GenomeNet

Database: UniProt
Entry: B3M1I7_DROAN
LinkDB: B3M1I7_DROAN
Original site: B3M1I7_DROAN 
ID   B3M1I7_DROAN            Unreviewed;      1032 AA.
AC   B3M1I7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1 {ECO:0000256|ARBA:ARBA00014929, ECO:0000256|PIRNR:PIRNR015947};
GN   Name=Dana\GF16602 {ECO:0000313|EMBL:EDV43278.2};
GN   Synonyms=dana_GLEANR_17871 {ECO:0000313|EMBL:EDV43278.2};
GN   ORFNames=GF16602 {ECO:0000313|EMBL:EDV43278.2};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV43278.2, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV43278.2, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
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; CH902617; EDV43278.2; -; Genomic_DNA.
DR   RefSeq; XP_001954717.2; XM_001954681.2.
DR   STRING; 7217.B3M1I7; -.
DR   EnsemblMetazoa; FBtr0121302; FBpp0119794; FBgn0093623.
DR   eggNOG; KOG2062; Eukaryota.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   InParanoid; B3M1I7; -.
DR   Proteomes; UP000007801; 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; 2.
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:UP000007801};
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..907
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   DOMAIN          901..996
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          279..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  114481 MW;  F4BB18C24FAF5855 CRC64;
     MSLTSAAGII SLLDEPMPDL KVFALKKLDN IVDEFWPEIS ESIEKIEMLH EDRSFPENKL
     AGMVASKVFY HLGSFEDALT YALGAGDLFD VNARNEYTET IIAKCIDFYI AQRVEFIENP
     KEATAVDERL EGIVNRMIQR CLDDNQFRQA LGIALETRRM DIFEVAIMKS DDVRGMLAYA
     YNVTMSLIQN RAFRNQVLRC LVGLYRDLGV PDYVNMCQCL IFLEDPLAVA EMLDALTRSS
     VETNNLMAYQ IAFDLYESAT QEFLGNVLQA LKNTAPIPTA LPSTFKPQGT SSGDSKSEDD
     GKSKSSEDIT EEKEADAKVE RTIESLNEVE KLHQKNIEKL ISILSGEVSI DLQLQFLIRS
     NHADLQVLRG TKEAVRVSIC HTATVIANAF MHSGTTSDQF LRDNLDWLAR ATNWAKLTAT
     ASLGVIHRGH EKDSLALMQS YLPKEAGPSS GYSEGGALYA LGLIHANHGA NIIDYLLQQL
     KDAQNENVRH GGCLGLGLAG MGTHRQDLYE QLKFNLYQDD AVTGEAAGIA MGMVMLGSKN
     AQAIEDMVSY AQETQHEKIL RGLAVGISLT MFSRLEEADP LVTSLSTDKD PVLRRSGMYT
     LAMAYNGTGS NKAIRKLLHV AVSDVNDDVR RAAVTAIGFI LFRTPEQCPS VVSLLAESYN
     PHVRYGAAMA LGIACAGTGL REAIALLEPM VKFDPVNFVR QGALIASAMI LIQHTDQSCP
     KTTFFRQLYA EVISNKHEDV MAKYGAILAQ GIIDAGGRNA TLSLQSRTGH TNLQAVVGML
     AFTQYWYWFP LAHTLSLAFT PTCVIGLNSD LKMPKMEFKS AAKPSLYAYP APLEEKKSEE
     REKVATAVLS IAARQKRREN ADKKEDEKMD VDEDSKEATT SVKKEEEAKT EEKPAVEEKP
     KKKEEKEKKK EEDKEAASTS SSSDKEKEKE KEKDKKEKKE PEPTSEVLQN PARVLRQQLK
     VLSVIDGQLY EPLKEVTIGG IIVFQHTGKA EDQELVEPVA AFGPMNDEEK EPEPPEPFEY
     IEDXMGMLFV II
//
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