ID C3XVK6_BRAFL Unreviewed; 221 AA.
AC C3XVK6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=GTP-binding nuclear protein Ran {ECO:0000256|ARBA:ARBA00040533, ECO:0000256|RuleBase:RU363057};
GN Name=LOC118426421 {ECO:0000313|RefSeq:XP_035691687.1,
GN ECO:0000313|RefSeq:XP_035691688.1};
GN ORFNames=BRAFLDRAFT_282949 {ECO:0000313|EMBL:EEN68133.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN68133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN68133.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN68133.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035691687.1, ECO:0000313|RefSeq:XP_035691688.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035691687.1,
RC ECO:0000313|RefSeq:XP_035691688.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035691687.1,
RC ECO:0000313|RefSeq:XP_035691688.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU363057}.
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:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000256|ARBA:ARBA00008028, ECO:0000256|RuleBase:RU363057}.
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; GG666468; EEN68133.1; -; Genomic_DNA.
DR RefSeq; XP_002612124.1; XM_002612078.1.
DR RefSeq; XP_035691687.1; XM_035835794.1.
DR RefSeq; XP_035691688.1; XM_035835795.1.
DR STRING; 7739.C3XVK6; -.
DR KEGG; bfo:118426421; -.
DR eggNOG; KOG0096; Eukaryota.
DR InParanoid; C3XVK6; -.
DR OMA; NSGICCH; -.
DR OrthoDB; 5471873at2759; -.
DR Proteomes; UP000001554; Chromosome 11.
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 CDD; cd00877; Ran; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24071:SF0; GTP-BINDING NUCLEAR PROTEIN RAN; 1.
DR PANTHER; PTHR24071; RAN GTPASE; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51418; RAN; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU363057};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363057};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363057};
KW Protein transport {ECO:0000256|RuleBase:RU363057};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Transport {ECO:0000256|RuleBase:RU363057}.
FT REGION 193..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 25173 MW; E827CBC85779E9C2 CRC64;
MAQEIAGAND RQPATFKLVL VGDGGTGKTT FVKRHVTGEF EKKYVATLGV EVHPIKFNTN
RGEIKFNVWD TAGQEKFGGL RDGYYIQGQC AIIMFDVTSR VTYKNVPNWH RDLVRVCENI
PIVLCGNKVD IKDRKVKAKA ITFHRKKNLQ YYDISAKSNY NFEKPFLWLA RKLAGDANLE
FVEMPALQPP EVQMDPELAS QYERDLKQAQ ETALPEEDDD L
//
