PS12B_ARATH
ID PS12B_ARATH Reviewed; 442 AA.
AC Q8VWK0; Q9FGF7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 12 homolog B;
DE AltName: Full=26S proteasome regulatory subunit RPN5b;
DE Short=AtRPN5b;
DE AltName: Full=26S proteasome regulatory subunit p55 homolog B;
GN Name=RPN5B; OrderedLocusNames=At5g64760; ORFNames=MVP7.9;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19252082; DOI=10.1105/tpc.108.064444;
RA Book A.J., Smalle J., Lee K.H., Yang P., Walker J.M., Casper S.,
RA Holmes J.H., Russo L.A., Buzzinotti Z.W., Jenik P.D., Vierstra R.D.;
RT "The RPN5 subunit of the 26s proteasome is essential for gametogenesis,
RT sporophyte development, and complex assembly in Arabidopsis.";
RL Plant Cell 21:460-478(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, AND SUBUNIT.
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 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins (By
CC similarity). Acts redundantly with RPN5A. {ECO:0000250,
CC ECO:0000269|PubMed:19252082}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19252082}. Nucleus
CC {ECO:0000269|PubMed:19252082}.
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=Q8VWK0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19252082}.
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10309.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY230833; AAP86660.1; -; mRNA.
DR EMBL; AB025637; BAB10309.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97947.1; -; Genomic_DNA.
DR EMBL; AY062093; AAL32972.1; -; mRNA.
DR EMBL; AY062113; AAL32985.1; -; mRNA.
DR EMBL; AY124872; AAM70581.1; -; mRNA.
DR RefSeq; NP_568994.2; NM_125872.4. [Q8VWK0-1]
DR AlphaFoldDB; Q8VWK0; -.
DR SMR; Q8VWK0; -.
DR BioGRID; 21839; 103.
DR IntAct; Q8VWK0; 1.
DR STRING; 3702.AT5G64760.1; -.
DR PaxDb; Q8VWK0; -.
DR PRIDE; Q8VWK0; -.
DR ProteomicsDB; 226300; -. [Q8VWK0-1]
DR EnsemblPlants; AT5G64760.1; AT5G64760.1; AT5G64760. [Q8VWK0-1]
DR GeneID; 836597; -.
DR Gramene; AT5G64760.1; AT5G64760.1; AT5G64760. [Q8VWK0-1]
DR KEGG; ath:AT5G64760; -.
DR Araport; AT5G64760; -.
DR TAIR; locus:2176100; AT5G64760.
DR eggNOG; KOG1498; Eukaryota.
DR HOGENOM; CLU_033860_1_0_1; -.
DR OrthoDB; 937686at2759; -.
DR PRO; PR:Q8VWK0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VWK0; baseline and differential.
DR Genevisible; Q8VWK0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA: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:0030163; P:protein catabolic process; TAS:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR040896; RPN5_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18098; RPN5_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..442
FT /note="26S proteasome non-ATPase regulatory subunit 12
FT homolog B"
FT /id="PRO_0000423172"
FT DOMAIN 232..403
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT COILED 1..129
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 51118 MW; 4ED16CA4F843FBA0 CRC64;
MEESRQLESS IDRLLNEEKQ MRLAENVAGT RKAATEILKL CFEAKDWKLL NEQILNLSKK
RGQLKQAVQS MVQQAMQYID QTLDIETRIE LIKTLNNVAA GKIYVEIERA RLTKMLAKIK
EEQGLIAEAA DLMQEVAVET FGAMAKTEKI AFILEQVRLC LDQKDFVRAQ ILSRKINPRV
FDADTTKEKK KPKEGENMVE EAPADIPTLL VLKRIYYELM IRYYSHNNEY IEICRSYKAI
YDIPSVKENP EQWIPVLRKI CWFLALAPHD PMQSSLLNAT LEDKKLSEIP DFKMLLKQIV
TMEVIQWTSL WNKYKDEFEN EKNMIGGSLG DKAGEDLKLR IIEHNILVVS KYYSRITFKR
LAELLCLTTE EAEKHLSEMV VSKALIAKID RPSGIICFQI VKDSNEILNS WATNLEKLLD
LVEKSCHQIH KETMVHKVAL RA
