RAN2_ARATH
ID RAN2_ARATH Reviewed; 221 AA.
AC P41917; Q0WVD9; Q94K33;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=GTP-binding nuclear protein Ran-2 {ECO:0000303|PubMed:9025305};
DE AltName: Full=Ras-related nuclear protein 2 {ECO:0000303|PubMed:9025305};
GN Name=RAN2 {ECO:0000303|PubMed:9025305};
GN OrderedLocusNames=At5g20020 {ECO:0000312|Araport:AT5G20020};
GN ORFNames=F28I16.170 {ECO:0000312|EMBL:AF296836};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH RANBP1A AND RANBP1B.
RX PubMed=9025305; DOI=10.1046/j.1365-313x.1997.11010093.x;
RA Haizel T., Merkle T., Pay A., Fejes E., Nagy F.;
RT "Characterization of proteins that interact with the GTP-bound form of the
RT regulatory GTPase Ran in Arabidopsis.";
RL Plant J. 11:93-103(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-221.
RX PubMed=7987414; DOI=10.1046/j.1365-313x.1994.6040555.x;
RA Merkle T., Haizel T., Matsumoto T., Harter K., Dallmann G., Nagy F.;
RT "Phenotype of the fission yeast cell cycle regulatory mutant pim1-46 is
RT suppressed by a tobacco cDNA encoding a small, Ran-like GTP-binding
RT protein.";
RL Plant J. 6:555-565(1994).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12644670; DOI=10.1104/pp.013052;
RA Vernoud V., Horton A.C., Yang Z., Nielsen E.;
RT "Analysis of the small GTPase gene superfamily of Arabidopsis.";
RL Plant Physiol. 131:1191-1208(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PHRIP1.
RX PubMed=17530257; DOI=10.1007/s00299-007-0367-y;
RA Ma L., Hong Z., Zhang Z.;
RT "Perinuclear and nuclear envelope localizations of Arabidopsis Ran
RT proteins.";
RL Plant Cell Rep. 26:1373-1382(2007).
RN [9]
RP INTERACTION WITH PHIP1, AND DEVELOPMENTAL STAGE.
RX PubMed=18621982; DOI=10.1104/pp.108.120527;
RA Ma L., Xie B., Hong Z., Verma D.P.S., Zhang Z.;
RT "A novel RNA-binding protein associated with cell plate formation.";
RL Plant Physiol. 148:223-234(2008).
RN [10]
RP INTERACTION WITH KPNB1.
RX PubMed=23582042; DOI=10.1111/tpj.12207;
RA Luo Y., Wang Z., Ji H., Fang H., Wang S., Tian L., Li X.;
RT "An Arabidopsis homolog of importin beta1 is required for ABA response and
RT drought tolerance.";
RL Plant J. 75:377-389(2013).
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}.
CC -!- SUBUNIT: Found in a nuclear export complex with RanGTP, exportin and
CC pre-miRNA (By similarity). Interacts with RanBP1a and RanBP1b
CC (PubMed:9025305). Interacts with PHRIP1 (PubMed:17530257). Interacts
CC with KPNB1 (PubMed:23582042). Binds to PHIP1 (PubMed:18621982).
CC {ECO:0000250|UniProtKB:P62825, ECO:0000269|PubMed:17530257,
CC ECO:0000269|PubMed:18621982, ECO:0000269|PubMed:23582042,
CC ECO:0000269|PubMed:9025305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17530257}. Nucleus
CC envelope {ECO:0000269|PubMed:17530257}. Note=Localized in the
CC perinuclear region with the highest concentration at the nuclear
CC envelope at the interphase.
CC -!- DEVELOPMENTAL STAGE: RAN2 transcripts mRNA interacts with PHIP1 to be
CC distributed toward the cell plate during cytokinesis.
CC {ECO:0000269|PubMed:18621982}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
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DR EMBL; X97380; CAA66048.1; -; mRNA.
DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92780.1; -; Genomic_DNA.
DR EMBL; AF370337; AAK44152.1; -; mRNA.
DR EMBL; AY062997; AAL34171.1; -; mRNA.
DR EMBL; BT000424; AAN17401.1; -; mRNA.
DR EMBL; BT000659; AAN31806.1; -; mRNA.
DR EMBL; BT006264; AAP13372.1; -; mRNA.
DR EMBL; AK226813; BAE98909.1; -; mRNA.
DR EMBL; L16790; AAA32852.1; -; mRNA.
DR RefSeq; NP_197502.1; NM_122009.4.
DR AlphaFoldDB; P41917; -.
DR SMR; P41917; -.
DR BioGRID; 17400; 9.
DR IntAct; P41917; 4.
DR STRING; 3702.AT5G20020.1; -.
DR PaxDb; P41917; -.
DR PRIDE; P41917; -.
DR EnsemblPlants; AT5G20020.1; AT5G20020.1; AT5G20020.
DR GeneID; 832124; -.
DR Gramene; AT5G20020.1; AT5G20020.1; AT5G20020.
DR KEGG; ath:AT5G20020; -.
DR Araport; AT5G20020; -.
DR TAIR; locus:2147715; AT5G20020.
DR eggNOG; KOG0096; Eukaryota.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; P41917; -.
DR OMA; TCGHIPI; -.
DR OrthoDB; 1083175at2759; -.
DR PhylomeDB; P41917; -.
DR PRO; PR:P41917; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P41917; baseline and differential.
DR Genevisible; P41917; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; ISS:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..221
FT /note="GTP-binding nuclear protein Ran-2"
FT /id="PRO_0000208718"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 153..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT CONFLICT 198..199
FT /note="QQ -> PK (in Ref. 1; CAA66048 and 6; AAA32852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25062 MW; 349390AC56E05AFB CRC64;
MALPNQQTVD YPSFKLVIVG DGGTGKTTFV KRHLTGEFEK KYEPTIGVEV HPLDFFTNCG
KIRFYCWDTA GQEKFGGLRD GYYIHGQCAI IMFDVTARLT YKNVPTWHRD LCRVCENIPI
VLCGNKVDVK NRQVKAKQVT FHRKKNLQYY EISAKSNYNF EKPFLYLARK LAGDQNLHFV
ESPALAPPEV HLDIAAQQQN EADLAAAAAQ PLPDDDDDAF E
