RAGP1_DROME
ID RAGP1_DROME Reviewed; 596 AA.
AC Q9VIW3; Q9XZI5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ran GTPase-activating protein;
DE Short=RanGAP;
DE AltName: Full=Protein segregation distorter;
GN Name=RanGAP; Synonyms=Sd; ORFNames=CG9999;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Testis;
RX PubMed=10073941; DOI=10.1126/science.283.5408.1742;
RA Merrill C., Bayraktaroglu L., Kusano A., Ganetzky B.;
RT "Truncated RanGAP encoded by the Segregation Distorter locus of
RT Drosophila.";
RL Science 283:1742-1745(1999).
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433; THR-434 AND SER-436, 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).
RN [6]
RP IDENTIFICATION IN COMPLEX WITH NUP358; SBR AND NXT1, AND ASSOCIATION WITH
RP NUCLEAR PORE COMPLEX.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [7]
RP ASSOCIATION WITH NUCLEAR PORE COMPLEX.
RX PubMed=17032737; DOI=10.1242/jcs.03201;
RA Xylourgidis N., Roth P., Sabri N., Tsarouhas V., Samakovlis C.;
RT "The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates
RT NFkappaB activation in Drosophila.";
RL J. Cell Sci. 119:4409-4419(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31626769; DOI=10.1016/j.cell.2019.09.022;
RA Hampoelz B., Schwarz A., Ronchi P., Bragulat-Teixidor H., Tischer C.,
RA Gaspar I., Ephrussi A., Schwab Y., Beck M.;
RT "Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.";
RL Cell 179:671-686.E17(2019).
CC -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein Ran, converting it to the putatively inactive GDP-bound state
CC (By similarity). Trans-acting factor necessary for meiotic distortion
CC (PubMed:10073941). Distortion is only seen in individuals that carry
CC the RanGAP tandem duplication and express a RanGAP truncated protein.
CC Binding of truncated RanGAP product to the Responder(RSP) locus
CC initiates events that lead to sperm dysfunction (PubMed:10073941).
CC During oogenesis, plays a role in the biogenesis of annulate lamellae
CC containing nuclear pore complex components (PubMed:31626769).
CC {ECO:0000250|UniProtKB:Q684P5, ECO:0000269|PubMed:10073941,
CC ECO:0000269|PubMed:31626769}.
CC -!- SUBUNIT: Forms a complex with Nup358/RanBP2, sbr/Nxf1 and Nxt1
CC (PubMed:14729961). Associates with the nuclear pore complex via its
CC interaction with Nup358/RanBP2 (PubMed:14729961, PubMed:17032737).
CC {ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:17032737}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17032737}. Nucleus
CC membrane {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:31626769};
CC Peripheral membrane protein {ECO:0000269|PubMed:17032737}; Cytoplasmic
CC side {ECO:0000269|PubMed:17032737}. Note=Association to cytoplasmic
CC side of the nuclear pore complex is promoted by Nup214
CC (PubMed:17032737). Co-localizes with Nup358/RanBP2 to annulate lamellae
CC (PubMed:31626769). {ECO:0000269|PubMed:17032737,
CC ECO:0000269|PubMed:31626769}.
CC -!- TISSUE SPECIFICITY: Both full-length and truncated protein are
CC expressed in testis (at protein level) (PubMed:10073941). Expressed in
CC oocytes and nurse cells (at protein level) (PubMed:31626769).
CC {ECO:0000269|PubMed:10073941, ECO:0000269|PubMed:31626769}.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR EMBL; AF143860; AAD31518.1; -; mRNA.
DR EMBL; AE014134; AAF53801.1; -; Genomic_DNA.
DR EMBL; AY061219; AAL28767.1; -; mRNA.
DR RefSeq; NP_001260578.1; NM_001273649.1.
DR RefSeq; NP_476712.1; NM_057364.4.
DR AlphaFoldDB; Q9VIW3; -.
DR SMR; Q9VIW3; -.
DR BioGRID; 61202; 38.
DR DIP; DIP-23850N; -.
DR IntAct; Q9VIW3; 4.
DR MINT; Q9VIW3; -.
DR STRING; 7227.FBpp0080775; -.
DR iPTMnet; Q9VIW3; -.
DR PaxDb; Q9VIW3; -.
DR PRIDE; Q9VIW3; -.
DR DNASU; 35223; -.
DR EnsemblMetazoa; FBtr0081234; FBpp0080775; FBgn0003346.
DR EnsemblMetazoa; FBtr0334174; FBpp0306291; FBgn0003346.
DR GeneID; 35223; -.
DR KEGG; dme:Dmel_CG9999; -.
DR CTD; 35223; -.
DR FlyBase; FBgn0003346; RanGAP.
DR VEuPathDB; VectorBase:FBgn0003346; -.
DR eggNOG; KOG1909; Eukaryota.
DR GeneTree; ENSGT00440000039203; -.
DR InParanoid; Q9VIW3; -.
DR OrthoDB; 1357476at2759; -.
DR PhylomeDB; Q9VIW3; -.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9VIW3; -.
DR BioGRID-ORCS; 35223; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 35223; -.
DR PRO; PR:Q9VIW3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003346; Expressed in eye disc (Drosophila) and 78 other tissues.
DR ExpressionAtlas; Q9VIW3; baseline and differential.
DR Genevisible; Q9VIW3; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; TAS:FlyBase.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0006611; P:protein export from nucleus; IMP:FlyBase.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.200; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR036720; RanGAP1_C_sf.
DR Pfam; PF13516; LRR_6; 4.
DR SUPFAM; SSF69099; SSF69099; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Leucine-rich repeat; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..596
FT /note="Ran GTPase-activating protein"
FT /id="PRO_0000056740"
FT REPEAT 44..71
FT /note="LRR 1"
FT REPEAT 107..134
FT /note="LRR 2"
FT REPEAT 137..164
FT /note="LRR 3"
FT REPEAT 203..230
FT /note="LRR 4"
FT REPEAT 231..258
FT /note="LRR 5"
FT REPEAT 259..286
FT /note="LRR 6"
FT REGION 355..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 434
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 117
FT /note="D -> E (in Ref. 1; AAD31518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66070 MW; 257C9783E23464CD CRC64;
MSTFNFASMA AQLGQEQGIS FENKVLSWNT AADVQDVVDA LNKQTTVHYL NLDGNTLGVE
AAKAIGEGLK RHPEFRKALW KNMFTGRLIS EIPEALKHLG AALIVAGAKL TVLDLSDNAL
GPNGMRGLEE LLRSPVCYSL QELLLCNCGL GPEGGSMLSR ALIDLHANAN KAGFPLQLRV
FIGSRNRLED AGATEMATAF QTLKTFEEIV LEQNSIYIEG VEALAESFKH NPHLRVLNMN
DNTLKSEGAE KIAEALPFLP LLREMSFGDC LIKTNGAYHF GEALERGNER LEVIDLGFNE
INSDGGLVLV NAMGNKPKLR ILNLDGNSFG EEGSEKIISE MSKLPTAAAL QPFQHQEEED
LEDEYQADKQ DADYEEEEEV HEHANDTTEE ADEDSEGDED DEEDEGDEEY SNVAEETAYV
TTNAYTTKLF NDTTNSMASE TFAVANKTIS QKCTPEKFCL SQKPCSQEDF DSLDMDNKLE
ALQSIVNQFT GDNHLLLLVF TTLKCAHLSQ SSKAALDLAV SLYQATFDYA IKTKQETRVL
NYVLMQLRLL PCKEVFHSDY DVKNCRFALR EALKQPTFAN DNIKNSFKTF LEGAES
