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Database: UniProt
Entry: A0A9Q0NC04_9DIPT
LinkDB: A0A9Q0NC04_9DIPT
Original site: A0A9Q0NC04_9DIPT 
ID   A0A9Q0NC04_9DIPT        Unreviewed;       388 AA.
AC   A0A9Q0NC04;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   Name=Rpn13 {ECO:0000313|EMBL:KAJ6647520.1};
GN   ORFNames=Bhyg_02743 {ECO:0000313|EMBL:KAJ6647520.1};
OS   Pseudolycoriella hygida.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Sciaroidea; Sciaridae;
OC   Pseudolycoriella.
OX   NCBI_TaxID=35572 {ECO:0000313|EMBL:KAJ6647520.1, ECO:0000313|Proteomes:UP001151699};
RN   [1] {ECO:0000313|EMBL:KAJ6647520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HSMRA1968 {ECO:0000313|EMBL:KAJ6647520.1};
RC   TISSUE=Whole embryos {ECO:0000313|EMBL:KAJ6647520.1};
RA   Trinca V., Uliana J.V.C., Torres T.T., Ward R.J., Monesi N.;
RL   Submitted (JUL-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:KAJ6647520.1}.
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DR   EMBL; WJQU01000001; KAJ6647520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9Q0NC04; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP001151699; Chromosome A.
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   Receptor {ECO:0000313|EMBL:KAJ6647520.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP001151699}.
FT   DOMAIN          16..129
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          258..370
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          173..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..209
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  42296 MW;  809CA546BFD58F13 CRC64;
     MSGPIFGNNS SMGSSGGNRH LVEFRAGRMN MVGKMVTPDT RKGLVYLFQA EDQLIHFCWK
     DRSTGKVEDD LIIFPDDCEF KRIDQCKTGR VYLLKFKSSS KRLFFWMQEP KNDKDDEYCR
     RMNDIMNNPP SANSLSSSRV GESNDLQNML NNMSQMQLMQ LFGGVGQMGG LSNLLGSIHR
     PSDSSRTSAR TSTTSTTPAS ATATATTAPE TPNNAVSVVT PTAPKKNDSG KKDDVSKVLL
     SELQSFLSGL KTSDGSGPSS TNGRNIDLST AVNAETVSFL TDAERTENLL AHLPNIESND
     NTKQQLRETI SSPQFQQALS MFSSALQSGQ LGPVVSQFQL NDEAVAAATT GDLEQFVKAL
     EKNAKEIVAK ASEKDKEQDK KEDKSGST
//
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