PSD1A_ARATH
ID PSD1A_ARATH Reviewed; 1004 AA.
AC O48844; Q570D7; Q6XJG7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1 homolog A;
DE AltName: Full=26S proteasome regulatory subunit RPN2a;
DE Short=AtRPN2a;
DE AltName: Full=26S proteasome regulatory subunit S1 homolog A;
GN Name=RPN2A; OrderedLocusNames=At2g32730; ORFNames=F24L7.13;
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=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 [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] OF 740-1004.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-896, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-896, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-896, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND UBIQUITINATION AT LYS-166.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 26 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) base
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 S1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY230830; AAP86657.1; -; mRNA.
DR EMBL; AC003974; AAC04490.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08730.1; -; Genomic_DNA.
DR EMBL; AY099861; AAM20712.1; -; mRNA.
DR EMBL; AK220772; BAD93983.1; -; mRNA.
DR PIR; T00795; T00795.
DR RefSeq; NP_180832.1; NM_128832.5.
DR AlphaFoldDB; O48844; -.
DR SMR; O48844; -.
DR BioGRID; 3180; 101.
DR IntAct; O48844; 3.
DR STRING; 3702.AT2G32730.1; -.
DR iPTMnet; O48844; -.
DR MetOSite; O48844; -.
DR PaxDb; O48844; -.
DR PRIDE; O48844; -.
DR ProMEX; O48844; -.
DR ProteomicsDB; 226432; -.
DR EnsemblPlants; AT2G32730.1; AT2G32730.1; AT2G32730.
DR GeneID; 817833; -.
DR Gramene; AT2G32730.1; AT2G32730.1; AT2G32730.
DR KEGG; ath:AT2G32730; -.
DR Araport; AT2G32730; -.
DR TAIR; locus:2046402; AT2G32730.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; O48844; -.
DR OMA; MIMVQQN; -.
DR OrthoDB; 235012at2759; -.
DR PhylomeDB; O48844; -.
DR PRO; PR:O48844; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48844; baseline and differential.
DR Genevisible; O48844; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR040623; RPN2_C.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1004
FT /note="26S proteasome non-ATPase regulatory subunit 1
FT homolog A"
FT /id="PRO_0000423176"
FT REPEAT 412..447
FT /note="PC 1"
FT REPEAT 452..485
FT /note="PC 2"
FT REPEAT 487..521
FT /note="PC 3"
FT REPEAT 522..555
FT /note="PC 4"
FT REPEAT 557..590
FT /note="PC 5"
FT REPEAT 591..626
FT /note="PC 6"
FT REPEAT 627..659
FT /note="PC 7"
FT REPEAT 661..695
FT /note="PC 8"
FT REPEAT 696..736
FT /note="PC 9"
FT REPEAT 739..771
FT /note="PC 10"
FT REGION 858..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CONFLICT 45
FT /note="S -> G (in Ref. 1; AAP86657)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="I -> L (in Ref. 5; BAD93983)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="N -> S (in Ref. 5; BAD93983)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="T -> I (in Ref. 1; AAP86657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 108977 MW; 10D58A5D85D3171D CRC64;
MATPMVSSAG GLLAMLNEPH PVLKLHALSN LNNLVDQFWP EISTSVPIIE SLYEDEEFDL
HQRQLAALLV SKVFYYLGEL NDSLSYALGA GPLFDVSEDS DYVHTLLAKA IDEYASLRSK
AVESNEMVDI DPRLEAIVER MLGKCISDGK YQQAMGIAIE CRRLDKLEEA IIKSDNVQGT
LSYCINVSHS FVNRREYRHE VLSLLVKVYQ KLPSPDYLSI CQCLMFLDEP QGVASILEKL
LRSENKDDAL LALQIAFDLV ENEHQAFLLS VRDRLPAPKT RAVEATQAVE TTIAPNENPS
GDVQMADETP AQTIVHETDP VDATYAERLT KIKGILSGET SIQLTLQFLY SHNKSDLLIL
KTIKQSVEMR NSVCHSATIY ANAIMHAGTT VDTFLRENLD WLSRATNWAK FSATAGLGVI
HRGHLQQGRS LMAPYLPQGG AGGGGSPYSE GGALYALGLI HANHGEGIKQ FLRDSLRSTN
VEVIQHGACL GLGLSALGTA DEEIYDDVKS VLYTDSAVAG EAAGISMGLL LVGTATEKAS
EMLAYAHETQ HEKIIRGLAL GIALTVYGRE EGADTLIEQM TRDQDPIIRY GGMYALALAY
SGTANNKAIR QLLHFAVSDV SDDVRRTAVL ALGFVLYSDP EQTPRIVSLL SESYNPHVRY
GAALAVGISC AGTGLSEAIS LLEPLTSDVV DFVRQGALIA MAMVMVQISE ASDSRVGVFR
RQLEKIILDK HEDTMSKMGA ILASGILDAG GRNVTIRLLS KTKHDKVTAV IGLAVFSQFW
YWYPLIYFIS LAFSPTAFIG LNYDLKVPKF EFMSHAKPSL FEYPKPTTVP TANTAVKLPT
AVLSTSVKAK ARAKKEAEQK AIAEKTSGPE KPVNESGSGK GKASTEKEGD SMQVDSPAAV
EKKAPEPEPA FEILVNPARV VPAQEKYIKL LDDSRYVPVK LAPSGFVLLK DLREHEPEVL
SLTDAPTSTA SPATGTAAAA QGTPASAMAV DDEPQPPQAF EYAS
