GenomeNet

Database: UniProt
Entry: A0A8S4RGI4_9NEOP
LinkDB: A0A8S4RGI4_9NEOP
Original site: A0A8S4RGI4_9NEOP 
ID   A0A8S4RGI4_9NEOP        Unreviewed;       464 AA.
AC   A0A8S4RGI4;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   Name=jg10694 {ECO:0000313|EMBL:CAH2236311.1};
GN   ORFNames=PAEG_LOCUS13767 {ECO:0000313|EMBL:CAH2236311.1};
OS   Pararge aegeria aegeria.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX   NCBI_TaxID=348720 {ECO:0000313|EMBL:CAH2236311.1, ECO:0000313|Proteomes:UP000838756};
RN   [1] {ECO:0000313|EMBL:CAH2236311.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lindestad O.;
RL   Submitted (MAR-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}.
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:CAH2236311.1}.
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DR   EMBL; CAKXAJ010025202; CAH2236311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8S4RGI4; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000838756; 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:UP000838756}.
FT   DOMAIN          49..162
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          307..435
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          154..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..225
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..237
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..272
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..435
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  48361 MW;  A1B40C4C97F94F6B CRC64;
     MKFLYSNNFQ HYIEDCNYEL KTKQNRSVYI TMSATALFGN TSGLGGSSGG NKHLVEFRAG
     RMTLKGRMVH PDKRKGLLYV YQGEDSLMHF CWKDRTTGEV EDDLLIFPDD CEFMRVNECT
     TGRVYVLKFK SFSKKYFFWM QEPKTDKDDD LCRRINESLN NPPTSGERGS SGSGAQDGEL
     QNLLNNMSQQ QLMQLFGGVG QIGGLTSLLG TMGNNSSGGT GGSRTSGGSN SSSRGGSAPR
     TTDASARTPA RPRYPAAPNA TPTAAAAPAP SPAASATAAA PTAAAAATPT PTAAATAATA
     AAAAATPRSG QIFLSDLQRY FSGLGTAPEG EAAVGAAGAA APRVDLGAAL AAPDVLSTAS
     EPPNAQRLTP HLPPATSAAA DDAANQFSSA LTSGQMGPVV SQFGLPADVT SAANTGDMQA
     FFKALESASS GSESNRSQEA DKKKDKPQEE KSSKKDDDAG MSLD
//
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