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Database: UniProt
Entry: A0A8C0JFD6_CANLU
LinkDB: A0A8C0JFD6_CANLU
Original site: A0A8C0JFD6_CANLU 
ID   A0A8C0JFD6_CANLU        Unreviewed;       406 AA.
AC   A0A8C0JFD6;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000256|ARBA:ARBA00068549};
DE   AltName: Full=Rpn13 homolog {ECO:0000256|ARBA:ARBA00079688};
GN   Name=ADRM1 {ECO:0000313|Ensembl:ENSCAFP00020000113.1};
OS   Canis lupus dingo (dingo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=286419 {ECO:0000313|Ensembl:ENSCAFP00020000113.1, ECO:0000313|Proteomes:UP000694391};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00020000113.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00020000113.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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). Interacts with the proteasomal scaffolding
CC       protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction
CC       activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts
CC       with UBQLN2 and ubiquitin. {ECO:0000256|ARBA:ARBA00061738}.
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_025326400.1; XM_025470615.3.
DR   AlphaFoldDB; A0A8C0JFD6; -.
DR   Ensembl; ENSCAFT00020000137.1; ENSCAFP00020000113.1; ENSCAFG00020000118.1.
DR   GeneID; 112674229; -.
DR   KEGG; clud:112674229; -.
DR   CTD; 11047; -.
DR   GeneTree; ENSGT00390000013839; -.
DR   Proteomes; UP000694391; 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:UP000694391}.
FT   DOMAIN          18..131
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          277..391
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          196..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..248
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  42030 MW;  479E82BDFB6C8EBE CRC64;
     MTTSGALFPS LVPGSRGSSN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
     WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
     CRKVNEYLNN PPMPGALGTS GSGGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
     GGLGALTGPG LASLLGSGGP PASSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASVT
     SPSPAPSSGN GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGGQQVDLAS VLTPEIMAPI
     LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
     LPAEAVEAAN KGDVEAFAKA MQNSARSEQE GDGKDKKDEE EDMSLD
//
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