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RAN3_ARATH
ID   RAN3_ARATH              Reviewed;         221 AA.
AC   Q8H156; O04148; O04664; O22495;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=GTP-binding nuclear protein Ran-3;
DE   AltName: Full=Ras-related nuclear protein 3;
GN   Name=RAN3; OrderedLocusNames=At5g55190; ORFNames=MCO15.14;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RA   Bischoff F., Palme K.;
RT   "A new member of the Ran-GTPases in Arabidopsis thaliana.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Pih K.T., Park J.M., Jang H.J., Kang S.G., Piao H.L., Hwang I.H.;
RT   "Isolation of salt stress inducible Ran1 isoform.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [5]
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   [6]
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   [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   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   [9]
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 KPNB1 (PubMed:23582042).
CC       {ECO:0000250|UniProtKB:P62825, ECO:0000269|PubMed:23582042,
CC       ECO:0000269|PubMed:9025305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Induced by salt treatment. Regulated by light.
CC       {ECO:0000269|PubMed:18481083}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
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DR   EMBL; X97381; CAA66049.1; -; mRNA.
DR   EMBL; U73810; AAB58478.1; -; mRNA.
DR   EMBL; U75601; AAC34900.1; -; mRNA.
DR   EMBL; AF017991; AAB97312.1; -; mRNA.
DR   EMBL; AB010071; BAB08588.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96598.1; -; Genomic_DNA.
DR   EMBL; AY042796; AAK68736.1; -; mRNA.
DR   EMBL; AY050317; AAK91334.1; -; mRNA.
DR   EMBL; AY116939; AAM51573.1; -; mRNA.
DR   EMBL; BT000723; AAN31865.1; -; mRNA.
DR   RefSeq; NP_200330.1; NM_124901.5.
DR   AlphaFoldDB; Q8H156; -.
DR   SMR; Q8H156; -.
DR   BioGRID; 20856; 8.
DR   IntAct; Q8H156; 3.
DR   STRING; 3702.AT5G55190.1; -.
DR   PaxDb; Q8H156; -.
DR   PRIDE; Q8H156; -.
DR   EnsemblPlants; AT5G55190.1; AT5G55190.1; AT5G55190.
DR   GeneID; 835612; -.
DR   Gramene; AT5G55190.1; AT5G55190.1; AT5G55190.
DR   KEGG; ath:AT5G55190; -.
DR   Araport; AT5G55190; -.
DR   TAIR; locus:2161600; AT5G55190.
DR   eggNOG; KOG0096; Eukaryota.
DR   HOGENOM; CLU_041217_13_0_1; -.
DR   InParanoid; Q8H156; -.
DR   OMA; IRFNIWD; -.
DR   OrthoDB; 1083175at2759; -.
DR   PhylomeDB; Q8H156; -.
DR   PRO; PR:Q8H156; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8H156; baseline and differential.
DR   Genevisible; Q8H156; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; 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-3"
FT                   /id="PRO_0000208719"
FT   REGION          201..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        38
FT                   /note="F -> P (in Ref. 1; CAA66049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="L -> P (in Ref. 3; AAC34900/AAB97312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="D -> E (in Ref. 6; AAN31865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="K -> R (in Ref. 3; AAC34900/AAB97312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145..146
FT                   /note="KN -> EE (in Ref. 3; AAC34900/AAB97312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="Q -> R (in Ref. 1; CAA66049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203..204
FT                   /note="EL -> DV (in Ref. 1; CAA66049)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   221 AA;  25080 MW;  96648D02606EDC0B CRC64;
     MALPNQQTVD YPSFKLVIVG DGGTGKTTFV KRHLTGEFEK KYEPTIGVEV HPLDFFTNCG
     KIRFYCWDTA GQEKFGGLRD GYYIHGQCAI IMFDVTARLT YKNVPTWHRD LCRVCENIPI
     VLCGNKVDVK NRQVKAKQVT FHRKKNLQYY EISAKSNYNF EKPFLYLARK LAGDANLHFV
     ESPALAPPEV QIDLAAQQQH EAELAAAASQ PLPDDDDDTF E
 
 
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