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Database: UniProt
Entry: A0AAD1SNN4_PELCU
LinkDB: A0AAD1SNN4_PELCU
Original site: A0AAD1SNN4_PELCU 
ID   A0AAD1SNN4_PELCU        Unreviewed;       405 AA.
AC   A0AAD1SNN4;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   SubName: Full=Proteasomal ubiquitin receptor ADRM1 isoform X1 {ECO:0000313|EMBL:CAH2303155.1};
GN   ORFNames=PECUL_23A006554 {ECO:0000313|EMBL:CAH2303155.1};
OS   Pelobates cultripes (Western spadefoot toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pelobatoidea; Pelobatidae; Pelobates.
OX   NCBI_TaxID=61616 {ECO:0000313|EMBL:CAH2303155.1, ECO:0000313|Proteomes:UP001295444};
RN   [1] {ECO:0000313|EMBL:CAH2303155.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Alioto T., Alioto T., Gomez Garrido J.;
RL   Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
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   EMBL; OW240917; CAH2303155.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD1SNN4; -.
DR   Proteomes; UP001295444; Chromosome 06.
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|EMBL:CAH2303155.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP001295444}.
FT   DOMAIN          17..130
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          277..391
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          195..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..258
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  42167 MW;  98D40415D8B84282 CRC64;
     MSSGALFPSL VPGSRGSTSK YLVEFRAGKM SLKGSTVTPD KRKGLVYIQQ TDDSLIHFCW
     KDRTSGNVDD DLIIFPDDCE FKKVTQCTTG RVFVLKFKAG SKRLFFWMQE PKTDKDEENC
     RKVNEYLNNP PMPGALGGSG SGGHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
     GLGALTGPGL ASLLGSGGPT TSSSSSSSRS QSAAVTPSST TSSTRTATAA PVTPAAVPAA
     TPSPAVSSGN GASAAASPTQ PIQLSDLQNI LATMNVPATG EDGQRVDLAT VLTPEIMAPI
     LANAEVQERL MPYLPSGESL PQTAEEIQNT LTSPQFQQAL SMFSAALASG QLGPLMSQFG
     LPAEAVDAAN KGDIEAFAKA MQSSSSQKER DSKEKKEEEE DMSLD
//
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