ID A0A2K6NKA1_RHIRO Unreviewed; 407 AA.
AC A0A2K6NKA1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 32.
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:ENSRROP00000004701.1};
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:ENSRROP00000004701.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000004701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSRROP00000004701.1}
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_010363494.1; XM_010365192.2.
DR RefSeq; XP_010363495.1; XM_010365193.2.
DR AlphaFoldDB; A0A2K6NKA1; -.
DR Ensembl; ENSRROT00000021592.1; ENSRROP00000004701.1; ENSRROG00000019480.1.
DR GeneID; 104663820; -.
DR KEGG; rro:104663820; -.
DR CTD; 11047; -.
DR GeneTree; ENSGT00390000013839; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000233200; Unplaced.
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:UP000233200}.
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 277..391
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 194..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 42140 MW; CDF580C76152C2DA CRC64;
MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNEYLNN PPMPGALGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSSGP PGSSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT
SPSPAPSSGN GASTAASPTQ PIQLSDLQSI LATMNVPAGP AGGQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNSAKPEQK EGDTKDKKDE EEDMSLD
//