PSD7B_ARATH
ID PSD7B_ARATH Reviewed; 310 AA.
AC Q9C774;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 7 homolog B;
DE AltName: Full=26S proteasome regulatory subunit RPN8b;
DE Short=AtRPN8b;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 34;
GN Name=RPN8B; Synonyms=MEE34; OrderedLocusNames=At3g11270; ORFNames=F11B9.19;
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, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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=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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C774-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR EMBL; AY258412; AAP83300.1; -; mRNA.
DR EMBL; AC073395; AAG50979.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75022.1; -; Genomic_DNA.
DR EMBL; AK228032; BAE99993.1; -; mRNA.
DR RefSeq; NP_187736.1; NM_111962.5. [Q9C774-1]
DR AlphaFoldDB; Q9C774; -.
DR SMR; Q9C774; -.
DR BioGRID; 5632; 91.
DR IntAct; Q9C774; 15.
DR STRING; 3702.AT3G11270.1; -.
DR MEROPS; M67.973; -.
DR iPTMnet; Q9C774; -.
DR PaxDb; Q9C774; -.
DR PRIDE; Q9C774; -.
DR DNASU; 820298; -.
DR EnsemblPlants; AT3G11270.1; AT3G11270.1; AT3G11270. [Q9C774-1]
DR GeneID; 820298; -.
DR Gramene; AT3G11270.1; AT3G11270.1; AT3G11270. [Q9C774-1]
DR KEGG; ath:AT3G11270; -.
DR Araport; AT3G11270; -.
DR TAIR; locus:2074653; AT3G11270.
DR eggNOG; KOG1556; Eukaryota.
DR HOGENOM; CLU_027018_3_0_1; -.
DR InParanoid; Q9C774; -.
DR OrthoDB; 1275837at2759; -.
DR PhylomeDB; Q9C774; -.
DR PRO; PR:Q9C774; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C774; baseline and differential.
DR Genevisible; Q9C774; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0005838; C:proteasome regulatory particle; IEA:InterPro.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP: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 GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR CDD; cd08062; MPN_RPN7_8; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033858; MPN_RPN7_8.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Proteasome; Reference proteome.
FT CHAIN 1..310
FT /note="26S proteasome non-ATPase regulatory subunit 7
FT homolog B"
FT /id="PRO_0000423178"
FT DOMAIN 17..154
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20516081"
SQ SEQUENCE 310 AA; 35085 MW; 122D45B6A9E2A7ED CRC64;
MDVIKTQQIS ARTIEKVIVH PLVLLSIVDH YNRVAKDTSK RVVGVLLGSS SRGTVDVTNS
YAVPFEEDDK DTSIWFLDHN YHESMFHMFK RINAKEHIVG WYSTGPKLRE NDLDVHALFN
GYVPNPVLVI IDVQPKELGI PTKAYYAVEE VKENATQKSQ QVFVHVPTEI AAHEVEEIGV
EHLLRDVKDT TISTLATEVT AKLTALKGLD ARLREIRTYL DLVIEGKLPL NHEILYHLQD
VFNLLPNLNV NELVKAFAVK TNDMMLVIYL SSLIRSVIAL HSLINNKLLN KEHEKAEDSK
PVDIPLITES
