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RAN_BOVIN
ID   RAN_BOVIN               Reviewed;         216 AA.
AC   Q3T054;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 130.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. The complex with BIRC5/survivin plays a role
CC       in mitotic spindle formation by serving as a physical scaffold to help
CC       deliver the RAN effector molecule TPX2 to microtubules. Acts as a
CC       negative regulator of the kinase activity of VRK1 and VRK2. Enhances
CC       AR-mediated transactivation. {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. Found in a nuclear export complex with RANBP3 and XPO1. Interacts
CC       with RANBP2/NUP358. Interaction with RANBP1 or RANBP2 induces a
CC       conformation change in the complex formed by XPO1 and RAN that triggers
CC       the release of the nuclear export signal of cargo proteins. Component
CC       of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and
CC       XPO1 (By similarity). Found in a nuclear export complex with RAN, XPO5
CC       and pre-miRNA (By similarity). Interacts (GTP-bound form) with XPO5 (By
CC       similarity). Part of a complex consisting of RANBP9, RAN, DYRK1B and
CC       COPS5. Interacts with RANBP9 and RANBP10. Interacts in its GTP-bound
CC       form with BIRC5/survivin at S and M phases of the cell cycle. Interacts
CC       with TERT; the interaction requires hydrogen peroxide-mediated
CC       phosphorylation of TERT and transports TERT to the nucleus. Interacts
CC       with MAD2L2. Interacts with VRK1 and VRK3. Interacts with VRK2 (By
CC       similarity). Interacts with NEMP1 and KPNB1 (By similarity). Interacts
CC       (GDP-bound form) with NUTF2; regulates RAN nuclear import. Interacts
CC       with CAPG; mediates CAPG nuclear import. Interacts with NUP153.
CC       Interacts with the AR N-terminal poly-Gln region; the interaction with
CC       AR is inversely correlated with the poly-Gln length (By similarity).
CC       Interacts with MYCBP2, which promotes RAN-mediated GTP hydrolysis (By
CC       similarity). Interacts with EPG5 (By similarity).
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}. Melanosome
CC       {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during
CC       interphase. Becomes dispersed throughout the cytoplasm during mitosis
CC       (By similarity). Identified by mass spectrometry in melanosome
CC       fractions from stage I to stage IV (By similarity).
CC       {ECO:0000250|UniProtKB:P62826}.
CC   -!- PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis,
CC       impairs RANGRF binding and enhances RCC1 binding. Acetylation at Lys-37
CC       enhances the association with nuclear export components. Deacetylation
CC       of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit
CC       RELA/p65. {ECO:0000250|UniProtKB:P62826}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
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DR   EMBL; BC102559; AAI02560.1; -; mRNA.
DR   RefSeq; NP_001029877.1; NM_001034705.1.
DR   AlphaFoldDB; Q3T054; -.
DR   BMRB; Q3T054; -.
DR   SMR; Q3T054; -.
DR   PaxDb; Q3T054; -.
DR   PeptideAtlas; Q3T054; -.
DR   PRIDE; Q3T054; -.
DR   Ensembl; ENSBTAT00000077257; ENSBTAP00000067034; ENSBTAG00000055033.
DR   GeneID; 540457; -.
DR   KEGG; bta:540457; -.
DR   CTD; 5901; -.
DR   VEuPathDB; HostDB:ENSBTAG00000055033; -.
DR   eggNOG; KOG0096; Eukaryota.
DR   GeneTree; ENSGT00940000153786; -.
DR   InParanoid; Q3T054; -.
DR   OMA; TIVFHRK; -.
DR   OrthoDB; 1083175at2759; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000055033; Expressed in spermatid and 102 other tissues.
DR   ExpressionAtlas; Q3T054; baseline and differential.
DR   GO; GO:0005814; C:centriole; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0042565; C:RNA nuclear export complex; IEA:Ensembl.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
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:0070883; F:pre-miRNA binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:1902570; P:protein localization to nucleolus; IEA:Ensembl.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IEA:Ensembl.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IEA:Ensembl.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
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   Acetylation; Cell cycle; Cell division; Cytoplasm; GTP-binding; Hydrolase;
KW   Isopeptide bond; Magnesium; Metal-binding; Mitosis; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   CHAIN           2..216
FT                   /note="GTP-binding nuclear protein Ran"
FT                   /id="PRO_0000249772"
FT   REGION          211..216
FT                   /note="Interaction with RANBP1"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
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:P62825"
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:P62825"
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   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         24
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         37
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         134
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   MOD_RES         159
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62827"
FT   CROSSLNK        71
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   CROSSLNK        71
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
FT   CROSSLNK        152
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62826"
SQ   SEQUENCE   216 AA;  24423 MW;  D5C9B7275C34BCE0 CRC64;
     MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK
     FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC
     GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP
     ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL
 
 
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