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Database: UniProt
Entry: A0A8C6QCH1_NANGA
LinkDB: A0A8C6QCH1_NANGA
Original site: A0A8C6QCH1_NANGA 
ID   A0A8C6QCH1_NANGA        Unreviewed;       309 AA.
AC   A0A8C6QCH1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000256|ARBA:ARBA00068549};
DE   AltName: Full=110 kDa cell membrane glycoprotein {ECO:0000256|ARBA:ARBA00083501};
DE   AltName: Full=Adhesion-regulating molecule 1 {ECO:0000256|ARBA:ARBA00078376};
DE   AltName: Full=Rpn13 homolog {ECO:0000256|ARBA:ARBA00079688};
GN   Name=Adrm1 {ECO:0000313|Ensembl:ENSNGAP00000001376.1};
OS   Nannospalax galili (Northern Israeli blind subterranean mole rat) (Spalax
OS   galili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Spalacidae; Spalacinae; Nannospalax.
OX   NCBI_TaxID=1026970 {ECO:0000313|Ensembl:ENSNGAP00000001376.1, ECO:0000313|Proteomes:UP000694381};
RN   [1] {ECO:0000313|Ensembl:ENSNGAP00000001376.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNGAP00000001376.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). Interacts with the proteasomal scaffolding
CC       protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction
CC       activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts
CC       with UBQLN2 and ubiquitin. {ECO:0000256|ARBA:ARBA00061738}.
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   AlphaFoldDB; A0A8C6QCH1; -.
DR   Ensembl; ENSNGAT00000001398.1; ENSNGAP00000001376.1; ENSNGAG00000001016.1.
DR   GeneTree; ENSGT00390000013839; -.
DR   Proteomes; UP000694381; 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; 1.10.2020.20:FF:000001; Proteasomal ubiquitin receptor ADRM1; 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:UP000694381}.
FT   DOMAIN          18..146
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          179..293
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          139..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..150
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  32823 MW;  2F1F9EE8E392E87B CRC64;
     MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
     WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ VGLGPSLGQV
     WPACWGAVGL RQAALHPAAS ATSPSPAPSS GNGTSTAASP TQPIQLSDLQ SILATMNVPA
     GPGGSQQVDL ASVLTPEIMA PILANADVQE RLLPYLPSGE SLPQTADEIQ NTLTSPQFQQ
     ALGMFSAALA SGQLGPLMCQ FGLPAEAVEA ANKGDVEAFA KAMQNNAKSE PKEGDSKDKK
     DEEEDMSLD
//
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