PSD11_ARATH
ID PSD11_ARATH Reviewed; 419 AA.
AC Q9LP45; O81694; Q6XJG1; Q6XJG4;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11 homolog;
DE AltName: Full=19S proteosome subunit 9;
DE Short=AtS9;
DE AltName: Full=26S proteasome regulatory subunit RPN6;
DE Short=AtRPN6;
DE AltName: Full=26S proteasome regulatory subunit S9 homolog;
GN Name=RPN6; Synonyms=ATS9, RPN6A; OrderedLocusNames=At1g29150;
GN ORFNames=F28N24.15;
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], AND INTERACTION WITH CSN1.
RC STRAIN=cv. Columbia;
RX PubMed=9878390; DOI=10.1006/jmbi.1998.2315;
RA Kwok S.F., Staub J.M., Deng X.-W.;
RT "Characterization of two subunits of Arabidopsis 19S proteasome regulatory
RT complex and its possible interaction with the COP9 complex.";
RL J. Mol. Biol. 285:85-95(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=14623884; DOI=10.1074/jbc.m311977200;
RA Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
RT "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
RT analyses revealed the presence of multiple isoforms.";
RL J. Biol. Chem. 279:6401-6413(2004).
RN [3]
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 [4]
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 [5]
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 [6]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
RX PubMed=11179422; DOI=10.1091/mbc.12.2.383;
RA Peng Z., Staub J.M., Serino G., Kwok S.F., Kurepa J., Bruce B.D.,
RA Vierstra R.D., Wei N., Deng X.W.;
RT "The cellular level of PR500, a protein complex related to the 19S
RT regulatory particle of the proteasome, is regulated in response to stresses
RT in plants.";
RL Mol. Biol. Cell 12:383-392(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND UBIQUITINATION AT LYS-160.
RX PubMed=20516081; DOI=10.1074/jbc.m110.136622;
RA Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
RT array of plant proteolytic complexes.";
RL J. Biol. Chem. 285:25554-25569(2010).
CC -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, RPN6A is required for
CC proteasome assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) lid
CC subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC core protease (CP), known as the 20S proteasome, capped at one or both
CC ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
CC composed of at least 17 different subunits in two subcomplexes, the
CC base and the lid, which form the portions proximal and distal to the
CC 20S proteolytic core, respectively. Interacts with CSN1.
CC {ECO:0000269|PubMed:11179422, ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081, ECO:0000269|PubMed:9878390}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34120.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF083890; AAC34120.1; ALT_SEQ; mRNA.
DR EMBL; AY230834; AAP86661.1; -; mRNA.
DR EMBL; AY230835; AAP86662.1; -; mRNA.
DR EMBL; AY230836; AAP86663.1; -; mRNA.
DR EMBL; AY230837; AAP86664.1; -; mRNA.
DR EMBL; AC021043; AAF88122.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31050.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61082.1; -; Genomic_DNA.
DR EMBL; AF370203; AAK44018.1; -; mRNA.
DR EMBL; AY056311; AAL07160.1; -; mRNA.
DR PIR; A86414; A86414.
DR PIR; T52033; T52033.
DR RefSeq; NP_001323322.1; NM_001332840.1.
DR RefSeq; NP_174210.1; NM_102656.4.
DR AlphaFoldDB; Q9LP45; -.
DR SMR; Q9LP45; -.
DR BioGRID; 25024; 90.
DR IntAct; Q9LP45; 2.
DR STRING; 3702.AT1G29150.1; -.
DR iPTMnet; Q9LP45; -.
DR MetOSite; Q9LP45; -.
DR PaxDb; Q9LP45; -.
DR PRIDE; Q9LP45; -.
DR ProMEX; Q9LP45; -.
DR ProteomicsDB; 226233; -.
DR EnsemblPlants; AT1G29150.1; AT1G29150.1; AT1G29150.
DR EnsemblPlants; AT1G29150.2; AT1G29150.2; AT1G29150.
DR GeneID; 839789; -.
DR Gramene; AT1G29150.1; AT1G29150.1; AT1G29150.
DR Gramene; AT1G29150.2; AT1G29150.2; AT1G29150.
DR KEGG; ath:AT1G29150; -.
DR Araport; AT1G29150; -.
DR TAIR; locus:2030017; AT1G29150.
DR eggNOG; KOG1463; Eukaryota.
DR HOGENOM; CLU_029573_2_1_1; -.
DR InParanoid; Q9LP45; -.
DR OMA; LYFDTGM; -.
DR OrthoDB; 1052430at2759; -.
DR PhylomeDB; Q9LP45; -.
DR PRO; PR:Q9LP45; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LP45; baseline and differential.
DR Genevisible; Q9LP45; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..419
FT /note="26S proteasome non-ATPase regulatory subunit 11
FT homolog"
FT /id="PRO_0000419983"
FT DOMAIN 217..388
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CONFLICT 55
FT /note="T -> I (in Ref. 2; AAP86661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46749 MW; 6446C06D702FD9BF CRC64;
MVSYRATTET ISLALEANSS EAITILYQVL EDPSSSPEAI RIKEQAITNL CDRLTEEKRG
EDLRKLLTKL RPFFSLIPKA KTAKIVRGII DAVAKIPGTT DLQITLCKEM VEWTRAEKRT
FLRQRVEARL AALLMENKEY VEALALLSTL VKEVRRLDDK LLLVDIDLLE SKLHFSLRNL
PKAKAALTAA RTAANAIYVP PAQQGTIDLQ SGILHAEEKD YKTGYSYFFE AFESFNALGD
PRAVFSLKYM LLCKIMVSQA DDVAGIISSK AGLQYVGPDL DAMKAVADAH SKRSLKLFEN
ALRDYKAQLE DDPIVHRHLS SLYDTLLEQN LCRLIEPFSR VEIAHIAELI GLPLDHVEKK
LSQMILDKKF AGTLDQGAGC LIIFEDPKAD AIYSATLETI ANMGKVVDSL YVRSAKIMS
