ID A0A9N9WTS1_9DIPT Unreviewed; 407 AA.
AC A0A9N9WTS1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=CHIRRI_LOCUS11718 {ECO:0000313|EMBL:CAG9808883.1};
OS Chironomus riparius.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Chironomus.
OX NCBI_TaxID=315576 {ECO:0000313|EMBL:CAG9808883.1, ECO:0000313|Proteomes:UP001153620};
RN [1] {ECO:0000313|EMBL:CAG9808883.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAG9808883.1}
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; OU895879; CAG9808883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9WTS1; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP001153620; Chromosome 3.
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:UP001153620}.
FT DOMAIN 8..129
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 271..392
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 125..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 43860 MW; 8F5F63D331FE21F5 CRC64;
MFGSAAMSSS SNKLEFKAGR MTLIDSVQEG TKKKMVHADK RKGLVYIYSA DDGLTHFCWK
DRTSGNVEDD LIIFPDDCEF KKVDQCKDGR VFLLKFKSSN RKLFFWLQEP TNDKDDEYCR
KVNELLNNPP SANNGSSGGS GSRQEGSDLQ YMLNNMSQQQ LMQLFGGVGQ MGGLSSLLGS
LNRPSSGSRN TTTTSASSTP SATRTTTASS GGTAVAQTPE NTNQPATPRA PRKATNSGPT
EAATPATGSN TEASRVLLSE LQNYLAGISA GGSKQSSVDL STSLNSDTIN SILSDPELLK
SLQDHLPNIN ETDDEKKPVD SNSVKQQLKE TLASPQFQQA LSMFSNALQS GQLGPVVSQF
KLSDDAVLAA NSGDLEQFVK ALEKTSITDS KESDKNDEDD KKDESKN
//
