ID A0A8C5R6X5_9ANUR Unreviewed; 424 AA.
AC A0A8C5R6X5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=ADRM1 26S proteasome ubiquitin receptor {ECO:0000313|Ensembl:ENSLLEP00000047290.1};
GN Name=ADRM1 {ECO:0000313|Ensembl:ENSLLEP00000047290.1};
OS Leptobrachium leishanense (Leishan spiny toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Megophryidae; Leptobrachium.
OX NCBI_TaxID=445787 {ECO:0000313|Ensembl:ENSLLEP00000047290.1, ECO:0000313|Proteomes:UP000694569};
RN [1] {ECO:0000313|Ensembl:ENSLLEP00000047290.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLLEP00000047290.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. Within the complex, functions as a proteasomal ubiquitin
CC receptor. {ECO:0000256|ARBA:ARBA00053191}.
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). {ECO:0000256|ARBA:ARBA00065254}.
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; A0A8C5R6X5; -.
DR Ensembl; ENSLLET00000049148.1; ENSLLEP00000047290.1; ENSLLEG00000029790.1.
DR GeneTree; ENSGT00390000013839; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000694569; 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:UP000694569}.
FT DOMAIN 26..139
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 298..410
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 205..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 44091 MW; F81D0391F57B783B CRC64;
MPPFSPPCRM SSGALFPSLV PGSRGSTSKY LVEFRAGKMS LKGSTVTPDK RKGLVYIQQT
DDSLIHFCWK DRTSGNVEDD LIIFPDDCEF KKVAQCTTGR VFVLKFKAGS KRLFFWMQEP
KTDKDEDNCR KVNEYLNNPP MPGALGGSGS GGHELSALGG EGGLQSLLGN MSHNQLMQLI
GPTGLGGLGG LGALTGPGLA SLLGSGAPTT SRGGYQSAAA TPSSTTSSTR TTTTTTAVAA
AAAAAAPVTP AAAAATLPAT PSPAVSSSNE ASAVASPTQP IQLSDLQNIL ATMNVPATAE
GGQRVDLAAV LTPEIMAPIL ANAEVQERLM PYLPSGESLP QTADEIQNTL TSPQFQQALS
MFSAALSSGQ LGPLMSQFGL PAEAVDAANK GDIEAFAKAM QSNSSQKERE SKEKKEEEED
MSLD
//
