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RAN1_ARATH
ID   RAN1_ARATH              Reviewed;         221 AA.
AC   P41916;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=GTP-binding nuclear protein Ran-1;
DE   AltName: Full=Ras-related nuclear protein 1;
GN   Name=RAN1; OrderedLocusNames=At5g20010; ORFNames=F28I16.160;
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].
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   [2]
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   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INTERACTION WITH XPO1.
RC   STRAIN=cv. Columbia;
RX   PubMed=10652141; DOI=10.1046/j.1365-313x.1999.00644.x;
RA   Haasen D., Koehler C., Neuhaus G., Merkle T.;
RT   "Nuclear export of proteins in plants: AtXPO1 is the export receptor for
RT   leucine-rich nuclear export signals in Arabidopsis thaliana.";
RL   Plant J. 20:695-705(1999).
RN   [8]
RP   INTERACTION WITH TRN1.
RX   PubMed=14756317; DOI=10.1023/b:plan.0000009288.46713.1f;
RA   Ziemienowicz A., Haasen D., Staiger D., Merkle T.;
RT   "Arabidopsis transportin1 is the nuclear import receptor for the circadian
RT   clock-regulated RNA-binding protein AtGRP7.";
RL   Plant Mol. Biol. 53:201-212(2003).
RN   [9]
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   [10]
RP   INTERACTION WITH NTF2B.
RC   STRAIN=cv. Columbia;
RX   PubMed=16428596; DOI=10.1104/pp.105.075499;
RA   Zhao Q., Leung S., Corbett A.H., Meier I.;
RT   "Identification and characterization of the Arabidopsis orthologs of
RT   nuclear transport factor 2, the nuclear import factor of ran.";
RL   Plant Physiol. 140:869-878(2006).
RN   [11]
RP   INTERACTION WITH ATX1.
RX   PubMed=17223078; DOI=10.1016/j.bbrc.2006.12.215;
RA   Puig S., Mira H., Dorcey E., Sancenon V., Andres-Colas N.,
RA   Garcia-Molina A., Burkhead J.L., Gogolin K.A., Abdel-Ghany S.E.,
RA   Thiele D.J., Ecker J.R., Pilon M., Penarrubia L.;
RT   "Higher plants possess two different types of ATX1-like copper
RT   chaperones.";
RL   Biochem. Biophys. Res. Commun. 354:385-390(2007).
RN   [12]
RP   INDUCTION.
RX   PubMed=18481083; DOI=10.1007/s00425-008-0745-x;
RA   Lee Y., Kim M.-H., Kim S.-K., Kim S.-H.;
RT   "Phytochrome-mediated differential gene expression of plant Ran/TC4 small
RT   G-proteins.";
RL   Planta 228:215-224(2008).
RN   [13]
RP   INTERACTION WITH MOS14.
RX   PubMed=21738492; DOI=10.1371/journal.pgen.1002159;
RA   Xu S., Zhang Z., Jing B., Gannon P., Ding J., Xu F., Li X., Zhang Y.;
RT   "Transportin-SR is required for proper splicing of resistance genes and
RT   plant immunity.";
RL   PLoS Genet. 7:E1002159-E1002159(2011).
RN   [14]
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 TRN1 (PubMed:14756317). Interacts with
CC       ATX1 (PubMed:17223078). Interacts with KPNB1 (PubMed:23582042). Binds
CC       to XPO1 (PubMed:10652141). Interacts with MOS14 (PubMed:21738492).
CC       Binds to NTF2B (PubMed:16428596). {ECO:0000250|UniProtKB:P62825,
CC       ECO:0000269|PubMed:10652141, ECO:0000269|PubMed:14756317,
CC       ECO:0000269|PubMed:16428596, ECO:0000269|PubMed:17223078,
CC       ECO:0000269|PubMed:21738492, ECO:0000269|PubMed:23582042,
CC       ECO:0000269|PubMed:9025305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Regulated by light. {ECO:0000269|PubMed:18481083}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
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DR   EMBL; L16789; AAA32851.1; -; mRNA.
DR   EMBL; X97379; CAA66047.1; -; mRNA.
DR   EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92779.1; -; Genomic_DNA.
DR   EMBL; AF428417; AAL16185.1; -; mRNA.
DR   EMBL; AY125542; AAM78052.1; -; mRNA.
DR   EMBL; AY088774; AAM67087.1; -; mRNA.
DR   RefSeq; NP_197501.1; NM_122008.3.
DR   AlphaFoldDB; P41916; -.
DR   SMR; P41916; -.
DR   BioGRID; 17399; 11.
DR   IntAct; P41916; 4.
DR   STRING; 3702.AT5G20010.1; -.
DR   iPTMnet; P41916; -.
DR   PaxDb; P41916; -.
DR   PRIDE; P41916; -.
DR   ProteomicsDB; 236517; -.
DR   EnsemblPlants; AT5G20010.1; AT5G20010.1; AT5G20010.
DR   GeneID; 832123; -.
DR   Gramene; AT5G20010.1; AT5G20010.1; AT5G20010.
DR   KEGG; ath:AT5G20010; -.
DR   Araport; AT5G20010; -.
DR   TAIR; locus:2147700; AT5G20010.
DR   eggNOG; KOG0096; Eukaryota.
DR   HOGENOM; CLU_041217_13_0_1; -.
DR   OMA; MESNGHQ; -.
DR   OrthoDB; 1083175at2759; -.
DR   PhylomeDB; P41916; -.
DR   PRO; PR:P41916; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P41916; baseline and differential.
DR   Genevisible; P41916; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; 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:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP: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-1"
FT                   /id="PRO_0000208717"
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"
SQ   SEQUENCE   221 AA;  25276 MW;  672097A226E51A64 CRC64;
     MALPNQQTVD YPSFKLVIVG DGGTGKTTFV KRHLTGEFEK KYEPTIGVEV HPLDFFTNCG
     KIRFYCWDTA GQEKFGGLRD GYYIHGQCAI IMFDVTARLT YKNVPTWHRD LCRVCENIPI
     VLCGNKVDVK NRQVKAKQVT FHRKKNLQYY EISAKSNYNF EKPFLYLARK LAGDQNLHFV
     ETPALAPPEV HIDIADQQKN EAELLQAAAQ PLPDDDDDIF E
 
 
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