RPN13_ARATH
ID RPN13_ARATH Reviewed; 300 AA.
AC O48726; Q94JW3;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=26S proteasome regulatory subunit RPN13;
DE Short=AtRPN13;
DE AltName: Full=26S proteasome non-ATPase regulatory subunit 13;
GN Name=RPN13; OrderedLocusNames=At2g26590; ORFNames=T9J22.26;
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;
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 [4]
RP INTERACTION WITH DSK2A, MUTAGENESIS OF LEU-47; PHE-67; GLU-70 AND PHE-88,
RP 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 [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).
RN [6]
RP FUNCTION, AND POLYUBIQUITIN BINDING.
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22751321; DOI=10.4161/psb.20360;
RA Lin Y.L., Fu H.;
RT "In vivo relevance of substrate recognition function of major Arabidopsis
RT ubiquitin receptors.";
RL Plant Signal. Behav. 7:722-727(2012).
CC -!- FUNCTION: Functions as a proteasomal ubiquitin receptor. Binds and
CC presumably selects ubiquitin-conjugates for destruction. Prefers
CC multiubiquitin chains rather than single ubiquitins, with a binding
CC affinity for 'Lys-63'-linked ubiquitin chains.
CC {ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:22751321}.
CC -!- SUBUNIT: Interacts with 'Lys-63'-linked polyubiquitin chains. Interacts
CC with DSK2a. {ECO:0000269|PubMed:20059542}.
CC -!- INTERACTION:
CC O48726; Q9SII8: DSK2B; NbExp=5; IntAct=EBI-7710745, EBI-4433040;
CC O48726; P48510: DSK2; Xeno; NbExp=4; IntAct=EBI-7710745, EBI-6174;
CC O48726; P0CG48: UBC; Xeno; NbExp=9; IntAct=EBI-7710745, EBI-3390054;
CC O48726; Q9UHD9: UBQLN2; Xeno; NbExp=4; IntAct=EBI-7710745, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01265}.
CC Nucleus {ECO:0000255|PROSITE-ProRule:PRU01265}.
CC -!- DOMAIN: The PH domain mediates interactions with ubiquitin and DSK2A.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22751321}.
CC -!- SIMILARITY: Belongs to the RPN13 family. {ECO:0000305}.
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DR EMBL; AC002505; AAC14506.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07862.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07863.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07864.1; -; Genomic_DNA.
DR EMBL; AF372873; AAK49589.1; -; mRNA.
DR EMBL; BT002671; AAO11587.1; -; mRNA.
DR PIR; T00992; T00992.
DR RefSeq; NP_001031424.1; NM_001036347.2.
DR RefSeq; NP_001031425.1; NM_001036348.2.
DR RefSeq; NP_565626.1; NM_128216.3.
DR AlphaFoldDB; O48726; -.
DR SMR; O48726; -.
DR BioGRID; 2552; 5.
DR IntAct; O48726; 4.
DR MINT; O48726; -.
DR STRING; 3702.AT2G26590.2; -.
DR PaxDb; O48726; -.
DR PRIDE; O48726; -.
DR ProteomicsDB; 228208; -.
DR EnsemblPlants; AT2G26590.1; AT2G26590.1; AT2G26590.
DR EnsemblPlants; AT2G26590.2; AT2G26590.2; AT2G26590.
DR EnsemblPlants; AT2G26590.3; AT2G26590.3; AT2G26590.
DR GeneID; 817200; -.
DR Gramene; AT2G26590.1; AT2G26590.1; AT2G26590.
DR Gramene; AT2G26590.2; AT2G26590.2; AT2G26590.
DR Gramene; AT2G26590.3; AT2G26590.3; AT2G26590.
DR KEGG; ath:AT2G26590; -.
DR Araport; AT2G26590; -.
DR TAIR; locus:2066200; AT2G26590.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_0_0_1; -.
DR InParanoid; O48726; -.
DR OrthoDB; 1479349at2759; -.
DR PhylomeDB; O48726; -.
DR PRO; PR:O48726; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48726; baseline and differential.
DR Genevisible; O48726; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; -; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; PTHR12225; 1.
DR Pfam; PF04683; Proteasom_Rpn13; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..300
FT /note="26S proteasome regulatory subunit RPN13"
FT /id="PRO_0000423175"
FT DOMAIN 9..121
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 13..120
FT /note="PH"
FT DOMAIN 192..295
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT MUTAGEN 47
FT /note="L->A: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin chains."
FT /evidence="ECO:0000269|PubMed:20059542"
FT MUTAGEN 67
FT /note="F->R: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin chains and interaction with DSK2A."
FT /evidence="ECO:0000269|PubMed:20059542"
FT MUTAGEN 70
FT /note="E->Q: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin chains and interaction with DSK2A."
FT /evidence="ECO:0000269|PubMed:20059542"
FT MUTAGEN 88
FT /note="F->R: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin chains and interaction with DSK2A."
FT /evidence="ECO:0000269|PubMed:20059542"
FT CONFLICT 265
FT /note="T -> I (in Ref. 3; AAK49589/AAO11587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33297 MW; CC5993E87FF331F5 CRC64;
MSSSEAFPVM QEIMLEFRAG KMSLQGTRVV PDARKGLVRI ARGDEGLIHF QWLDRNQNTV
EDDQIVFPDE ALFEKVNQSS DRVYILKFNS DDRKLFFWMQ EPRAEGDAEL CSSVNQYLNQ
PLEFPGEEGL AAAITEELED MAEDNTSSRA GNLVVPNLSS EVSDVTSSSG PVKLADLQRI
LNNLSGGPVG IAGDQDEGLA LGDILKPELI MPLLEALPVQ ERLSSHLPEG HSRAEDILEL
LQSPPFRQQV DAFTYVLRTG QIDLTQFGID PSKYKFTVDS FLEALEDSVS TQSRDAMDES
