RANT_RAT
ID RANT_RAT Reviewed; 216 AA.
AC Q8K586;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTP-binding nuclear protein Ran, testis-specific isoform;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62826};
GN Name=Rasl2-9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12211070; DOI=10.1002/mrd.10164;
RA Kierszenbaum A.L., Gil M., Rivkin E., Tres L.L.;
RT "Ran, a GTP-binding protein involved in nucleocytoplasmic transport and
RT microtubule nucleation, relocates from the manchette to the centrosome
RT region during rat spermiogenesis.";
RL Mol. Reprod. Dev. 63:131-140(2002).
CC -!- FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport.
CC Required for the import of protein into the nucleus and also for RNA
CC export. Involved in chromatin condensation and control of cell cycle
CC (By similarity). {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12211070}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12211070}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF507943; AAM33416.1; -; mRNA.
DR RefSeq; NP_001160147.1; NM_001166675.1.
DR AlphaFoldDB; Q8K586; -.
DR SMR; Q8K586; -.
DR BioGRID; 623649; 3.
DR IntAct; Q8K586; 2.
DR STRING; 10116.ENSRNOP00000039019; -.
DR iPTMnet; Q8K586; -.
DR PhosphoSitePlus; Q8K586; -.
DR jPOST; Q8K586; -.
DR PaxDb; Q8K586; -.
DR PRIDE; Q8K586; -.
DR Ensembl; ENSRNOT00000050233; ENSRNOP00000039019; ENSRNOG00000032913.
DR GeneID; 751812; -.
DR KEGG; rno:751812; -.
DR UCSC; RGD:2314256; rat.
DR CTD; 19428; -.
DR RGD; 2314256; Rasl2-9.
DR eggNOG; KOG0096; Eukaryota.
DR GeneTree; ENSGT00940000153786; -.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; Q8K586; -.
DR OMA; AQCAVIM; -.
DR OrthoDB; 1083175at2759; -.
DR PhylomeDB; Q8K586; -.
DR TreeFam; TF106302; -.
DR PRO; PR:Q8K586; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000032913; Expressed in testis and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; GTP-binding; Hydrolase; Isopeptide bond; 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, testis-specific
FT isoform"
FT /id="PRO_0000208700"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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 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; 24451 MW; 6756F467B8B6DA59 CRC64;
MAGQGKPQIQ FKLVLVGDGG TGKTTFMKRH LTGEFEKEYV ATLGVEVHTL VFHTNRGPIK
FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPSWHKDLVR VCENIPIVLC
GNKVDIKDMK VKAKPILFHR KKNLQYYDIS AKSNYNFEKP FFWLARKLIG DPNLEFVAMP
ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEEDDL
