PSMD6_ARATH
ID PSMD6_ARATH Reviewed; 387 AA.
AC Q93Y35; Q6EMB5; Q9SZX2;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 6 homolog;
DE AltName: Full=26S proteasome regulatory subunit RPN7;
DE Short=AtRPN7;
DE AltName: Full=26S proteasome regulatory subunit S10 homolog;
GN Name=RPN7; OrderedLocusNames=At4g24820; ORFNames=F6I7.30;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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].
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 IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND ACETYLATION AT MET-1.
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {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. {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41122.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79392.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY230838; AAP86665.1; -; mRNA.
DR EMBL; AL049657; CAB41122.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84966.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84967.1; -; Genomic_DNA.
DR EMBL; AY054500; AAK96691.1; -; mRNA.
DR EMBL; AY093269; AAM13268.1; -; mRNA.
DR EMBL; BT000653; AAN31800.1; -; mRNA.
DR EMBL; AY087847; AAM65400.1; -; mRNA.
DR PIR; T06666; T06666.
DR RefSeq; NP_567709.1; NM_118615.3.
DR RefSeq; NP_974611.1; NM_202882.1.
DR AlphaFoldDB; Q93Y35; -.
DR SMR; Q93Y35; -.
DR BioGRID; 13874; 95.
DR IntAct; Q93Y35; 18.
DR STRING; 3702.AT4G24820.1; -.
DR iPTMnet; Q93Y35; -.
DR PaxDb; Q93Y35; -.
DR PRIDE; Q93Y35; -.
DR ProteomicsDB; 226234; -.
DR DNASU; 828585; -.
DR EnsemblPlants; AT4G24820.1; AT4G24820.1; AT4G24820.
DR EnsemblPlants; AT4G24820.2; AT4G24820.2; AT4G24820.
DR GeneID; 828585; -.
DR Gramene; AT4G24820.1; AT4G24820.1; AT4G24820.
DR Gramene; AT4G24820.2; AT4G24820.2; AT4G24820.
DR KEGG; ath:AT4G24820; -.
DR Araport; AT4G24820; -.
DR TAIR; locus:2126798; AT4G24820.
DR eggNOG; KOG0687; Eukaryota.
DR HOGENOM; CLU_031814_0_0_1; -.
DR InParanoid; Q93Y35; -.
DR OMA; SLYNCHY; -.
DR OrthoDB; 1194691at2759; -.
DR PhylomeDB; Q93Y35; -.
DR PRO; PR:Q93Y35; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93Y35; baseline and differential.
DR Genevisible; Q93Y35; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Proteasome; Reference proteome.
FT CHAIN 1..387
FT /note="26S proteasome non-ATPase regulatory subunit 6
FT homolog"
FT /id="PRO_0000173842"
FT DOMAIN 191..359
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT COILED 65..101
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20516081,
FT ECO:0007744|PubMed:22223895"
SQ SEQUENCE 387 AA; 44282 MW; EFDD1AD4A59CC6C3 CRC64;
MDGGAEGSQQ PHLILANKLF LLTHPDVPDI EKVQLKSEVL DFIRSHGMAP LYETLIASSV
LDLDQSLLES MRAANEEELK KLDEKIADAE ENLGESEVRE AHLAKALYFI RISDKEKALE
QLKLTEGKTV AVGQKMDVVF YTLQLAFFYM DFDLVSKSID KAKKLFEEGG DWERKNRLKV
YEGLYCMSTR NFKKAASLFL DSISTFTTYE IFPYETFIFY TVLTSIITLD RVSLKQKVVD
APEILTVLGK IPFLSEFLNS LYECQYKAFF SAFAGMAVQI KYDRYLYPHF RFYMREVRTV
VYSQFLESYK SVTVEAMAKA FGVSVDFIDQ ELSRFIAAGK LHCKIDKVAG VLETNRPDAK
NALYQATIKQ GDFLLNRIQK LSRVIDL
