ID A0A194PCC3_PAPXU Unreviewed; 1000 AA.
AC A0A194PCC3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1 {ECO:0000256|ARBA:ARBA00014929, ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=RR46_14435 {ECO:0000313|EMBL:KPI90931.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI90931.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI90931.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI90931.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI90931.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. {ECO:0000256|PIRNR:PIRNR015947}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). {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; KQ459606; KPI90931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PCC3; -.
DR STRING; 66420.A0A194PCC3; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProtKB-UniRule.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
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:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF01851; PC_rep; 3.
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:UP000053268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..272
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 791..967
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 276..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 110381 MW; F5834F954D3CA9A1 CRC64;
MNITSAAGII SLLDEPMHEV KEFALKRLDN IVDQFWPEIS ESIEKIEILH EDKVFSQHQL
AALVASKVYY HLGAFEDSLT YALGAGDLFD VNARNEYVDT TIAKAIDFYT QKRKALFVDN
SAETIDPRLE AIVNRMFQRC LDDGQYRQAL GLALETRRMD IFEESIMKSD DISGMLQYAF
TVAMSLLQNR GFRSTVLRSL VGLYRGLNIP DYVNMCQCLI FLEDPLSVAE ILDKLTHGPQ
ESVLMAYQIA FDLYDSATQQ FLGRVLQALR TTAPIPSALG GKPQPQGGPF PESSMEVDQT
PTEEAKKPER DIESLNDEEK EHQKRVEKLI SILGGDVSIG LQLQFLIRSN HADMLILKNT
KDAIRVSICH TATVIANSFM HAGTTSDQFL RDNLEWLARA TNWAKLTVTA SLGVIHRGHE
NESLALMQSY LPKEAGPSSG YSEGGGLYAL GLIHANHGAN IIDYLLTQLK DAQNEMVRHG
GCLGLGLAAM GTHRQDVYEQ LKFNLYQDDA VTGEAAGIAM GMVMLGSRNA AAIEDMVAYA
QETQHEKILR GLAVGISFTM YGRLEEADAL VQQLLRDKDP LLRRAGCYTI ATAYCGTGNN
DSIRTLLHVA VSDVNDDVRR AAVTALGFLL FRTPEQCPSV VSLLAESYNP HVRYGAAMAL
GIACAGTGNR EAIGLLEPMV KFDPVNFVRQ GALIASAMIL IQQTETLCPK VTYFRQLYAQ
VISNKHEDVM AKFGGILAQG IIDAGGRNVT VSLQNRTGHM NMLAVVGMLV FTQYWYWFPL
AHCLSLAFTP TCLIALNSDL KMPQLDFKSN AKPSLYAYPA PLEEKKREER ERVTTAVLSI
AAARARRRAH GTDSSSSSSA TTSTTSKMEV EEEEKKPTKS PNPNITVHGK SDKDAGTSKE
IKKEEKEGDE KEAKEKKEPE PNFEILNNPA RVVRQQLKGI TVVEGSGFIP LKDVTIGGIV
MLNHSGDVEQ VLVEPVAAFG PKTEEEKEPE PPEPFEYLDD
//
