ID E4V5N3_ARTGP Unreviewed; 1156 AA.
AC E4V5N3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=MGYG_08420 {ECO:0000313|EMBL:EFR05408.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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DR EMBL; DS989830; EFR05408.1; -; Genomic_DNA.
DR RefSeq; XP_003169515.1; XM_003169467.1.
DR AlphaFoldDB; E4V5N3; -.
DR STRING; 535722.E4V5N3; -.
DR GeneID; 10024745; -.
DR VEuPathDB; FungiDB:MGYG_08420; -.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_1_1; -.
DR InParanoid; E4V5N3; -.
DR OMA; IMFGRQE; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000002669; 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; IPR004155; PBS_lyase_HEAT.
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; 1.
DR Pfam; PF18004; RPN2_C; 1.
DR Pfam; PF21505; RPN2_N; 2.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SMART; SM00567; EZ_HEAT; 2.
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:UP000002669};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..117
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 197..358
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 892..1063
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 122..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 125667 MW; 6B0788039DF4E815 CRC64;
MVGLASAAGL VGFLSEPDTE LKVFALKALD AQVDLLWTEI AGSVGQIEAL SEDESFPERE
LASLVAAKVY YHLQEYSESM VFALGAGNRF DIENGGEFEE TIISKCVDTF ISTCSMLKAS
QNAGRGGAPQ LNTSFPRNEG GVSSTSAGLS SPITPFSQSA LPSKSLLSRP ESSAETSYPV
GEDRGSGRDE VPLVLQRGIQ RQLQNVIKRL FDRCFEQQRY RQVIGIAVEA KNLDIIRVAI
LRAAHDAKEQ GVEPSKRGEE LMDYVLGICM NVVQERGFRN EILKLILELL NEIPSPDYFS
IAKCVVYLNE HSMASDILQK LVEKGDARSL AVAYQISFDL YDNSTQEFLK KVRQELSVAI
TEFKETDSAK KMEQEPKESK ETDKLLSDDD EDDDDDDDDD EDEDEAPPAR RKFTDEGRAS
LKSIRSILDG ANSIQLNLEF LYRNNKADIA ILDKIKDSLE ARNSIFHTAV TCANAFMHAG
TTHDKFFRDN LDWLGKAVNW SKFTATAALG VIHRGNLTQG QKLLAPYLPK ESMAGVGNSG
SVYSQGGSLY AFGLIYANHE GWAVDHIREH FNKATEEVVQ HGGALGLGVA AMGTGDEGIY
SDLNKVLNAD LALNGEAVGL AMGLVMLGTG NMKALEDMIQ YAHLTQHEKI IRGLAMGMAL
IMYGRQEAAD ELINGLLGDP DPTLRYGGIM AIALAYCGTG SNKAVRKLLH VAVSDVSDDV
RRAAVMSLGF ILFRKHQSVP RMVELLSESY NPHVRYGAAM ALGISCAGTG LDEAIDLLEP
MLKDPTDFVR QGALIALSMV LVQQNEAMNP KVGTIRTAMQ KVIADRHEDA MAKFGCALAL
GIIDAGGRNC TISLQTQSGN LNMPGIVGMA VFTQYWYWFP LTHFLSLSFT PTAVIGVDQK
LEVPDFKFHS NTRPSLFDYP AEQQVKTDEA PEKIKTAVLS TTAQAKRRAQ KREKQRSGSI
DIEQTPSTPK SAAQQLPEKM DVDEASKAEE EKAGSEKETA TVEPKRKPEK EKVGYEISNL
SRVLPAQVKY ISFPDQRYEP VKKATGGVII LLDKKPSEPR DIIELSASKE TKPAATTAAG
GNQPSTIQSR LNAALQGAAQ AASGAAPTTP SRPGASTGAA AAAGVLTAVD EDEEGVEEAP
VPDDFTYESE GEDEEI
//
