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RAN_ONCVO
ID   RAN_ONCVO               Reviewed;         215 AA.
AC   P38544;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=GTP-binding nuclear protein Ran;
DE   AltName: Full=GTPase Ran;
DE   AltName: Full=Ras-like protein TC4;
DE   AltName: Full=Ras-related nuclear protein;
GN   Name=ran-1;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1484550; DOI=10.1016/0166-6851(92)90175-j;
RA   Dissanayake S., Xu M., Piessens W.F.;
RT   "Filarial parasites contain a ras homolog of the TC4/ran/Spil family.";
RL   Mol. Biochem. Parasitol. 56:259-268(1992).
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. {ECO:0000250|UniProtKB:P62826}.
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: Monomer. Interacts with RANGAP1, which promotes RAN-mediated
CC       GTP hydrolysis. Interacts with KPNB1. Interaction with KPNB1 inhibits
CC       RANGAP1-mediated stimulation of GTPase activity. Interacts with RCC1
CC       which promotes the exchange of RAN-bound GDP by GTP. Interaction with
CC       KPNB1 inhibits RCC1-mediated exchange of RAN-bound GDP by GTP.
CC       Interacts (GTP-bound form) with TNPO1; the interaction is direct.
CC       Interacts with KPNB1 and with TNPO1; both inhibit RAN GTPase activity.
CC       Interacts (via C-terminus) with RANBP1, which alleviates the inhibition
CC       of RAN GTPase activity. Interacts with RANGRF, which promotes the
CC       release of bound guanine nucleotide. RANGRF and RCC1 compete for an
CC       overlapping binding site on RAN. Identified in a complex with KPNA2 and
CC       CSE1L; interaction with RANBP1 mediates dissociation of RAN from this
CC       complex. Interaction with both RANBP1 and KPNA2 promotes dissociation
CC       of the complex between RAN and KPNB1. Identified in a complex composed
CC       of RAN, RANGAP1 and RANBP1. Identified in a complex that contains
CC       TNPO1, RAN and RANBP1. Identified in a nuclear export complex with
CC       XPO1. Interaction with RANBP1 or RANBP2 induces a conformation change
CC       in the complex formed by XPO1 and RAN that triggers the release of the
CC       nuclear export signal of cargo proteins. Component of a nuclear export
CC       receptor complex composed of KPNB1, RAN, SNUPN and XPO1.
CC       {ECO:0000250|UniProtKB:P62825, ECO:0000250|UniProtKB:P62826,
CC       ECO:0000250|UniProtKB:P62827}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus
CC       envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62826}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during
CC       interphase. Becomes dispersed throughout the cytoplasm during mitosis
CC       (By similarity). {ECO:0000250|UniProtKB:P62826}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
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DR   EMBL; M98811; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M98812; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; B48463; B48463.
DR   AlphaFoldDB; P38544; -.
DR   SMR; P38544; -.
DR   STRING; 6282.P38544; -.
DR   HOGENOM; CLU_041217_13_0_1; -.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..215
FT                   /note="GTP-binding nuclear protein Ran"
FT                   /id="PRO_0000208713"
FT   REGION          210..215
FT                   /note="Interaction with RANBP1"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         35..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   BINDING         67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         149..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   SITE            68
FT                   /note="Essential for GTP hydrolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
SQ   SEQUENCE   215 AA;  24233 MW;  8F59B7A0022487CD CRC64;
     MATGDDIPTF KLVLVGDGGT GKTTFVKRHL TGDPEKKYVA TLGVEVHPLI FHTNRGQIRF
     NVWDTAGQEK FGGLRDGYYI QGQCAIIMFD VTARVTYKNV PNWHRDLARV CENIPIVLCG
     NFVDVKDRKV KAKTITFHRK KNLQYYDISA KSNYNFEKPS LWLVRKLLGD PNLEFVAMPA
     LAPPEVQMDP TMVAQYEQEI AAAANAELPD DDEDL
 
 
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