ID A0A0A6YVU8_MOUSE Unreviewed; 407 AA.
AC A0A0A6YVU8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 28-JAN-2026, entry version 61.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000256|ARBA:ARBA00068549};
DE AltName: Full=110 kDa cell membrane glycoprotein {ECO:0000256|ARBA:ARBA00083501};
DE AltName: Full=Adhesion-regulating molecule 1 {ECO:0000256|ARBA:ARBA00078376};
DE AltName: Full=Rpn13 homolog {ECO:0000256|ARBA:ARBA00079688};
GN Name=Adrm1b {ECO:0000313|Ensembl:ENSMUSP00000141274.2,
GN ECO:0000313|MGI:MGI:3642386};
GN Synonyms=Gm9774 {ECO:0000313|MGI:MGI:3642386};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000141274.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000141274.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141274.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG Mouse Genome Sequencing Consortium;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000141274.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141274.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=21750661;
RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT "Modernizing reference genome assemblies.";
RL PLoS Biol. 9:e1001091-e1001091(2011).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000141274.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141274.2};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000141274.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141274.2};
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 AlphaFoldDB; A0A0A6YVU8; -.
DR SMR; A0A0A6YVU8; -.
DR FunCoup; A0A0A6YVU8; 1913.
DR STRING; 10090.ENSMUSP00000141274; -.
DR GlyGen; A0A0A6YVU8; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; A0A0A6YVU8; -.
DR jPOST; A0A0A6YVU8; -.
DR ProteomicsDB; 334378; -.
DR Ensembl; ENSMUST00000192538.2; ENSMUSP00000141274.2; ENSMUSG00000042165.10.
DR AGR; MGI:3642386; -.
DR MGI; MGI:3642386; Adrm1b.
DR VEuPathDB; HostDB:ENSMUSG00000042165; -.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; A0A0A6YVU8; -.
DR OMA; DQNQLMQ; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A0A0A6YVU8; protein.
DR Bgee; ENSMUSG00000042165; Expressed in blastoderm cell in morula and 54 other cell types or tissues.
DR ExpressionAtlas; A0A0A6YVU8; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR GO; GO:0000502; C:proteasome complex; ISO:GO_Central.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0061133; F:endopeptidase activator activity; ISO:GO_Central.
DR GO; GO:0140678; F:molecular function inhibitor activity; ISO:GO_Central.
DR GO; GO:0002020; F:protease binding; ISO:GO_Central.
DR GO; GO:0070628; F:proteasome binding; ISO:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; ISO:GO_Central.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; ISO:GO_Central.
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:UP000000589}.
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 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..254
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 42147 MW; 3E9040EA4BE1ED2D CRC64;
MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNECLNN PPMPGSLGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSSGP PASSSSSSSR SQSAAVTPSS STSSARATPA PSAPAAASAT
SPSPAPSSGN GTSTAASPTQ PIQLSDLQSI LATMNVPAWP GGSQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTADESQNT LTSPQFQQAL GMFSAALASG QLGPLMSQFG
LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE EEDMSLD
//
