RD23A_ARATH
ID RD23A_ARATH Reviewed; 368 AA.
AC Q84L32; Q9S9L8; Q9SA20;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Probable ubiquitin receptor RAD23a;
DE Short=AtRAD23a;
DE AltName: Full=Putative DNA repair protein RAD23-2;
DE AltName: Full=RAD23-like protein 2;
DE Short=AtRAD23-2;
GN Name=RAD23A; Synonyms=RAD23, RAD23-2; OrderedLocusNames=At1g16190;
GN ORFNames=F3O9.1;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Flower bud;
RA Ishikawa Y., Endo M., Abe K., Osakabe K., Nakajima N., Saji H., Ito Y.,
RA Ichikawa H., Kameya T., Toki S.;
RT "Isolation of four RAD23 genes from Arabidopsis thaliana and detection of
RT alternative splicing variants.";
RL Submitted (APR-2003) 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 GENE FAMILY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20086187; DOI=10.1105/tpc.109.072660;
RA Farmer L.M., Book A.J., Lee K.H., Lin Y.L., Fu H., Vierstra R.D.;
RT "The RAD23 family provides an essential connection between the 26S
RT proteasome and ubiquitylated proteins in Arabidopsis.";
RL Plant Cell 22:124-142(2010).
RN [5]
RP REVIEW.
RX PubMed=20399133; DOI=10.1016/j.tplants.2010.03.004;
RA Fu H., Lin Y.L., Fatimababy A.S.;
RT "Proteasomal recognition of ubiquitylated substrates.";
RL Trends Plant Sci. 15:375-386(2010).
CC -!- FUNCTION: May be involved in nucleotide excision repair (By
CC similarity). Binds and presumably selects ubiquitin-conjugates for
CC destruction. Prefers multiubiquitin chains rather than single
CC ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin
CC chains. Acts as a ubiquitin receptor that associates with the 26S
CC proteasomal docking subunit RPN10 for the indirect recognition of
CC ubiquitinated substrates of ubiquitin/26S proteasome-mediated
CC proteolysis (UPP) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with 'Lys-48'-linked polyubiquitin chains. Interacts
CC with RPN10. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20086187}. Cytoplasm
CC {ECO:0000269|PubMed:20086187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84L32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84L32-2; Sequence=VSP_014979;
CC -!- TISSUE SPECIFICITY: Widely expressed in the whole plant.
CC {ECO:0000269|PubMed:20086187}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF18513.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB109195; BAC76391.1; -; mRNA.
DR EMBL; AC006341; AAD34676.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010924; AAF18513.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29418.1; -; Genomic_DNA.
DR PIR; G86296; G86296.
DR PIR; H86296; H86296.
DR RefSeq; NP_173070.1; NM_101486.3. [Q84L32-1]
DR AlphaFoldDB; Q84L32; -.
DR SMR; Q84L32; -.
DR IntAct; Q84L32; 5.
DR MINT; Q84L32; -.
DR STRING; 3702.AT1G16190.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q84L32; -.
DR PRIDE; Q84L32; -.
DR ProteomicsDB; 236540; -. [Q84L32-1]
DR EnsemblPlants; AT1G16190.1; AT1G16190.1; AT1G16190. [Q84L32-1]
DR GeneID; 838188; -.
DR Gramene; AT1G16190.1; AT1G16190.1; AT1G16190. [Q84L32-1]
DR KEGG; ath:AT1G16190; -.
DR Araport; AT1G16190; -.
DR TAIR; locus:2200522; AT1G16190.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_1_0_1; -.
DR InParanoid; Q84L32; -.
DR PhylomeDB; Q84L32; -.
DR PRO; PR:Q84L32; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84L32; baseline and differential.
DR Genevisible; Q84L32; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.540; -; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR TIGRFAMs; TIGR00601; rad23; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..368
FT /note="Probable ubiquitin receptor RAD23a"
FT /id="PRO_0000114909"
FT DOMAIN 1..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 142..185
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 239..282
FT /note="STI1"
FT DOMAIN 320..360
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 80..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 20..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014979"
SQ SEQUENCE 368 AA; 39842 MW; BFBF4FE75E6C431F CRC64;
MKLTVKTLKG SHFEIRVLPT DTIMAVKKNI EDSQSKDNYP CGQQLLIHNG KVLKDETTLV
ENKVTEEGFL VVMLSKSKTA SSAGPSSTQP TSTTTSTISS TTLAAPSTTQ SIAVPASNST
PVQEQPTAQS DTYGQAASTL VSGSSIEQMV QQIMEMGGGS WDKETVTRAL RAAYNNPERA
VDYLYSGIPE TVTIPATNLS GVGSGRELTA PPPSGGPNSS PLDLFPQEAV SDAAGGDLGT
LEFLRGNDQF QQLRSMVNSN PQILQPMLQE LGKQNPQLLR LIQENQAEFL QLLNEPYEGS
DGDVDIFDQP DQEMPHSVNV TPEEQESIER LEAMGFDRAI VIEAFLSCDR NEELAANYLL
EHSADFED
