RLIP_DROME
ID RLIP_DROME Reviewed; 625 AA.
AC Q9VDG2; O96392; Q8MZ58;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=RalA-binding protein 1;
DE Short=RalBP1;
DE AltName: Full=Ral-interacting protein 1;
GN Name=Rlip {ECO:0000312|EMBL:AAF55832.1}; ORFNames=CG11622;
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] {ECO:0000312|EMBL:AAD02099.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mirey G.N., Camonis J.H.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAF55832.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF55832.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAM29343.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND RNA EDITING OF POSITIONS 229;
RP 230; 233; 254 AND 265.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29343.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CYCB AND NUMB.
RX PubMed=12775724; DOI=10.1074/jbc.m302191200;
RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
RT phosphorylate epsin during the switch off of endocytosis in mitosis.";
RL J. Biol. Chem. 278:30597-30604(2003).
RN [6] {ECO:0000305}
RP RNA EDITING OF POSITIONS 229; 230; 233; 254 AND 265.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-69, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Participates in receptor endocytosis during interphase, is
CC also involved in mitotic processes when endocytosis is switched off.
CC {ECO:0000269|PubMed:12775724}.
CC -!- SUBUNIT: Interacts with CycB and numb. {ECO:0000269|PubMed:12775724}.
CC -!- RNA EDITING: Modified_positions=229 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 230 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 233 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 254 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 265 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29343.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF037470; AAD02099.1; -; mRNA.
DR EMBL; AE014297; AAF55832.1; -; Genomic_DNA.
DR EMBL; AY113338; AAM29343.1; ALT_SEQ; mRNA.
DR RefSeq; NP_650933.2; NM_142676.4.
DR AlphaFoldDB; Q9VDG2; -.
DR SMR; Q9VDG2; -.
DR BioGRID; 67455; 27.
DR IntAct; Q9VDG2; 8.
DR STRING; 7227.FBpp0083406; -.
DR iPTMnet; Q9VDG2; -.
DR PaxDb; Q9VDG2; -.
DR EnsemblMetazoa; FBtr0084002; FBpp0083406; FBgn0026056.
DR GeneID; 42484; -.
DR KEGG; dme:Dmel_CG11622; -.
DR UCSC; CG11622-RA; d. melanogaster.
DR CTD; 42484; -.
DR FlyBase; FBgn0026056; Rlip.
DR VEuPathDB; VectorBase:FBgn0026056; -.
DR eggNOG; KOG4370; Eukaryota.
DR GeneTree; ENSGT00940000154639; -.
DR HOGENOM; CLU_028068_0_1_1; -.
DR InParanoid; Q9VDG2; -.
DR OrthoDB; 514124at2759; -.
DR PhylomeDB; Q9VDG2; -.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR SignaLink; Q9VDG2; -.
DR BioGRID-ORCS; 42484; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42484; -.
DR PRO; PR:Q9VDG2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0026056; Expressed in brain and 26 other tissues.
DR ExpressionAtlas; Q9VDG2; baseline and differential.
DR Genevisible; Q9VDG2; DM.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; ISS:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:FlyBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IC:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; PTHR12783; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Developmental protein; GTPase activation; Phosphoprotein;
KW Reference proteome; Repeat; RNA editing.
FT CHAIN 1..625
FT /note="RalA-binding protein 1"
FT /id="PRO_0000278144"
FT DOMAIN 191..385
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 229
FT /note="I -> V (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 230
FT /note="E -> G (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 233
FT /note="K -> E (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 254
FT /note="E -> G (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 265
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT CONFLICT 123
FT /note="V -> F (in Ref. 1; AAD02099)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="H -> R (in Ref. 4; AAM29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Q -> R (in Ref. 4; AAM29343)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="T -> A (in Ref. 1; AAD02099)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="Q -> H (in Ref. 1; AAD02099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 71896 MW; 81D2DFCE13CD9B9F CRC64;
MDFDSPEEKE FPGLYASEAA DAKSRKSKEE SDFSEDHDHS KKDLLIGRRK DKKEKGKDRG
YAALEGESSP EEELDTKSPS KSKKSKTFKF TSSKSKEKRE KSRDKSEKDS KHAEEEPSVS
HKVKEKERDK EKDRDEPKKK DKEEKRKEKD KKADKKDKKD KKSKQLSQQQ DDVSAAEEVL
ALGYPVFGVS VSLATERSRC HDGVDIPLVV RDCIDFLQDH LKCEQIYKIE PIKTRLMHFK
RLYNNREHDS AVDELNLPTA CSLLKLFLRE LPEPLLTTDL VARFEEVASH PKVTTQQAEL
QQLLEQLPKC NRTLLAWVLL HFDAVIQQER HNKLNAQSLA MLLSPTLQMS HRLMVALLCH
CNNLFADVQL IKYVPPLTST SPKLPDTPED IQTELRKQDS LLSQIHSEMN AGFITKKREE
QLWEVQRIIT QLKRKLRTFE KKQEKTAEEV DNSSSAPPAV ASEDTTDSKP AGTPAVSTNN
SISQEEPKTD TLTPKDAPND FTIDPSTGFI LLPKSNPHRE NLLRLQIEYD ELMEWQNELK
ARIVAERNEV YRLKQLYEQQ SINSQMASLA SGSQAPPESD YERIIEHYTR ENALLEHKKN
MLGMELKEER RACIALQVEL RLQQF
