ID A0A6P7YR01_9AMPH Unreviewed; 411 AA.
AC A0A6P7YR01;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000313|RefSeq:XP_030067398.1, ECO:0000313|RefSeq:XP_030067399.1};
GN Name=ADRM1 {ECO:0000313|RefSeq:XP_030067398.1,
GN ECO:0000313|RefSeq:XP_030067399.1};
OS Microcaecilia unicolor.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Gymnophiona; Siphonopidae; Microcaecilia.
OX NCBI_TaxID=1415580 {ECO:0000313|Proteomes:UP000515156, ECO:0000313|RefSeq:XP_030067398.1};
RN [1] {ECO:0000313|RefSeq:XP_030067398.1, ECO:0000313|RefSeq:XP_030067399.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-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}.
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_030067398.1; XM_030211538.1.
DR RefSeq; XP_030067399.1; XM_030211539.1.
DR AlphaFoldDB; A0A6P7YR01; -.
DR GeneID; 115475641; -.
DR KEGG; muo:115475641; -.
DR CTD; 11047; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000515156; Chromosome 8.
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 Receptor {ECO:0000313|RefSeq:XP_030067398.1,
KW ECO:0000313|RefSeq:XP_030067399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000515156}.
FT DOMAIN 17..130
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 286..398
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 193..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 42511 MW; 36D6C85D1724BC70 CRC64;
MSSGALFPSL VSGSRGSSSK YLVEFRAGKM SLKGTTVTPD KRKGLVYIQQ TDDSLIHFCW
KDRTSGNLED DLIIFPDDCE FKRVPQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDEEYC
RKVNEYLNNP PMPGALGGSG SGGHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
GLGALTGPGL ASLLGSGGPP ASSSSSSSRS QSTAVTPSST TSSTRVASTP SAPAAAAASA
TTTTAAASPT TATSSGNGAS TAASPTQPIQ LSDLQNILAT MNVPAVAGGG QQVDLASVLT
PEIMAPILAN AAVQERLMPY LPSGESLPQT VDEIQNTLTS PQFQQALSMF SAALASGQLG
PLMSQFGLPT EAVDAANKGD VEAFASAMQT NSQSDPKEED KKEEEEDMSL D
//