PSD3A_ARATH
ID PSD3A_ARATH Reviewed; 488 AA.
AC Q9LNU4; Q6EMB6; Q8L852;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3 homolog A {ECO:0000303|PubMed:14623884};
DE AltName: Full=26S proteasome regulatory subunit RPN3a {ECO:0000303|PubMed:14623884};
DE Short=AtRPN3a {ECO:0000303|PubMed:14623884};
DE AltName: Full=26S proteasome regulatory subunit S3 homolog A;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2719;
DE AltName: Full=Protein HAPLESS 15 {ECO:0000303|PubMed:15514068};
GN Name=RPN3A {ECO:0000303|PubMed:14623884};
GN Synonyms=EMB2719, HAP15 {ECO:0000303|PubMed:15514068};
GN OrderedLocusNames=At1g20200 {ECO:0000312|Araport:AT1G20200};
GN ORFNames=T20H2.3 {ECO:0000312|EMBL:AAF79894.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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.
RX PubMed=15514068; DOI=10.1534/genetics.104.029447;
RA Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D.,
RA Levin J.Z., Preuss D.;
RT "Arabidopsis hapless mutations define essential gametophytic functions.";
RL Genetics 168:971-982(2004).
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).
RN [7]
RP INTERACTION WITH UCH1 AND UCH2.
RX PubMed=22951400; DOI=10.4161/psb.21899;
RA Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT associate with the 26S proteasome and the TREX-2 complex.";
RL Plant Signal. Behav. 7:1415-1419(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|UniProtKB:O43242}.
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 (PubMed:14623884, PubMed:20516081).
CC Interacts with UCH1 and UCH2 (PubMed:22951400).
CC {ECO:0000269|PubMed:14623884, ECO:0000269|PubMed:20516081,
CC ECO:0000269|PubMed:22951400}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- DISRUPTION PHENOTYPE: Short pollen tube growth and failure to exit the
CC style. {ECO:0000269|PubMed:15514068}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79894.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY230831; AAP86658.1; -; mRNA.
DR EMBL; AC022472; AAF79894.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29950.1; -; Genomic_DNA.
DR EMBL; AY120740; AAM53298.1; -; mRNA.
DR PIR; G86335; G86335.
DR RefSeq; NP_173447.1; NM_101873.3.
DR AlphaFoldDB; Q9LNU4; -.
DR SMR; Q9LNU4; -.
DR BioGRID; 23848; 95.
DR IntAct; Q9LNU4; 4.
DR STRING; 3702.AT1G20200.1; -.
DR iPTMnet; Q9LNU4; -.
DR PaxDb; Q9LNU4; -.
DR PRIDE; Q9LNU4; -.
DR ProteomicsDB; 226007; -.
DR EnsemblPlants; AT1G20200.1; AT1G20200.1; AT1G20200.
DR GeneID; 838609; -.
DR Gramene; AT1G20200.1; AT1G20200.1; AT1G20200.
DR KEGG; ath:AT1G20200; -.
DR Araport; AT1G20200; -.
DR TAIR; locus:2198561; AT1G20200.
DR eggNOG; KOG2581; Eukaryota.
DR HOGENOM; CLU_019858_1_0_1; -.
DR InParanoid; Q9LNU4; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR PhylomeDB; Q9LNU4; -.
DR PRO; PR:Q9LNU4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNU4; baseline and differential.
DR Genevisible; Q9LNU4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Proteasome; Reference proteome.
FT CHAIN 1..488
FT /note="26S proteasome non-ATPase regulatory subunit 3
FT homolog A"
FT /id="PRO_0000173822"
FT DOMAIN 240..421
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 451..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="K -> E (in Ref. 4; AAM53298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55582 MW; 615C5F3F28EC2D80 CRC64;
MTQDVEMKDN NTPSQSIISS STSTMQNLKE IAALIDTGSY TKEVRRIARA VRLTIGLRQK
LTGSVLSSFL DFALVPGSEA HSRLSSFVPK GDEHDMEVDT ASSATQAAPS KHLPAELEIY
CYFIVLLFLI DQKKYNEAKA CSSASIARLK NVNRRTIDVI ASRLYFYYSL SYEQTGDLAE
IRGTLLALHH SATLRHDELG QETLLNLLLR NYLHYNLYDQ AEKLRSKAPR FEAHSNQQFC
RYLFYLGKIR TIQLEYTDAK ESLLQAARKA PIAALGFRIQ CNKWAILVRL LLGEIPERSI
FTQKGMEKAL RPYFELTNAV RIGDLELFRT VQEKFLDTFA QDRTHNLIVR LRHNVIRTGL
RNISISYSRI SLPDVAKKLR LNSENPVADA ESIVAKAIRD GAIDATIDHK NGCMVSKETG
DIYSTNEPQT AFNSRIAFCL NMHNEAVRAL RFPPNTHKEK ESDEKRRERK QQEEELAKHM
AEEDDDDF
