RD23B_ARATH
ID RD23B_ARATH Reviewed; 371 AA.
AC Q84L33; Q84L34; Q8LA46; Q94CE9; Q9MA10;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Ubiquitin receptor RAD23b;
DE Short=AtRAD23b;
DE AltName: Full=Putative DNA repair protein RAD23-1;
DE AltName: Full=RAD23-like protein 1;
DE Short=AtRAD23-1;
GN Name=RAD23B; Synonyms=RAD23, RAD23-1; OrderedLocusNames=At1g79650;
GN ORFNames=F20B17.8;
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=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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, AND INTERACTION WITH RPN10.
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 [7]
RP GENE FAMILY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH UBQ
RP AND IAA16, POLYUBIQUITIN BINDING, INTERACTION WITH RPN10, DISRUPTION
RP PHENOTYPE, AND FUNCTION.
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 [8]
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 [9]
RP INTERACTION WITH RPN10, AND MUTAGENESIS OF 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:20086187}.
CC -!- SUBUNIT: Interacts with 'Lys-48'-linked polyubiquitin chains. Interacts
CC with RPN10 via its ubiquitin-like domain. Interacts with UBQ1, UBQ2,
CC UBQ5, UBQ7, UBQ10, UBQ11 and IAA16. {ECO:0000269|PubMed:20059542,
CC ECO:0000269|PubMed:20086187, ECO:0000269|PubMed:21764993}.
CC -!- INTERACTION:
CC Q84L33; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-20557876, EBI-15193683;
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, RAD23bi;
CC IsoId=Q84L33-1; Sequence=Displayed;
CC Name=2; Synonyms=beta, RAD23bii;
CC IsoId=Q84L33-2; Sequence=VSP_011875;
CC -!- TISSUE SPECIFICITY: Widely expressed in the whole plant.
CC {ECO:0000269|PubMed:20086187}.
CC -!- DISRUPTION PHENOTYPE: Slow growth with abnormal phyllotaxy, shorter
CC primary root with fewer lateral roots, shorter inflorescences, smaller
CC siliques and reduced seed set, with unfertilized ovules interspersed
CC among seeds of normal appearance. Mutant displays resistance to
CC mitomycin C (MMC). {ECO:0000269|PubMed:20086187}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB109193; BAC76389.1; -; mRNA.
DR EMBL; AB109194; BAC76390.1; -; mRNA.
DR EMBL; AC010793; AAF68123.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36279.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36281.1; -; Genomic_DNA.
DR EMBL; AY034912; AAK59419.1; -; mRNA.
DR EMBL; AY063103; AAL34277.1; -; mRNA.
DR EMBL; AY088037; AAM65583.1; -; mRNA.
DR PIR; F96827; F96827.
DR RefSeq; NP_565216.2; NM_106614.6. [Q84L33-2]
DR RefSeq; NP_850982.1; NM_180651.3. [Q84L33-1]
DR AlphaFoldDB; Q84L33; -.
DR SMR; Q84L33; -.
DR BioGRID; 29522; 6.
DR IntAct; Q84L33; 2.
DR MINT; Q84L33; -.
DR STRING; 3702.AT1G79650.4; -.
DR PRIDE; Q84L33; -.
DR ProteomicsDB; 236223; -. [Q84L33-1]
DR EnsemblPlants; AT1G79650.1; AT1G79650.1; AT1G79650. [Q84L33-1]
DR EnsemblPlants; AT1G79650.2; AT1G79650.2; AT1G79650. [Q84L33-2]
DR GeneID; 844304; -.
DR Gramene; AT1G79650.1; AT1G79650.1; AT1G79650. [Q84L33-1]
DR Gramene; AT1G79650.2; AT1G79650.2; AT1G79650. [Q84L33-2]
DR KEGG; ath:AT1G79650; -.
DR Araport; AT1G79650; -.
DR eggNOG; KOG0011; Eukaryota.
DR InParanoid; Q84L33; -.
DR OMA; EGEMFEQ; -.
DR PhylomeDB; Q84L33; -.
DR PRO; PR:Q84L33; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84L33; baseline and differential.
DR Genevisible; Q84L33; 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:UniProtKB.
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:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
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..371
FT /note="Ubiquitin receptor RAD23b"
FT /id="PRO_0000114908"
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 146..189
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 242..285
FT /note="STI1"
FT DOMAIN 325..365
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 79..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 89..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1"
FT /id="VSP_011875"
FT MUTAGEN 47
FT /note="I->A: Abolishes interaction with RPN10."
FT /evidence="ECO:0000269|PubMed:21764993"
FT CONFLICT 253..254
FT /note="FQ -> LE (in Ref. 1; BAC76389/BAC76390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 39747 MW; 081493086EA976E7 CRC64;
MKLTVKTLKG SHFEIRVLPS DTIMAVKKNI EDSQGKDNYP CGQQLLIHNG KVLKDETSLV
ENKVTEEGFL VVMLSKSKSG GSAGQASVQT SSVSQPVSAT TSSTKPAAPS TTQSSPVPAS
PIPAQEQPAA QTDTYGQAAS TLVSGSSLEQ MVQQIMEMGG GSWDKETVTR ALRAAYNNPE
RAVDYLYSGI PQTAEVAVPV PEAQIAGSGA APVAPASGGP NSSPLDLFPQ ETVAAAGSGD
LGTLEFLRNN DQFQQLRTMV HSNPQILQPM LQELGKQNPQ LLRLIQENQA EFLQLVNEPY
EGSDGEGDMF DQPEQEMPHA INVTPAEQEA IQRLEAMGFD RALVIEAFLA CDRNEELAAN
YLLENSGDFE D
