PRS7A_ARATH
ID PRS7A_ARATH Reviewed; 426 AA.
AC Q9SSB5; Q9SEI6;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=26S proteasome regulatory subunit 7 homolog A;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT1a;
DE AltName: Full=26S proteasome subunit 7 homolog A;
DE AltName: Full=Regulatory particle triple-A ATPase subunit 1a;
GN Name=RPT1A; OrderedLocusNames=At1g53750; ORFNames=F22G10.2, T18A20.1;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=10417703; DOI=10.1046/j.1365-313x.1999.00479.x;
RA Fu H., Doelling J.H., Rubin D.M., Vierstra R.D.;
RT "Structural and functional analysis of the six regulatory particle triple-A
RT ATPase subunits from the Arabidopsis 26S proteasome.";
RL Plant J. 18:529-539(1999).
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 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND UBIQUITINATION AT LYS-400.
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 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF123390; AAF22521.1; -; mRNA.
DR EMBL; AC009324; AAF02852.1; -; Genomic_DNA.
DR EMBL; AC024260; AAG51970.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32992.1; -; Genomic_DNA.
DR EMBL; AY062860; AAL32938.1; -; mRNA.
DR EMBL; BT000069; AAN15388.1; -; mRNA.
DR PIR; G96577; G96577.
DR RefSeq; NP_175778.1; NM_104252.3.
DR AlphaFoldDB; Q9SSB5; -.
DR SMR; Q9SSB5; -.
DR BioGRID; 27037; 114.
DR IntAct; Q9SSB5; 2.
DR STRING; 3702.AT1G53750.1; -.
DR iPTMnet; Q9SSB5; -.
DR PaxDb; Q9SSB5; -.
DR PRIDE; Q9SSB5; -.
DR ProteomicsDB; 226337; -.
DR EnsemblPlants; AT1G53750.1; AT1G53750.1; AT1G53750.
DR GeneID; 841812; -.
DR Gramene; AT1G53750.1; AT1G53750.1; AT1G53750.
DR KEGG; ath:AT1G53750; -.
DR Araport; AT1G53750; -.
DR TAIR; locus:2024822; AT1G53750.
DR eggNOG; KOG0729; Eukaryota.
DR HOGENOM; CLU_000688_6_1_1; -.
DR InParanoid; Q9SSB5; -.
DR OMA; INGYKKF; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9SSB5; -.
DR PRO; PR:Q9SSB5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSB5; baseline and differential.
DR Genevisible; Q9SSB5; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..426
FT /note="26S proteasome regulatory subunit 7 homolog A"
FT /id="PRO_0000084714"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
FT CONFLICT 327
FT /note="P -> S (in Ref. 1; AAF22521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 47803 MW; 81FC7DCDEA4D1A9F CRC64;
MVRDIEDEIR DEKNPRPLDE DDIALLKTYG LGPYSAPIKK VEKEIKDLAK KINDLCGIKE
SDTGLAPPSQ WDLVSDKQMM QEEQPLQVAR CTKIISPNTE DAKYVINVKQ IAKFVVGLGD
KVSPTDIEEG MRVGVDRNKY QIQIPLPPKI DPSVTMMTVE EKPDVTYNDV GGCKEQIEKM
REVVELPMLH PEKFVKLGID PPKGVLCYGP PGTGKTLLAR AVANRTDACF IRVIGSELVQ
KYVGEGARMV RELFQMARSK KACIVFFDEV DAIGGARFDD GVGGDNEVQR TMLEIVNQLD
GFDARGNIKV LMATNRPDTL DPALLRPGRL DRKVEFGLPD LESRTQIFKI HTRTMNCERD
IRFELLARLC PNSTGADIRS VCTEAGMYAI RARRKTVTEK DFLDAVNKVI KGYQKFSATP
KYMVYN
