PS13A_ARATH
ID PS13A_ARATH Reviewed; 386 AA.
AC Q8RWF0; Q9FK79;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 13 homolog A;
DE AltName: Full=26S proteasome regulatory subunit RPN9a;
DE Short=AtRNP9a;
DE AltName: Full=26S proteasome regulatory subunit S11 homolog A;
GN Name=RPN9A; OrderedLocusNames=At5g45620; ORFNames=MRA19.2;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND CLEAVAGE OF INITIATOR METHIONINE.
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 [6]
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 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=Q8RWF0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09205.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY230841; AAP86668.1; -; mRNA.
DR EMBL; AB012245; BAB09205.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95277.1; -; Genomic_DNA.
DR EMBL; AY093136; AAM13135.1; -; mRNA.
DR EMBL; BT003384; AAO30047.1; -; mRNA.
DR RefSeq; NP_199375.2; NM_123930.5. [Q8RWF0-1]
DR AlphaFoldDB; Q8RWF0; -.
DR SMR; Q8RWF0; -.
DR BioGRID; 19851; 106.
DR IntAct; Q8RWF0; 5.
DR STRING; 3702.AT5G45620.1; -.
DR iPTMnet; Q8RWF0; -.
DR PaxDb; Q8RWF0; -.
DR PRIDE; Q8RWF0; -.
DR ProteomicsDB; 226341; -. [Q8RWF0-1]
DR EnsemblPlants; AT5G45620.1; AT5G45620.1; AT5G45620. [Q8RWF0-1]
DR GeneID; 834602; -.
DR Gramene; AT5G45620.1; AT5G45620.1; AT5G45620. [Q8RWF0-1]
DR KEGG; ath:AT5G45620; -.
DR Araport; AT5G45620; -.
DR TAIR; locus:2171998; AT5G45620.
DR eggNOG; KOG2908; Eukaryota.
DR HOGENOM; CLU_042989_0_0_1; -.
DR InParanoid; Q8RWF0; -.
DR OMA; TWVQPRI; -.
DR PhylomeDB; Q8RWF0; -.
DR PRO; PR:Q8RWF0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWF0; baseline and differential.
DR Genevisible; Q8RWF0; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035298; PSMD13.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10539; PTHR10539; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:20516081,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..386
FT /note="26S proteasome non-ATPase regulatory subunit 13
FT homolog A"
FT /id="PRO_0000423173"
FT DOMAIN 173..347
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 386 AA; 44168 MW; 96222963E95E4743 CRC64;
MAALQYLESL KNTHPELGEW YNSLADLYQK KLWHQLTLKL EQFIALAVFQ AGDALIQFYH
NFITDFETKI NLLKLAHFAV VVSRQYSEKE AAVSYLESVI EKLRATKEPR ITEPIIYIET
QKALFKLEQG DQKECKKILD DGKSSLDSMT DIDPSVYANF YWVSSQYHKC RQEFSDFYKS
ALLYLAYTSV EDLSESFKLD LAFDLSLSAL LGENIYNFGE LLAHPILKSL LGTNVEWLYH
ILQAFNHGDL VQYQELCRVH NASLIAQPAL VENEKKLLEK INILCLIEII FSRPAEDRTI
PLSIIAERTK LSIEDVEHLL MKSLSVHLIE GIIDQVNGTI YVSWAQPRVL GIPQIKALRD
QLDSWVDKVH TTLLSVEAET PDLVAA
