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Database: UniProt
Entry: A0A6I8VF12_DROPS
LinkDB: A0A6I8VF12_DROPS
Original site: A0A6I8VF12_DROPS 
ID   A0A6I8VF12_DROPS        Unreviewed;       419 AA.
AC   A0A6I8VF12;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   Name=Rpn13 {ECO:0000313|RefSeq:XP_015039898.1};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015039898.1};
RN   [1] {ECO:0000313|Proteomes:UP000001819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 {ECO:0000313|Proteomes:UP000001819};
RG   RefSeq;
RL   Submitted (JUN-2024) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_015039898.1}
RP   IDENTIFICATION.
RC   STRAIN=MV-25-SWS-2005 {ECO:0000313|RefSeq:XP_015039898.1};
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_015039898.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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   RefSeq; XP_015039898.1; XM_015184412.2.
DR   AlphaFoldDB; A0A6I8VF12; -.
DR   FunCoup; A0A6I8VF12; 1436.
DR   GeneID; 4804377; -.
DR   KEGG; dpo:4804377; -.
DR   InParanoid; A0A6I8VF12; -.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0072270; Expressed in female reproductive system and 3 other cell types or tissues.
DR   ExpressionAtlas; A0A6I8VF12; baseline.
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   FunFam; 1.10.2020.20:FF:000003; Proteasomal ubiquitin receptor ADRM1 homolog; 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|RefSeq:XP_015039898.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001819}.
FT   DOMAIN          12..125
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          273..387
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          122..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..192
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..253
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  45249 MW;  B613723B5B40D70B CRC64;
     MFGRQSGLGS SSNSSNLVEF RAGRMNMVGK MVHPDSRKGS VYMTQSDDGL MHFCWKDRTS
     GKVEDDLIVF PDDFEYKRVE QCKTGRVYVL KFKSSTRRMF FWMQEPKTDK DEEHCRRINE
     LLNNPPSAHQ RGGGGGSNDG DLQYMLNNMS QQQLMQLFGG VGQMGGLSSL LGQMNSRTPS
     SRNTSSSGGA SALQTPENIS VPRTPTAPKG SKSGSSRSNL NSQSDTAGSA SSSIDADASG
     KNSTTSTTTA SETTGAYANP FQAYLSNLSP EHGAGRSLNI DLSTALSGAE AINQLIADPE
     RVKTLIVHLP ESENADEDRK QQIKDHITSP QFQQALAQFS NALQSAQLGP VVKQFELSND
     AVAAAYSGNL EDFVNALQKS LPAGTTMGGE KEATEKKAEP EAAKDDNPEP VEKPEEKQK
//
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