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Database: UniProt
Entry: A0A6P8NI37_GEOSA
LinkDB: A0A6P8NI37_GEOSA
Original site: A0A6P8NI37_GEOSA 
ID   A0A6P8NI37_GEOSA        Unreviewed;       418 AA.
AC   A0A6P8NI37;
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_033770119.1, ECO:0000313|RefSeq:XP_033770120.1};
GN   Name=ADRM1 {ECO:0000313|RefSeq:XP_033770119.1,
GN   ECO:0000313|RefSeq:XP_033770120.1};
OS   Geotrypetes seraphini (Gaboon caecilian) (Caecilia seraphini).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Gymnophiona; Geotrypetes.
OX   NCBI_TaxID=260995 {ECO:0000313|Proteomes:UP000515159, ECO:0000313|RefSeq:XP_033770119.1};
RN   [1] {ECO:0000313|RefSeq:XP_033770119.1, ECO:0000313|RefSeq:XP_033770120.1}
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_033770119.1; XM_033914228.1.
DR   RefSeq; XP_033770120.1; XM_033914229.1.
DR   AlphaFoldDB; A0A6P8NI37; -.
DR   GeneID; 117345493; -.
DR   KEGG; gsh:117345493; -.
DR   CTD; 11047; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000515159; Chromosome 11.
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_033770119.1,
KW   ECO:0000313|RefSeq:XP_033770120.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515159}.
FT   DOMAIN          17..130
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          293..405
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          193..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..418
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  43128 MW;  9F9689B34E66F3AE CRC64;
     MSSGALFPSL VSGSRGSSSK YLVEFRAGKM SLKGTTVTPD KRKGLVYIQQ TDDSLIHFCW
     KDRTSGNLED DLIIFPDDCE FKRVPQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDEEYC
     RKVNEYLNNP PMPGALGGSG SGGHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
     GLGALTGPGL ASLLGSGGPP ASSSSSSSRS QSTAVTPSST TSSTRVTSTP SAPAAVTSAA
     ATTTTTTAAA AAAASPTTAT SSGNGASTAA SPTQPIQLSD LQNILATMNV PAVAGGGQQV
     DLASVLTPEI MAPILANAAV QERLMPYLPS GESLPQTADE IQNTLTSPQF QQALSMFSAA
     LASGQLGPLM SQFGLPTEAV DAANKGDVEA FASAMQTNSQ SDPKEEDKKE EEEDMSLD
//
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