ID A0A2K6NKB4_RHIRO Unreviewed; 445 AA.
AC A0A2K6NKB4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 36.
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:ENSRROP00000004702.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000004702.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000004702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSRROP00000004702.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_030769773.1; XM_030913913.1.
DR AlphaFoldDB; A0A2K6NKB4; -.
DR STRING; 61622.ENSRROP00000004702; -.
DR Ensembl; ENSRROT00000021600.1; ENSRROP00000004702.1; ENSRROG00000019480.1.
DR GeneID; 104663820; -.
DR CTD; 11047; -.
DR GeneTree; ENSGT00390000013839; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0070628; F:proteasome binding; IEA:Ensembl.
DR GO; GO:0043248; P:proteasome assembly; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:Ensembl.
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:UP000233200}.
FT DOMAIN 18..169
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 315..429
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 232..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 46252 MW; 3CF29D5AF983CE25 CRC64;
MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ LQSVRWVQRP
LLILPSVSDH GACCRFCAVT GSVAENCLEP KTDQDEEHCR KVNEYLNNPP MPGALGASGS
SGHELSALGG EGGLQSLLGN MSHSQLMQLI GPAGLGGLGG LGALTGPGLA SLLGSSGPPG
SSSSSSSRSQ SAAVTPSSTT SSTRATPAPS APAAASATSP SPAPSSGNGA STAASPTQPI
QLSDLQSILA TMNVPAGPAG GQQVDLASVL TPEIMAPILA NADVQERLLP YLPSGESLPQ
TAEEIQNTLT SPQFQQALGM FSAALASGQL GPLMCQFGLP AEAVEAANKG DVEAFAKAMQ
NSAKPEQKEG DTKDKKDEEE DMSLD
//
