ID M7XCN1_RHOT1 Unreviewed; 1034 AA.
AC M7XCN1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=RHTO_01599 {ECO:0000313|EMBL:EMS21539.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21539.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21539.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21539.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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; KB722655; EMS21539.1; -; Genomic_DNA.
DR RefSeq; XP_016272658.1; XM_016415280.1.
DR AlphaFoldDB; M7XCN1; -.
DR GeneID; 27365612; -.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000016926; 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..346
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 792..937
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 298..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 110853 MW; D3B16F9945320775 CRC64;
MVQSAQGLLS LLDEPEAALQ AHALSNINQR IDQFWAEVAD HVVKIEALSE DSSFPSRQLA
SLVASKLYYH LGNLDEALAF ALGAGKLFDV EQTGDVSPGE AEYVETVISK AIDSYTAARS
ASAPSPAFVD PARVPRDVDA RLEAVVERMF ERCERDGEYK QALGVALSSH RLDVVQRVFD
KTKDASLLEW ILDIVVRESV AVGGTSRSYK SEILQLLIKL FESLPSPDYF SITQCFVFLN
DPSLASSLLA KLLNLDSSEP PKDDAVLTAY QIAFDLAETA SQEFLQVVRT SVAGSEPEAV
EAAGGAPAAE EAKPKEGAEL HRERLATILS GEESIKLYLE FLYRNNKADL LILKDTLSAL
EPRNSIYHSA ISLMNAFAHA GTTSDLFLRE NLDFLGKASN WSKFTTTAAL GVIHKGNLTQ
GKAILEPYLP RSDGGGATKS VYSEGGSLYA LGLVNANHGK EDIVKYLMDT LKNSQDEVIQ
HGAALGLGVA AMGSGNEELY EELRNVLFTD SAIAGEAAGY SMGLVMLGTA SEKALDEMLQ
YAHETQHEKI IRGLAVGLAF LMYGKEEEAD SLIDTLSKDA DAILRYGGMY AVALAYAGTG
NNKAIRKLLH VAVSDVSDDV RRAAVTALGF ILFRNPTQVP RIVQLLAESY NPHVRYGSAL
ALGISCAGTG LEEAIALLEP LTKDPVDFVR QGACVSLAMV LIEQNETSHP KVASTRELYK
KIVSDKHADP MAKFGAALSQ GIIDAGGRNV TISMQNKSGS GNMPSIVGMA LFAQFWYWFP
LTHCLSLAFT PTAIIGVDKD LKIPKFEFVS NAKPSLFAYQ PATKPPTKET VEKVKTAVLS
TTAKVTARAK AKEAEQGKTE AMETDDKAEE KPAESTDDAE MKIDEAAGED KKKDQTKRKA
PEPSSSRLEN LSRVTPAQLQ YVSFPSDSRY VPVRPVNSGS APTPASLSSV TSSRSAPPVG
FGGGILLMRD TKPGDAAEFH ELEVLKAIDT AGAGAAATQA PGGEAAAGGD DADLLTGPIA
DPPAPFEWTD WGSD
//
