PSA7A_ARATH
ID PSA7A_ARATH Reviewed; 250 AA.
AC P30186; Q41942; Q8LB36;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=Proteasome subunit alpha type-7-A;
DE AltName: Full=20S proteasome alpha subunit D-1;
DE AltName: Full=Proteasome component 6A;
DE AltName: Full=Proteasome subunit alpha type-4;
DE AltName: Full=TAS-G64;
GN Name=PAD1; Synonyms=PRC6A; OrderedLocusNames=At3g51260;
GN ORFNames=F24M12.300;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=1516703; DOI=10.1016/0014-5793(92)80796-j;
RA Genschik P., Philipps G., Gigot C., Fleck J.;
RT "Cloning and sequence analysis of a cDNA clone from Arabidopsis thaliana
RT homologous to a proteasome alpha subunit from Drosophila.";
RL FEBS Lett. 309:311-315(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9611183; DOI=10.1093/genetics/149.2.677;
RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.;
RT "Molecular organization of the 20S proteasome gene family from Arabidopsis
RT thaliana.";
RL Genetics 149:677-692(1998).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
RC STRAIN=cv. Columbia;
RA Philipps G., Gigot C.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7987412; DOI=10.1046/j.1365-313x.1994.6040537.x;
RA Genschik P., Jamet E., Phillips G., Parmentier Y., Gigot C., Fleck J.;
RT "Molecular characterization of a beta-type proteasome subunit from
RT Arabidopsis thaliana co-expressed at a high level with an alpha-type
RT proteasome subunit early in the cell cycle.";
RL Plant J. 6:537-546(1994).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=9373170; DOI=10.1016/s0014-5793(97)01228-3;
RA Parmentier Y., Bouchez D., Fleck J., Genschik P.;
RT "The 20S proteasome gene family in Arabidopsis thaliana.";
RL FEBS Lett. 416:281-285(1997).
RN [10]
RP SUBUNIT.
RX PubMed=10363660; DOI=10.1023/a:1006926322501;
RA Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M.,
RA Finley D., Vierstra R.D.;
RT "Structure and functional analyses of the 26S proteasome subunits from
RT plants.";
RL Mol. Biol. Rep. 26:137-146(1999).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIN10; KIN11 AND
RP SKP1A/ASK1.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [12]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [13]
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: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. Mediates
CC the association of the SCF(TIR1) E3 ubiquitin ligase complex with the
CC proteasome. {ECO:0000269|PubMed:11387208}.
CC -!- SUBUNIT: Component of the 20S core complex of the 26S proteasome. The
CC 26S proteasome is composed of a core protease (CP), known as the 20S
CC proteasome, capped at one or both ends by the 19S regulatory particle
CC (RP/PA700). The 20S proteasome core is composed of 28 subunits that are
CC arranged in four stacked rings, resulting in a barrel-shaped structure.
CC The two end rings are each formed by seven alpha subunits, and the two
CC central rings are each formed by seven beta subunits. The catalytic
CC chamber with the active sites is on the inside of the barrel. Interacts
CC with KIN10 and KIN11 SnRK subunits, and with the SKP1A/ASK1 subunit of
CC the SCF E3 ubiquitin ligase complex. {ECO:0000269|PubMed:10363660,
CC ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:11387208}.
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=P30186-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:1516703}.
CC -!- INDUCTION: During cell proliferation. {ECO:0000269|PubMed:7987412}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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; X66825; CAA47298.1; -; mRNA.
DR EMBL; AF043522; AAC32058.1; -; mRNA.
DR EMBL; AL132980; CAB62648.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78769.1; -; Genomic_DNA.
DR EMBL; AY042820; AAK68760.1; -; mRNA.
DR EMBL; AY052321; AAK96514.1; -; mRNA.
DR EMBL; AY061899; AAL31226.1; -; mRNA.
DR EMBL; AY081448; AAM10010.1; -; mRNA.
DR EMBL; AY087443; AAM64989.1; -; mRNA.
DR EMBL; Z17987; CAA79082.1; -; mRNA.
DR PIR; S29240; S29240.
DR RefSeq; NP_190694.1; NM_114985.3. [P30186-1]
DR AlphaFoldDB; P30186; -.
DR SMR; P30186; -.
DR BioGRID; 9607; 83.
DR IntAct; P30186; 4.
DR STRING; 3702.AT3G51260.1; -.
DR PaxDb; P30186; -.
DR PRIDE; P30186; -.
DR ProteomicsDB; 226488; -. [P30186-1]
DR EnsemblPlants; AT3G51260.1; AT3G51260.1; AT3G51260. [P30186-1]
DR GeneID; 824289; -.
DR Gramene; AT3G51260.1; AT3G51260.1; AT3G51260. [P30186-1]
DR KEGG; ath:AT3G51260; -.
DR Araport; AT3G51260; -.
DR TAIR; locus:2080833; AT3G51260.
DR eggNOG; KOG0183; Eukaryota.
DR InParanoid; P30186; -.
DR OMA; RLFHTEP; -.
DR PhylomeDB; P30186; -.
DR PRO; PR:P30186; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P30186; baseline and differential.
DR Genevisible; P30186; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus; Proteasome;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..250
FT /note="Proteasome subunit alpha type-7-A"
FT /id="PRO_0000124159"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O81149"
FT CONFLICT 15
FT /note="G -> N (in Ref. 7; CAA79082)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> L (in Ref. 6; AAM64989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 27337 MW; E026335F50C74AA3 CRC64;
MARYDRAITV FSPDGHLFQV EYALEAVRKG NAAVGVRGTD TVVLAVEKKS TPKLQDSRSA
RKIVSLDNHI ALACAGLKAD ARVLINKARI ECQSHRLTLE DPVTVEYITR YIAGLQQKYT
QSGGVRPFGL STLIVGFDPY TRIPALYQTD PSGTFSAWKA NATGRNSNSI REFLEKNYKE
SAGQETVKLA IRALLEVVES GGKNIEVAVM TREEGVLKQL EEEEIDIIVA EIEAEKAAAE
AAKKGPAKET
