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Database: UniProt
Entry: A0AA38I6P4_9CUCU
LinkDB: A0AA38I6P4_9CUCU
Original site: A0AA38I6P4_9CUCU 
ID   A0AA38I6P4_9CUCU        Unreviewed;       405 AA.
AC   A0AA38I6P4;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   ORFNames=Zmor_021640 {ECO:0000313|EMBL:KAJ3649924.1};
OS   Zophobas morio.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Zophobas.
OX   NCBI_TaxID=2755281 {ECO:0000313|EMBL:KAJ3649924.1, ECO:0000313|Proteomes:UP001168821};
RN   [1] {ECO:0000313|EMBL:KAJ3649924.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=QUZm001 {ECO:0000313|EMBL:KAJ3649924.1};
RX   PubMed=37002914; DOI=10.1093/g3journal/jkad079;
RA   Kaur S., Stinson S.A., diCenzo G.C.;
RT   "Whole genome assemblies of Zophobas morio and Tenebrio molitor.";
RL   G3 (Bethesda) 13:jkad079-jkad079(2023).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAJ3649924.1}.
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DR   EMBL; JALNTZ010000006; KAJ3649924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AA38I6P4; -.
DR   Proteomes; UP001168821; Unassembled WGS sequence.
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:UP001168821}.
FT   DOMAIN          19..132
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          272..382
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..405
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..235
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..405
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  43255 MW;  084E9D022FFE8237 CRC64;
     MPAGGALFGS AATGPGSTGG NKHLVEVRAG KMNLKGRMVY PDKRKGLLYV YQSDDSLMHF
     CWQDRTTGIV EDDLIIFPDD CEYIKVPQCT TGRVYLLKFK SSSRKFFFWL QEPRTDKDDD
     NCKRINELLN NPSSAVQSSQ SPDQDLQSLF NNMSQSQLMQ LFGSGVGQMG GLSSLLGTIR
     GPNSGSARTS TTPAITHRTT VPSTPTTNTT TTTVSSNPPA TTTTPQTTTA PVTAPGAPAR
     ASNTARSSDS SCGHRIQLSD LQNFLQGITP ISSSQQSGVD LSTALTADSL SGILNNPGAL
     QALQSHLPAV EGDPQEALRS TINSPQFQQA VSQFSSALES GQLGPVVSQL AVNPEAVAAA
     AQGNMQDFVK ALEKNEATGS KEESDKDKKE EKKDDKDDDQ NMQLD
//
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