RAN_DROME
ID RAN_DROME Reviewed; 216 AA.
AC Q9VZ23; Q9NH14; Q9NHN9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=GTP-binding nuclear protein Ran;
DE AltName: Full=Ras-related nuclear protein;
GN Name=Ran {ECO:0000312|FlyBase:FBgn0020255}; Synonyms=Ran10A;
GN ORFNames=CG1404 {ECO:0000312|FlyBase:FBgn0020255};
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:AAF60289.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nguyen H.T., Frasch M.;
RT "Drosophila Ran10A GTPase.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAF60289.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stivers C.W., Brody T., Odenwald W.F.;
RT "Drosophila Ran ORF.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAF48008.1}
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 [4]
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 [5] {ECO:0000312|EMBL:AAL28946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28946.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC Ovary {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 [6] {ECO:0000312|EMBL:AAF60289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39578.1}; TISSUE=Embryo;
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.
RN [7] {ECO:0000312|EMBL:AAF60289.1}
RP NUCLEOTIDE SEQUENCE OF 1-21.
RA Drivas G., Frasch M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:12121620};
RX PubMed=12121620; DOI=10.1016/s0960-9822(02)00934-x;
RA Trieselmann N., Wilde A.;
RT "Ran localizes around the microtubule spindle in vivo during mitosis in
RT Drosophila embryos.";
RL Curr. Biol. 12:1124-1129(2002).
RN [9] {ECO:0000305}
RP INTERACTION WITH TAMO, AND SUBCELLULAR LOCATION.
RX PubMed=12653959; DOI=10.1046/j.1365-2443.2002.00634.x;
RA Minakhina S., Yang J., Steward R.;
RT "Tamo selectively modulates nuclear import in Drosophila.";
RL Genes Cells 8:299-310(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF THR-24 AND GLN-69.
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 involved in nucleocytoplasmic transport, participating
CC both to the import and the export from the nucleus of proteins and
CC RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state
CC by nucleotide exchange and GTP hydrolysis. Nuclear import receptors
CC such as importin beta bind their substrates only in the absence of GTP-
CC bound RAN and release them upon direct interaction with GTP-bound RAN,
CC while export receptors behave in the opposite way. Thereby, RAN
CC controls cargo loading and release by transport receptors in the proper
CC compartment and ensures the directionality of the transport.
CC Interaction with RANBP1 induces a conformation change in the complex
CC formed by XPO1 and RAN that triggers the release of the nuclear export
CC signal of cargo proteins. RAN (GTP-bound form) triggers microtubule
CC assembly at mitotic chromosomes and is required for normal mitotic
CC spindle assembly and chromosome segregation. Required for normal
CC progress through mitosis (By similarity). GTP-bound Ran modulates both
CC spindle and nuclear envelope assembly, supporting a role during mitosis
CC (PubMed:12121620). During oogenesis, modulates formation of Nup358-
CC containing granules and biogenesis of the nuclear pore complex probably
CC by mediating the transport of their components along microtubules
CC (PubMed:31626769). {ECO:0000250|UniProtKB:P62826,
CC ECO:0000269|PubMed:12121620, ECO:0000269|PubMed:31626769}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P62826};
CC Note=Mg(2+) interacts primarily with the phosphate groups of the bound
CC guanine nucleotide. {ECO:0000250|UniProtKB:P62826};
CC -!- SUBUNIT: Found in a nuclear export complex with RanGTP, exportin and
CC pre-miRNA (By similarity). Interacts with tamo (PubMed:12653959).
CC {ECO:0000250|UniProtKB:P62825, ECO:0000269|PubMed:12653959}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12121620}. Nucleus
CC envelope {ECO:0000269|PubMed:12121620}. Cytoplasm
CC {ECO:0000269|PubMed:12121620, ECO:0000305|PubMed:12653959}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:12121620}. Note=Localizes
CC around the microtubule spindle during mitosis.
CC {ECO:0000269|PubMed:12121620}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
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DR EMBL; AF233584; AAF60289.1; -; mRNA.
DR EMBL; AF220950; AAF30287.1; -; mRNA.
DR EMBL; AE014298; AAF48008.1; -; Genomic_DNA.
DR EMBL; AY061398; AAL28946.1; -; mRNA.
DR EMBL; AY070533; AAL48004.1; -; mRNA.
DR EMBL; BT003574; AAO39578.1; -; mRNA.
DR EMBL; AF233585; AAF60290.1; -; mRNA.
DR RefSeq; NP_001285111.1; NM_001298182.1.
DR RefSeq; NP_001285112.1; NM_001298183.1.
DR RefSeq; NP_651969.1; NM_143712.4.
DR RefSeq; NP_727499.1; NM_167272.3.
DR AlphaFoldDB; Q9VZ23; -.
DR SMR; Q9VZ23; -.
DR BioGRID; 68814; 13.
DR ComplexPortal; CPX-3170; cdm-RanGTP complex.
DR IntAct; Q9VZ23; 10.
DR MINT; Q9VZ23; -.
DR STRING; 7227.FBpp0073328; -.
DR PaxDb; Q9VZ23; -.
DR PRIDE; Q9VZ23; -.
DR DNASU; 44072; -.
DR EnsemblMetazoa; FBtr0073471; FBpp0073327; FBgn0020255.
DR EnsemblMetazoa; FBtr0073472; FBpp0073328; FBgn0020255.
DR EnsemblMetazoa; FBtr0340164; FBpp0309150; FBgn0020255.
DR EnsemblMetazoa; FBtr0340165; FBpp0309151; FBgn0020255.
DR GeneID; 44072; -.
DR KEGG; dme:Dmel_CG1404; -.
DR UCSC; CG1404-RA; d. melanogaster.
DR CTD; 5901; -.
DR FlyBase; FBgn0020255; Ran.
DR VEuPathDB; VectorBase:FBgn0020255; -.
DR eggNOG; KOG0096; Eukaryota.
DR GeneTree; ENSGT00940000153786; -.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; Q9VZ23; -.
DR OMA; TIVFHRK; -.
DR OrthoDB; 1083175at2759; -.
DR PhylomeDB; Q9VZ23; -.
DR Reactome; R-DME-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9VZ23; -.
DR BioGRID-ORCS; 44072; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Ran; fly.
DR GenomeRNAi; 44072; -.
DR PRO; PR:Q9VZ23; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0020255; Expressed in cleaving embryo and 57 other tissues.
DR ExpressionAtlas; Q9VZ23; baseline and differential.
DR Genevisible; Q9VZ23; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IC:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; TAS:UniProtKB.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0051168; P:nuclear export; IC:ComplexPortal.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
DR GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; IC:ComplexPortal.
DR GO; GO:0006611; P:protein export from nucleus; ISS:FlyBase.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:FlyBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002041; Ran_GTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR24071; PTHR24071; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51418; RAN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding; Magnesium;
KW Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..216
FT /note="GTP-binding nuclear protein Ran"
FT /id="PRO_0000208710"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 36..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT BINDING 68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT BINDING 150..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT SITE 69
FT /note="Essential for GTP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P62826"
FT MUTAGEN 24
FT /note="T->N: Reduces numbers of granules containing
FT Nup358/RanBP2 and annulate lamellae containing nuclear pore
FT complex components in egg and nurse cells."
FT /evidence="ECO:0000269|PubMed:31626769"
FT MUTAGEN 69
FT /note="Q->L: Increases numbers of granules containing
FT Nup358/RanBP2 and annulate lamellae containing nuclear pore
FT complex components in egg and nurse cells."
FT /evidence="ECO:0000269|PubMed:31626769"
FT CONFLICT 90..93
FT /note="FDVT -> VDGN (in Ref. 2; AAF30287)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="WL -> CW (in Ref. 2; AAF30287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24708 MW; 95916B5D4C3413F6 CRC64;
MAQEGQDIPT FKCVLVGDGG TGKTTFVKRH MTGEFEKKYV ATLGVEVHPL IFHTNRGAIR
FNVWDTAGQE KFGGLRDGYY IQGQCAVIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC
GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLVG DPNLEFVAMP
ALLPPEVKMD KDWQAQIERD LQEAQATALP DEDEEL
