GenomeNet

Database: UniProt
Entry: B3P5K1_DROER
LinkDB: B3P5K1_DROER
Original site: B3P5K1_DROER 
ID   B3P5K1_DROER            Unreviewed;      1016 AA.
AC   B3P5K1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1 {ECO:0000256|ARBA:ARBA00014929, ECO:0000256|PIRNR:PIRNR015947};
GN   Name=Dere\GG11649 {ECO:0000313|EMBL:EDV53251.1};
GN   ORFNames=Dere_GG11649 {ECO:0000313|EMBL:EDV53251.1};
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000313|EMBL:EDV53251.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53251.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDV53251.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53251.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDV53251.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53251.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; CH954182; EDV53251.1; -; Genomic_DNA.
DR   RefSeq; XP_001981381.2; XM_001981345.2.
DR   AlphaFoldDB; B3P5K1; -.
DR   EnsemblMetazoa; FBtr0131703; FBpp0130195; FBgn0103946.
DR   GeneID; 6555053; -.
DR   KEGG; der:6555053; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   OMA; IMFGRQE; -.
DR   OrthoDB; 151732at2759; -.
DR   PhylomeDB; B3P5K1; -.
DR   Proteomes; UP000008711; 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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          4..274
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          802..989
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          279..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1016 AA;  112776 MW;  7F7839A024538E64 CRC64;
     MSLTSAAGII SLLDEPMPDL KVFALKKLDN IVDEFWPEIS ESIEKIEMLH EDRSFPENKL
     AGMVASKVFY HLGSFEDALT YALGAGDLFD VNARNEYTET IIAKCIDFYI AQRVEFIENP
     KEASVVDERL EGIVNRMIQR CLDDNQFRQA LGIALETRRM DTFKDAIMKS DDVRGMLAYA
     YNVTMSLIQN RGFRNEVLRC LVSLYRDLGV PDYVNMCQCL IFLEDPFAVA EMLDTLTRSS
     VETNNLMAYQ IAFDLYESAT QEFLGNVLQH LKNTAPIPTA LPSTFKPQGT TSEDGAKSEG
     DKSKSDEDIT EDKPADDKVE RTIDSLNEVE KLHQKNIEKL ISILSGEVSI DLQLQFLIRS
     NYADLQVLRG TKEAVRVSIC HTATVIANAF MHSGTTSDQF LRDNLDWLAR ATNWAKLTAT
     ASLGVIHRGH EKDSLALMQS YLPKEAGPSS GYSEGGALYA LGLIHANHGA NIIDYLLQQL
     KDAQNENVRH GGCLGLGLAG MGTHRQDLYE QLKFNLYQDD AVTGEAAGIA MGMVMLGSKN
     AQAIEDMVSY AQETQHEKIL RGLAVGISLT MFSRLEEADP LVTSLSSDKD PVLRRSGMYT
     IAMAYNGTGS NKAIRKLLHV AVSDVNDDVR RAAVTAIGFI LFRTPEQCPS VVSLLAESYN
     PHVRYGAAMA LGIACAGTGL REAIALLEPM VKFDPVNFVR QGALIASAMI LIQHTDQSCP
     KSTFFRQLYA EVISNKHEDV MAKYGAILAQ GIIDAGGRNA TLSLQSRTGH TNLQAVVGML
     AFTQYWYWFP LAHTLSLAFT PTCVIGLNSD LKMPKMVYKS AAKPSLYAYP APLEEKKSEE
     REKVATAVLS IAARQKRREN ADKKEDEKMD VDEDSKEGAA VKKDEETKTE EKPVTEEKPK
     KKEEKEKKKE EDKEAAGTSS EKDKEKDKKE KKEPEPTSEI LQNPARVLRQ QLKVLSVIDG
     QSYEPLKDVT IGGIIVFQHT GKAEDQELVE PVAAFGPMND EEKEPEPPEP FEYIED
//
DBGET integrated database retrieval system