RAN_SALSA
ID RAN_SALSA Reviewed; 215 AA.
AC Q9YGC0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GTP-binding nuclear protein Ran;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62826};
DE AltName: Full=GTPase Ran;
DE AltName: Full=Ras-related nuclear protein;
GN Name=ran; Synonyms=ran1;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=10902908; DOI=10.3109/10425170009033968;
RA Lundin M.H., Mikkelsen B., Gudim M., Syed M.;
RT "The structure and expression of the Salmo salar Ran gene.";
RL DNA Seq. 11:41-50(2000).
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 -!- 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;
CC Evidence={ECO:0000250|UniProtKB:P62826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={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 (GTP-bound form) with TNPO3; 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; AJ012478; CAA10040.1; -; mRNA.
DR EMBL; AJ012477; CAA10039.1; -; Genomic_DNA.
DR RefSeq; NP_001117103.1; NM_001123631.1.
DR RefSeq; XP_014055038.1; XM_014199563.1.
DR RefSeq; XP_014067596.1; XM_014212121.1.
DR RefSeq; XP_014067597.1; XM_014212122.1.
DR AlphaFoldDB; Q9YGC0; -.
DR SMR; Q9YGC0; -.
DR STRING; 8030.ENSSSAP00000059417; -.
DR GeneID; 100136389; -.
DR GeneID; 100136528; -.
DR KEGG; sasa:100136389; -.
DR KEGG; sasa:100136528; -.
DR CTD; 100136528; -.
DR CTD; 5901; -.
DR OrthoDB; 1083175at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000074478; Expressed in brain and 15 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0061015; P:snRNA import into nucleus; ISS:UniProtKB.
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; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..215
FT /note="GTP-binding nuclear protein Ran"
FT /id="PRO_0000208706"
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:P62825"
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; 24373 MW; 70764DD44FBE81F3 CRC64;
MAEGEPQVQF KLVLVGDGGT GKTTFVKRHL TGEFEKKYVA TLGVEVHPLV FHTNRGAIKY
NVWDTAGQEK FGGLRDGYYI QAQCAIIMFD VTSRVTYKNV PNWHRDLVRV CENIPIVLCG
NKVDIKDRKV KAKSIVFHRK KNLQYYDISA KSNYNFEKPF LWLARKLIGD PNLEFVAMPA
LAPPEILMDP SLAAQYEHDL KVASETALPD EDDDL
