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RAE1_ARATH
ID   RAE1_ARATH              Reviewed;         349 AA.
AC   Q38942; Q1LYY5; Q9SAJ0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 151.
DE   RecName: Full=Protein RAE1 {ECO:0000303|PubMed:21189294};
DE   AltName: Full=RNA export factor 1 {ECO:0000303|PubMed:21189294};
GN   Name=RAE1 {ECO:0000303|PubMed:21189294};
GN   OrderedLocusNames=At1g80670 {ECO:0000312|Araport:AT1G80670};
GN   ORFNames=F23A5.2 {ECO:0000312|EMBL:AAF14655.1};
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 [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Goodman H.M., Gallant P., Keifer-Higgins S., Rubenfield M., Church G.M.;
RT   "A 37.5 Kb sequence from Arabidopsis thaliana chromosome I.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   DWD MOTIF, AND INTERACTION WITH DDB1A.
RX   PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA   Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA   He Y.J., Xiong Y., Deng X.W.;
RT   "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT   substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL   Plant Cell 20:152-167(2008).
RN   [7]
RP   IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA   Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT   "Identification and characterization of nuclear pore complex components in
RT   Arabidopsis thaliana.";
RL   Plant Cell 22:4084-4097(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC       fold symmetrical structure comprising a central transport channel and
CC       two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC       are attached. The cytoplasmic filaments have loose ends, while the
CC       nuclear filaments are joined in a distal ring, forming a nuclear
CC       basket. NPCs are highly dynamic in configuration and composition, and
CC       can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC       subcomplex and the NUP93 subcomplex, containing approximately 30
CC       different nucleoporin proteins. Interacts with DDB1A.
CC       {ECO:0000305|PubMed:21189294}.
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21189294}.
CC       Nucleus, nuclear pore complex {ECO:0000269|PubMed:21189294}.
CC   -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC       {ECO:0000250|UniProtKB:Q42384}.
CC   -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA98915.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF14654.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U53501; AAA98915.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011713; AAF14654.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011713; AAF14655.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36435.1; -; Genomic_DNA.
DR   EMBL; BT025241; ABF18994.1; -; mRNA.
DR   EMBL; AY087683; AAM65220.1; -; mRNA.
DR   PIR; A96839; A96839.
DR   PIR; S71241; S71241.
DR   RefSeq; NP_178182.1; NM_106715.5.
DR   AlphaFoldDB; Q38942; -.
DR   SMR; Q38942; -.
DR   BioGRID; 29624; 192.
DR   IntAct; Q38942; 1.
DR   STRING; 3702.AT1G80670.1; -.
DR   iPTMnet; Q38942; -.
DR   PaxDb; Q38942; -.
DR   PRIDE; Q38942; -.
DR   ProteomicsDB; 236561; -.
DR   EnsemblPlants; AT1G80670.1; AT1G80670.1; AT1G80670.
DR   GeneID; 844406; -.
DR   Gramene; AT1G80670.1; AT1G80670.1; AT1G80670.
DR   KEGG; ath:AT1G80670; -.
DR   Araport; AT1G80670; -.
DR   TAIR; locus:2025732; AT1G80670.
DR   eggNOG; KOG0647; Eukaryota.
DR   HOGENOM; CLU_038526_1_0_1; -.
DR   InParanoid; Q38942; -.
DR   OMA; EAMDQSI; -.
DR   OrthoDB; 1048963at2759; -.
DR   PhylomeDB; Q38942; -.
DR   PRO; PR:Q38942; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q38942; baseline and differential.
DR   Genevisible; Q38942; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR   GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA transport; Nuclear pore complex; Nucleus;
KW   Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW   WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..349
FT                   /note="Protein RAE1"
FT                   /id="PRO_0000051180"
FT   REPEAT          23..62
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          70..109
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          112..151
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          153..190
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          244..283
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           128..144
FT                   /note="DWD box"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   349 AA;  38268 MW;  F1780EF3258C5632 CRC64;
     MATFGAPATA NSNPNKSYEV TPSPADSISS LSFSPRADIL VATSWDNQVR CWEISRSGAS
     LASAPKASIS HDQPVLCSAW KDDGTTVFSG GCDKQAKMWP LLSGGQPVTV AMHEGPIAAM
     AWIPGMNLLA TGSWDKTLKY WDTRQQNPVH TQQLPDKCYT LSVKHPLMVV GTADRNLIVF
     NLQNPQTEFK RIQSPLKYQT RCVTAFPDQQ GFLVGSIEGR VGVHHLDDSQ QSKNFTFKCH
     RDGNDIYSVN SLNFHPVHGT FATAGSDGAF NFWDKDSKQR LKAMSRCNQP IPCSSFNHDG
     SIYAYAACYD WSKGAENHNP ATAKSSIFLH LPQESEVKAK PRVGATGRK
 
 
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