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Database: UniProt
Entry: A0A6P7YR01_9AMPH
LinkDB: A0A6P7YR01_9AMPH
Original site: A0A6P7YR01_9AMPH 
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}.
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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
//
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