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RENT2_ARATH
ID   RENT2_ARATH             Reviewed;        1181 AA.
AC   F4IUX6; O80955;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Regulator of nonsense transcripts UPF2;
DE   AltName: Full=Nonsense mRNA reducing factor UPF2;
DE   AltName: Full=Up-frameshift suppressor 2 homolog;
DE            Short=AtUpf2;
GN   Name=UPF2; OrderedLocusNames=At2g39260; ORFNames=T16B24.10;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19602621; DOI=10.1105/tpc.109.067736;
RA   Kim S.H., Koroleva O.A., Lewandowska D., Pendle A.F., Clark G.P.,
RA   Simpson C.G., Shaw P.J., Brown J.W.S.;
RT   "Aberrant mRNA transcripts and the nonsense-mediated decay proteins UPF2
RT   and UPF3 are enriched in the Arabidopsis nucleolus.";
RL   Plant Cell 21:2045-2057(2009).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=22353561; DOI=10.1111/j.1744-7909.2012.01093.x;
RA   Shi C., Baldwin I.T., Wu J.;
RT   "Arabidopsis plants having defects in nonsense-mediated mRNA decay factors
RT   UPF1, UPF2, and UPF3 show photoperiod-dependent phenotypes in development
RT   and stress responses.";
RL   J. Integr. Plant Biol. 54:99-114(2012).
CC   -!- FUNCTION: Recruited by UPF3 associated with the EJC core at the
CC       cytoplasmic side of the nuclear envelope and the subsequent formation
CC       of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to
CC       release factors at the stalled ribosome) is believed to activate NMD.
CC       In cooperation with UPF3 stimulates both ATPase and RNA helicase
CC       activities of UPF1. Binds spliced mRNA (By similarity). Involved in
CC       nonsense-mediated decay (NMD) of mRNAs containing premature stop codons
CC       by associating with the nuclear exon junction complex (EJC). Required
CC       for plant development and adaptation to environmental stresses,
CC       including plant defense and response to wounding. {ECO:0000250,
CC       ECO:0000269|PubMed:22353561}.
CC   -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP)
CC       complex. Associates with the exon junction complex (EJC). Interacts
CC       with UPF1 and UPF3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19602621}.
CC       Cytoplasm {ECO:0000269|PubMed:19602621}. Cytoplasm, perinuclear region
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Seedling lethal. Accumulation of mRNAs with
CC       premature termination codons (PTC). Photoperiod-dependent altered
CC       development and stress responses; in long days (16 hours light),
CC       altered organ morphologies (e.g. epinastic leaves, small rosette size,
CC       long seeds, some abnormal flowers and stunted stem growth), disturbed
CC       homeostasis of wounding-induced jasmonic acid and pathogen-elicited
CC       salicylic acid. Increased resistance to Pseudomonas syringae pv. tomato
CC       strain DC3000. {ECO:0000269|PubMed:22353561}.
CC   -!- SIMILARITY: Belongs to the RENT2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AK227294; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC004697; AAC28982.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09651.1; -; Genomic_DNA.
DR   EMBL; AK227294; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T02576; T02576.
DR   RefSeq; NP_181459.4; NM_129484.5.
DR   AlphaFoldDB; F4IUX6; -.
DR   SMR; F4IUX6; -.
DR   STRING; 3702.AT2G39260.1; -.
DR   iPTMnet; F4IUX6; -.
DR   PaxDb; F4IUX6; -.
DR   PRIDE; F4IUX6; -.
DR   ProteomicsDB; 236871; -.
DR   EnsemblPlants; AT2G39260.1; AT2G39260.1; AT2G39260.
DR   GeneID; 818511; -.
DR   Gramene; AT2G39260.1; AT2G39260.1; AT2G39260.
DR   KEGG; ath:AT2G39260; -.
DR   Araport; AT2G39260; -.
DR   TAIR; locus:2056038; AT2G39260.
DR   eggNOG; KOG2051; Eukaryota.
DR   HOGENOM; CLU_002633_2_0_1; -.
DR   InParanoid; F4IUX6; -.
DR   OMA; DFQHHQI; -.
DR   OrthoDB; 653534at2759; -.
DR   PRO; PR:F4IUX6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IUX6; baseline and differential.
DR   Genevisible; F4IUX6; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0048571; P:long-day photoperiodism; IMP:UniProtKB.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR   GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   InterPro; IPR039762; Nmd2/UPF2.
DR   InterPro; IPR007193; Upf2/Nmd2_C.
DR   PANTHER; PTHR12839; PTHR12839; 1.
DR   Pfam; PF02854; MIF4G; 3.
DR   Pfam; PF04050; Upf2; 1.
DR   SMART; SM00543; MIF4G; 3.
DR   SUPFAM; SSF48371; SSF48371; 3.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Plant defense; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..1181
FT                   /note="Regulator of nonsense transcripts UPF2"
FT                   /id="PRO_0000421874"
FT   DOMAIN          61..264
FT                   /note="MIF4G 1"
FT   DOMAIN          469..655
FT                   /note="MIF4G 2"
FT   DOMAIN          672..871
FT                   /note="MIF4G 3"
FT   REGION          309..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..755
FT                   /note="Binds to UPF3"
FT                   /evidence="ECO:0000250"
FT   REGION          893..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1181
FT                   /note="Sufficient for interaction with UPF1 C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          999..1102
FT                   /note="Necessary for interaction with UPF1"
FT                   /evidence="ECO:0000250"
FT   REGION          999..1023
FT                   /note="Interaction with UPF1"
FT                   /evidence="ECO:0000250"
FT   REGION          1066..1111
FT                   /note="Interaction with UPF1"
FT                   /evidence="ECO:0000250"
FT   REGION          1129..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          6..41
FT                   /evidence="ECO:0000255"
FT   COILED          260..309
FT                   /evidence="ECO:0000255"
FT   COILED          425..451
FT                   /evidence="ECO:0000255"
FT   COILED          539..559
FT                   /evidence="ECO:0000255"
FT   COILED          1000..1021
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        378..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..943
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1135..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1181 AA;  133962 MW;  17C1964D4C402B65 CRC64;
     MDHPEDESHS EKQDDEEALA RLEEIKKSIE AKLTLRQNNL NPERPDSAYL RTLDSSIKRN
     TAVIKKLKQI NEEQREGLMD DLRGVNLSKF VSEAVTAICE AKLKSSDIQA AVQICSLLHQ
     RYKEFSASLT QGLLKVFFPG KSAEDLEADK NSKAMKKRST LKLLLELYYV GVIEDSNIFI
     NIIKDLTSVE QLKDRDTTQT NLTLLTSFAR QGRIFLGLPI SGQDEDFFKG LDVTADQKKS
     FKKAFNTYYD ALADLLQSEH KLLLQMEKEN AKLVNAKGEL SEDSASSYEK LRKSYDHLYR
     NISSLAEALD MQPPVMPEDG TTRLTAGDEA SPSGTVKDTS VPEPIWDDED TKTFYECLPD
     LRAFVPAVLL GEAEPKSNEQ SAKAKEKLSE SSSEVVENQQ TTEDTTEVSA DSASMDDRSN
     AEQPKEKEEV EKEKAKDTKK EKGKEKDSEK KMEHEKEKGK SLDVANFERL LQRLPGCVSR
     DLIDQLTVEY CYLNSKTNRK KLVKALFNVP RTSLELLAYY SRMVATLASC MKDIPSMLVQ
     MLEDEFNSLV HKKDQMNIET KIRNIRFIGE LCKFKIVPAG LVFSCLKACL DEFTHHNIDV
     ACNLLETCGR FLYRSPETTL RMTNMLDILM RLKNVKNLDP RQSTLVENAY YLCKPPERSA
     RISKVRPPLH QYVRKLLFSD LDKDSIANVL KQLRKLPWSE CEQYILKCFM KVHKGKYGQI
     HLIASLTSGL SRHHDEFVVA VVDEVLEEIR VGLELNEYGA QQKRLAHMRF LGELYNYEHV
     DSSVIFETLY LTLLYGHDTS EQEVLDPPED FFRVRMVIIL LETCGHYFDR GSSKKRLDQF
     LIHFQRYILS KGHLPLDIEF DLQDLFANLR PNMTRYSTID EVNAAILQLE EREHASSGDK
     VSIERHSDTK PSNKSSSDVI SSNGKSTAKD IRENGEAHGE ESDSDSGSGS VVRDGQNEEL
     DDGNHERGSE SGDGDDYDDG DGPGSDDDKF RVRQKVVTVD LEEQADFDQE LKALLQESME
     QRKLELRGRP ALNMTIPMSV FEGSGKDHHH FGRVVGENGE EVLDEENGEQ REVQVKVLVK
     RGNKQQTRQM LIPSDCALVQ STKQKEAAEL EEKQDIKRLV LEYNERDEEE ANGLGTQILN
     WTSGGSRGST RTGEGSGKSG GSRHRFYYHQ GGGGSYHARR K
 
 
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