ID A0A3P7EHJ5_WUCBA Unreviewed; 420 AA.
AC A0A3P7EHJ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=WBA_LOCUS10338 {ECO:0000313|EMBL:VDM19126.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:VDM19126.1, ECO:0000313|Proteomes:UP000270924};
RN [1] {ECO:0000313|EMBL:VDM19126.1, ECO:0000313|Proteomes:UP000270924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYWW01012163; VDM19126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P7EHJ5; -.
DR FunCoup; A0A3P7EHJ5; 1768.
DR InParanoid; A0A3P7EHJ5; -.
DR OMA; SNQRHFF; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000270924; 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:UP000270924}.
FT DOMAIN 13..132
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 268..379
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..145
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 45457 MW; ABA582C5A7CC9432 CRC64;
MSVMFANSRS SQANNGYLVE FKAGRSNLQA GSAVDRRKVV ADKTKGLVFI KQSSDQLMHF
CWKNRETGAI VDDLIIFPGD TEFLRVKECT DGRVYMLKFK STDEKRLFWM QDGKADKDDE
NCKKVNETLN NPPAPRAAAR GGTDRAGASS FGTLAALGNA GADGELGALG NLDQSQLMQL
LSLMNHTNGA SASEATNLLP QLPLVTDAPH PVASEESGVT STQGATPSNT PANGTVASSS
SNNAVQLSQL KEIIASITPP DGSGRKRFIS VSASIDFTDV LCCADKINDV LGKYAERLIC
HLPNQEPIYN KQEELEQTLR TPQFRQAADI FGHALQTGQL APVLRQFGID EKTATGAGNG
DMIAWATQFT ASESGKEKVA MKIENSSHPD MESDVEDEET NEKVVREAKR NKPDDHMDLD
//
