ID A0A8J9UX46_9NEOP Unreviewed; 367 AA.
AC A0A8J9UX46;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
DE Flags: Fragment;
GN ORFNames=BINO364_LOCUS12749 {ECO:0000313|EMBL:CAH0727402.1};
OS Brenthis ino (lesser marbled fritillary).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Heliconiinae; Argynnini; Brenthis.
OX NCBI_TaxID=405034 {ECO:0000313|EMBL:CAH0727402.1, ECO:0000313|Proteomes:UP000838878};
RN [1] {ECO:0000313|EMBL:CAH0727402.1}
RP NUCLEOTIDE SEQUENCE.
RA Martin H S.;
RL Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC the deubiquitinating activity associated with the 26S proteasome.
CC {ECO:0000256|ARBA:ARBA00054744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ADRM1 family.
CC {ECO:0000256|ARBA:ARBA00009216}.
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DR EMBL; OV170226; CAH0727402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J9UX46; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000838878; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000838878}.
FT DOMAIN 1..101
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 213..339
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..116
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 367
FT /evidence="ECO:0000313|EMBL:CAH0727402.1"
SQ SEQUENCE 367 AA; 38442 MW; 0FCE9B5E5799CB65 CRC64;
MTLKGRMVHP DKRKGLLYVY QGEDSLMHFC WKDRTTGEVE DDLLIFPDDC EFVRVNECTT
GRVYVLKFKS FSKKYFFWMQ EPKTDKDDDY CRRINEALNN PPTSGGRGGG GSGGQDGELQ
NLLNNMSQQQ LMQLFGGVGQ IGGLSSLLGT MGNNSSGTTG TRPSGNSGSS SRGGSAPRTT
SAEAARTPAR PRYAPAPTAT PPNTATAAAP GAPGAAGGQI FLSDLQRYFS GLGNAPAEGE
CAAGGSAAPR VDLGAALAAP EVVSTASEPP HAQRLAPHLP QAPQDDAANQ FSSALTSGQM
GPVMSQFGLP SEVTSAANTG DMQAFFKALE SASSGSDASK SQDDKKKDKP QDDKNDKKDG
DGGMSLD
//
