RD23C_ARATH
ID RD23C_ARATH Reviewed; 419 AA.
AC Q84L31; Q9M887;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ubiquitin receptor RAD23c;
DE Short=AtRAD23c;
DE AltName: Full=Putative DNA repair protein RAD23-3;
DE AltName: Full=RAD23-like protein 3;
DE Short=AtRAD23-3;
GN Name=RAD23C; Synonyms=RAD23, RAD23-3; OrderedLocusNames=At3g02540;
GN ORFNames=F16B3.17;
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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia; 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
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 [5]
RP FUNCTION, INTERACTION WITH RPN10, AND POLYUBIQUITIN BINDING.
RX PubMed=20059542; DOI=10.1111/j.1742-4658.2009.07531.x;
RA Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T.,
RA Tsai H.L., Lee Y., Fu H.;
RT "Cross-species divergence of the major recognition pathways of
RT ubiquitylated substrates for ubiquitin/26S proteasome-mediated
RT proteolysis.";
RL FEBS J. 277:796-816(2010).
RN [6]
RP GENE FAMILY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POLYUBIQUITIN
RP BINDING, AND DISRUPTION PHENOTYPE.
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 [7]
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).
RN [8]
RP FUNCTION, POLYUBIQUITIN BINDING, INTERACTION WITH RPN10, AND MUTAGENESIS OF
RP LEU-8 AND ILE-47.
RX PubMed=21764993; DOI=10.1105/tpc.111.086702;
RA Lin Y.-L., Sung S.-C., Tsai H.-L., Yu T.-T., Radjacommare R., Usharani R.,
RA Fatimababy A.S., Lin H.-Y., Wang Y.-Y., Fu H.;
RT "The defective proteasome but not substrate recognition function is
RT responsible for the null phenotypes of the Arabidopsis proteasome subunit
RT RPN10.";
RL Plant Cell 23:2754-2773(2011).
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). {ECO:0000250, ECO:0000269|PubMed:20059542,
CC ECO:0000269|PubMed:21764993}.
CC -!- SUBUNIT: Interacts with 'Lys-48'-linked polyubiquitin chains via its
CC both UBA domains. Interacts with RPN10 via its ubiquitin-like domain.
CC {ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993}.
CC -!- INTERACTION:
CC Q84L31; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-4437395, EBI-3390054;
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; Synonyms=alpha;
CC IsoId=Q84L31-1; Sequence=Displayed;
CC Name=2; Synonyms=beta;
CC IsoId=Q84L31-2; Sequence=VSP_011876;
CC -!- TISSUE SPECIFICITY: Widely expressed in the whole plant.
CC {ECO:0000269|PubMed:20086187}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:20086187}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
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DR EMBL; AB109196; BAC76392.1; -; mRNA.
DR EMBL; AB109197; BAC76393.1; -; mRNA.
DR EMBL; AC021640; AAF32461.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73824.1; -; Genomic_DNA.
DR EMBL; AY039562; AAK62617.1; -; mRNA.
DR EMBL; AY113034; AAM47342.1; -; mRNA.
DR RefSeq; NP_186903.1; NM_111121.4. [Q84L31-1]
DR AlphaFoldDB; Q84L31; -.
DR SMR; Q84L31; -.
DR BioGRID; 6528; 5.
DR DIP; DIP-57199N; -.
DR IntAct; Q84L31; 6.
DR MINT; Q84L31; -.
DR STRING; 3702.AT3G02540.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q84L31; -.
DR PaxDb; Q84L31; -.
DR ProteomicsDB; 236955; -. [Q84L31-1]
DR EnsemblPlants; AT3G02540.1; AT3G02540.1; AT3G02540. [Q84L31-1]
DR GeneID; 821195; -.
DR Gramene; AT3G02540.1; AT3G02540.1; AT3G02540. [Q84L31-1]
DR KEGG; ath:AT3G02540; -.
DR Araport; AT3G02540; -.
DR TAIR; locus:2076944; AT3G02540.
DR eggNOG; KOG0011; Eukaryota.
DR HOGENOM; CLU_040364_0_0_1; -.
DR InParanoid; Q84L31; -.
DR OMA; HEFENDQ; -.
DR OrthoDB; 1260050at2759; -.
DR PhylomeDB; Q84L31; -.
DR PRO; PR:Q84L31; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84L31; baseline and differential.
DR Genevisible; Q84L31; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..419
FT /note="Ubiquitin receptor RAD23c"
FT /id="PRO_0000114910"
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 185..228
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 288..331
FT /note="STI1"
FT DOMAIN 372..413
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 83..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 58..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011876"
FT MUTAGEN 8
FT /note="L->A: Abolishes interaction with RPN10."
FT /evidence="ECO:0000269|PubMed:21764993"
FT MUTAGEN 47
FT /note="I->A: Abolishes interaction with RPN10."
FT /evidence="ECO:0000269|PubMed:21764993"
SQ SEQUENCE 419 AA; 44247 MW; CAA13BC4FFEB1E25 CRC64;
MKIFVKTLKG THFEIEVKPE DSVVDVKKNI ESVQGADVYP AAKQMLIHQG KVLKDETTIE
ENKVAENSFI VIMMNKSKPA SAAASSASAG TSQAKSIPPS TSQPSISPQT PASVSAPVAP
APTRPPPPAP TPTPAPVAAT ETVTTPIPEP VPATISSSTP APDSAPVGSQ GDVYGQAASN
LAAGSNLEST IQQILDMGGG TWDRETVVLA LRAAFNNPER AVEYLYTGIP EQAEVPPVAR
PPASAGQPAN PPAQTQQPAA APASGPNANP LDLFPQGLPN VGGNPGAGTL DFLRNSQQFQ
ALRAMVQANP QVLQPMLQEL GKQNPNLMRL IQDHQADFLR LINEPVEGGG ESGNLLGQMA
AGMPQPQAIQ VTHEEREAIE RLEAMGFERA LVLEVFFACN KNEELAANYL LDHMHEFEE
