ID A0A5E4MF97_9HEMI Unreviewed; 402 AA.
AC A0A5E4MF97;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=CINCED_3A025497 {ECO:0000313|EMBL:VVC29005.1};
OS Cinara cedri.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Lachninae; Cinara.
OX NCBI_TaxID=506608 {ECO:0000313|EMBL:VVC29005.1, ECO:0000313|Proteomes:UP000325440};
RN [1] {ECO:0000313|EMBL:VVC29005.1, ECO:0000313|Proteomes:UP000325440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (AUG-2019) 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; CABPRJ010000486; VVC29005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4MF97; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000325440; 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, ECO:0000313|EMBL:VVC29005.1};
KW Receptor {ECO:0000313|EMBL:VVC29005.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325440}.
FT DOMAIN 15..128
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 257..380
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 114..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..230
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 43306 MW; 4DE9E8CEA9ECCAD7 CRC64;
MSGATALFGN TTGRNQSKNL VEFRAGKMSM RGKTVYPDKR KGLVYIHQSD DSLIHFCWKD
RTTGAVEDDL IIFPDDCEFK FVSQCTTGRV YVLKFKSSSK KQFFWLQEPS KDKDEENCRR
VNDVMNNPPA PGSNRSGGTT PDGDLQNLLS NMSQQQLMQL FGGVGQIGGL SSLLGTMRSS
QTGRSSSSTQ SSSAQPTNTS SSTNTNTGSN RSTSNSNSPP PTSSTSTSSA ESQDQKLAAT
GIQLRDLQSM LSGLTGAQGT TDKPAVDLSA AMDLENLESV IDNKGAVNQL AQHLPTTESD
PDYDHGLSTR TTPDELKETI LSPQFRQAVS MFSNALQTGQ LGSVVQQFDL GAGAVSAANQ
GNMEEFVRAL QQTNINAEES EDVSPVNPEK RKKPDNDDIG SK
//
