ID A0A9N9SAY9_PHACE Unreviewed; 411 AA.
AC A0A9N9SAY9;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=PHAECO_LOCUS246 {ECO:0000313|EMBL:CAG9813474.1};
OS Phaedon cochleariae (Mustard beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX NCBI_TaxID=80249 {ECO:0000313|EMBL:CAG9813474.1, ECO:0000313|Proteomes:UP001153737};
RN [1] {ECO:0000313|EMBL:CAG9813474.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAG9813474.1}
RP NUCLEOTIDE SEQUENCE.
RG ENA_rothamsted_submissions;
RG culmorum;
RA King R.;
RL Submitted (OCT-2022) 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; OU896707; CAG9813474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9SAY9; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP001153737; Chromosome 1.
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; 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.
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:UP001153737}.
FT DOMAIN 24..122
FT /note="Pru"
FT /evidence="ECO:0000259|Pfam:PF04683"
FT DOMAIN 264..377
FT /note="RPN13 DEUBAD"
FT /evidence="ECO:0000259|Pfam:PF16550"
FT REGION 182..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..220
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 43757 MW; C9510F3829FE64C9 CRC64;
MPAGGALFGS AAAGPGSTGG NKHLIEVRAG KMSLKGRMVY PDKRKGLMYV YQSEDSLMHF
CWQDRTTGVV EDDLIIFPDD CEYVKIPQCT TGRAYLLKFK SSNKKFFFWL QEPSSSKDDD
NCKRINELLN NPSTAVQSTP NPDQDLQSLL NNMSQSQLMQ LFGSGVSQMG GLSSLLGTIR
GPNSGSARTN TTPAITHRTT VPSTPTTTTT TTNQAATPSA GLITPQRAIP NSTPDAPKAK
ANSRVPDNST PVPYSNPIQL SDLQTFLSGI APPATAEGTQ AQSVDLSTAL TSDALTGVLS
NPDTLQQLQS HLPAVDSNTQ EALRSTLASP QFQQAVSQFS SALESGQLGP IVSQLAVNPE
AVAAAAQGNM ADFVKALEKS TSHTEGASSE NKEQSVKKDD KKDDEDQMQL D
//
