ID   PRS7B_ARATH             Reviewed;         464 AA.
AC   Q9SSB4; F4HTC4;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=26S proteasome regulatory subunit 7 homolog B;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT1b;
DE   AltName: Full=26S proteasome subunit 7 homolog B;
DE   AltName: Full=Regulatory particle triple-A ATPase subunit 1b;
GN   Name=RPT1B; OrderedLocusNames=At1g53780; ORFNames=T18A20.2;
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 [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   [2]
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   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
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   [4]
RP   CHARACTERIZATION OF THE 26S PROTEASOME 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 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:20516081}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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=Q9SSB4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- CAUTION: Was not identified as subunit of the 26S proteasome complex.
CC       {ECO:0000305|PubMed:20516081}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF02853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009324; AAF02853.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H96577; H96577.
DR   AlphaFoldDB; Q9SSB4; -.
DR   SMR; Q9SSB4; -.
DR   BioGRID; 27040; 113.
DR   IntAct; Q9SSB4; 1.
DR   STRING; 3702.AT1G53780.2; -.
DR   PaxDb; Q9SSB4; -.
DR   PRIDE; Q9SSB4; -.
DR   EnsemblPlants; AT1G53780.3; AT1G53780.3; AT1G53780.
DR   Gramene; AT1G53780.3; AT1G53780.3; AT1G53780.
DR   Araport; AT1G53780; -.
DR   eggNOG; KOG0415; Eukaryota.
DR   eggNOG; KOG0729; Eukaryota.
DR   InParanoid; Q9SSB4; -.
DR   PhylomeDB; Q9SSB4; -.
DR   PRO; PR:Q9SSB4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SSB4; baseline and differential.
DR   Genevisible; Q9SSB4; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   Alternative splicing; ATP-binding; Cytoplasm; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Proteasome; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..464
FT                   /note="26S proteasome regulatory subunit 7 homolog B"
FT                   /id="PRO_0000391486"
FT   BINDING         246..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        452
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SEI2"
SQ   SEQUENCE   464 AA;  51811 MW;  5DBA69CF503DE015 CRC64;
     MIIRDIMEDP ENEGPHNMRS DFEPLLSVLR LRDYETGDII EFDSTEASEE ALSDITEFGS
     TEASEAHFEE PYSARIKKVE KEINELAEKI CNLGIKESDT GLAPPNQWDL VSDKQMMQEE
     QPLLVATCTQ IISPNTEDAK YVVDIKKIGK YVVGLGDKAS PTDIEAGMRV GVDQKKYQIQ
     IPLPPKIDPS VTMMTVEEKP DATYSDIGGC KEQIEKIREV VELPMLHPEK FVRLGIDPPK
     GVLCYGPPGS GKTLVARAVA NRTGACFIRV VGSELVQKYI GEGARMVREL FQMARSKKAC
     ILFFDEIDAI GGARFDDGVG SDNEVQRTML EILYQLDGFD ARGNIKVLMA TNRPDILDPA
     LLRPGRLDRK VEFCLPDLEG RTQIFKIHTR TMSCERDIRF ELLAGLCPNS TGADIRSVCI
     EAGMYAIGAR RKSVTEKDFL DAVNKVVKGY QKFSATPKYM AYYI