ID A0A7J8DEQ3_ROUAE Unreviewed; 398 AA.
AC A0A7J8DEQ3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000256|ARBA:ARBA00068549};
DE AltName: Full=Rpn13 homolog {ECO:0000256|ARBA:ARBA00079688};
GN ORFNames=HJG63_000404 {ECO:0000313|EMBL:KAF6421631.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6421631.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6421631.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6421631.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6421631.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:KAF6421631.1}.
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DR EMBL; JACASE010000012; KAF6421631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8DEQ3; -.
DR Proteomes; UP000593571; 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 Reference proteome {ECO:0000313|Proteomes:UP000593571}.
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 268..382
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 187..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..233
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 41142 MW; 90118A3CBD1E6A8F CRC64;
MTTSGALFPS LVPGSRGSSN KYLVEFRAGK MSLKGTTVTP DKRKGLVYVQ QTDDSLIHFC
WKDRTSGSVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNEYLNN PPMPGALGAS GSGEGGLQSL LGNMSHSQLM QLIGPAGLGG LGGLGALTGP
GLASLLGSGG PPASSSSSSS RSQSAAVTPS STASSARATP APSAPAAASA TSPSPAPSPG
NGTSTAASPT QPIQLSDLQS ILATMNVPAG PGGGQQVDLA SVLTPEIMAP ILANADVQER
LLPYLPSGES LPQTADEIQN TLTSPQFQQA LGMFSAALAS GQLGPLMCQF GLPAEAVEAA
NKGDVEAFAK AMQNSARSEP KEGDGKDKKD EEEDMSLD
//
