ID I1I223_BRADI Unreviewed; 994 AA.
AC I1I223;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1 homolog {ECO:0000256|PIRNR:PIRNR015947};
GN Name=100835233 {ECO:0000313|EnsemblPlants:KQJ95640};
GN ORFNames=BRADI_3g18280v3 {ECO:0000313|EMBL:KQJ95640.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ95640};
RN [1] {ECO:0000313|EMBL:KQJ95640.1, ECO:0000313|EnsemblPlants:KQJ95640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95640.1,
RC ECO:0000313|EnsemblPlants:KQJ95640};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ95640.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95640.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ95640}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ95640};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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:0000256|PIRNR:PIRNR015947}.
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).
CC {ECO:0000256|PIRNR:PIRNR015947}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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DR EMBL; CM000882; KQJ95640.1; -; Genomic_DNA.
DR RefSeq; XP_003571547.1; XM_003571499.3.
DR AlphaFoldDB; I1I223; -.
DR STRING; 15368.I1I223; -.
DR EnsemblPlants; KQJ95640; KQJ95640; BRADI_3g18280v3.
DR GeneID; 100835233; -.
DR Gramene; KQJ95640; KQJ95640; BRADI_3g18280v3.
DR KEGG; bdi:100835233; -.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; I1I223; -.
DR OMA; NKVAHAD; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR048570; PSMD1_RPN2_N.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10943:SF13; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1 HOMOLOG; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18004; RPN2_C; 1.
DR Pfam; PF21505; RPN2_N; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR015947};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 8..350
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 793..957
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 282..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 108057 MW; E267BB5FAA8F45C1 CRC64;
MAAATVSSAS GLLAMLQEPA AELKLHALSN LNSLVHVFWP EISTSVPAIE SLYEDEEFDQ
RHLAALVVSK VFYYLSELND SLSYALGAGP LFDVSEDSDY TNTLLARALD EYASIRSKTS
KATEEEEMMD PRLEVIVERM LDKCILDGKY QQAMGMAVEC RRLDKLEDAI SRCDNLHGAL
SYCINLSHQY VSHREYRCEI LRCLVKIYKT LSNPDYLSIC QCLMFLGESE TVADILHKLL
SGSEDDALLA YQIAFDLVEN ENQAFLLNVR NHLDTLSMRT SALPSGQTDN AATEPAGDIQ
MGDDVATSNG SAQVVDPNEV AVTDKLSKIK GILSGETSIQ LTLQFLYSHN RSDLLILKTI
KQALEMRNSV CHSATICSNA IMHAGTTVDT FLRENLEWLS RATNWAKFSA TAGLGVIHRG
HLQQGRALMA PYLPQGGAVG GGSPYSEGGA LYALGLIHAN HGEGIKQFLR ESLRTTSSEV
VQHGACLGLG LASLGTADEE IFEDIKNILY TDSAVASEAA GIGLGLLMVG TATEKAGEML
AYAHDTQHEK IIRGLALGIA LTVYGREEEA DTLIEQMTRD QDPILRYGGM YAIALAYRGT
ANNKAIHQLL HFAVSDVNDD VRRTAVLALG FVLYNEPEQT PRIVSLLSES YNPHVRYGAA
LAVGISCAGT GLSDAISLLE PLTSDVVDFV RQGALIAMAM VMIQTNESYD PRVGTFRRQL
EKIILDKHED TMSKMGAILA SGIIDAGGRN VTIKLKSKSK HDKLTAVVGL AVFSQFWYWY
PLTYFISLAF SPTAIIGVNS DLRMPKLEFL SNAKPSLFDY PKPTSQQTAT AAVQLPTAIL
STYAKAKSRA AKKDAESKAQ EKAEAVQEKA ETAEGKAEAP TSEDASTSMQ VDGAAPEKKA
PEPEPTFQVL ANPARVLPAQ EKFIKFLEGS RYEPVKMAPS GFILLRDLKP TEAEELVLAD
TPSTAAAATN ATSQQSAMAV DEEPQPPEPF EYTS
//
