ID A0AA41NDY4_SCICA Unreviewed; 396 AA.
AC A0AA41NDY4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
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 ORFNames=SUZIE_198795 {ECO:0000313|EMBL:MBZ3888606.1};
OS Sciurus carolinensis (Eastern gray squirrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Sciurinae; Sciurini; Sciurus.
OX NCBI_TaxID=30640 {ECO:0000313|EMBL:MBZ3888606.1, ECO:0000313|Proteomes:UP001166674};
RN [1] {ECO:0000313|EMBL:MBZ3888606.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SUZIE {ECO:0000313|EMBL:MBZ3888606.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:MBZ3888606.1};
RA Glass D.;
RT "Studies in the Genomics of Life Span.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBZ3888606.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAATJV010424079; MBZ3888606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA41NDY4; -.
DR Proteomes; UP001166674; Unassembled WGS sequence.
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:MBZ3888606.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001166674}.
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 255..380
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 198..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..254
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 41507 MW; 637A4CF6C99CA226 CRC64;
MTTSGALFPS LVPGSRVSSN EYLVEFWAGK MSLKGTMVTL DKQKGLVYIQ KTNNLLIHFC
WKDRTSGTVE DDLITFPDDC EFKRMPQCPS GRVYVLKFKA GSNWLFFWMQ EPKTDQDEEH
CRKVNEYMNN PPMPGALGAS GSGGHELLPL GGEGGLQSLL GNMSHSHLMQ LIGPAGLGGL
GGRGALTGPG VASLLGSGGL PASSSSSSSQ SQSAAVTPSS TTSSAHITPA PSAPAGASTT
SPSPAPSSGN GTSTAASLTQ PIQLNDLQSI LATMNVPAGP GGSQQVDLTS VLMPEMMCLL
PYLPFGESLP QTAEEIQSTL TSLQFQQALG MFSVALASGQ LGLLMCQFGL PVGAMEVANK
GNVEAFAKAM QNNDRPEQKE GDAKDKKDNK EDMSLD
//