expressed in cleaving embryo and 36 other tissues.
DR ExpressionAtlas; P48555; baseline and differential.
DR Genevisible; P48555; DM.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0030165; F:PDZ domain binding; IPI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IDA:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:FlyBase.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:FlyBase.
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 InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..198
FT /note="Ras-related protein Ral-a"
FT /id="PRO_0000082697"
FT PROPEP 199..201
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281348"
FT MOTIF 40..48
FT /note="Effector region"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
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 MOD_RES 198
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 198
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:5CM8"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:5CM8"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5CM8"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:5CM8"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:5CM8"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5CM8"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5CM8"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5CM8"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:5CM8"
SQ SEQUENCE 201 AA; 22938 MW; 37F27FD84A813838 CRC64;
MSKKPTAGPA LHKVIMVGSG GVGKSALTLQ FMYDEFVEDY EPTKADSYRK KVVLDGEEVQ
IDILDTAGQE DYAAIRDNYF RSGEGFLCVF SITDDESFQA TQEFREQILR VKNDESIPFL
LVGNKCDLND KRKVPLSECQ LRAQQWAVPY VETSAKTREN VDKVFFDLMR EIRSRKTEDS
KATSGRAKDR CKKRRLKCTL L
