ID   ADRM1_CHICK             Reviewed;         406 AA.
AC   Q98SH3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE   AltName: Full=Adhesion-regulating molecule 1 {ECO:0000303|Ref.1};
DE            Short=ARM-1 {ECO:0000303|Ref.1};
GN   Name=ADRM1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Vigneron P., Dunon D.;
RT   "Expression pattern of chicken ARM-1.";
RL   Submitted (MAR-2001) 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:0000250|UniProtKB:Q16186}.
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:0000250|UniProtKB:Q16186}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16186}. Nucleus
CC       {ECO:0000250|UniProtKB:Q16186}.
CC   -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR   EMBL; AJ409217; CAC34571.1; -; mRNA.
DR   RefSeq; NP_989982.1; NM_204651.1.
DR   AlphaFoldDB; Q98SH3; -.
DR   SMR; Q98SH3; -.
DR   STRING; 9031.ENSGALP00000008336; -.
DR   PaxDb; Q98SH3; -.
DR   GeneID; 395365; -.
DR   KEGG; gga:395365; -.
DR   CTD; 11047; -.
DR   VEuPathDB; HostDB:geneid_395365; -.
DR   eggNOG; KOG3037; Eukaryota.
DR   InParanoid; Q98SH3; -.
DR   OrthoDB; 1479349at2759; -.
DR   PhylomeDB; Q98SH3; -.
DR   PRO; PR:Q98SH3; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0061133; F:endopeptidase activator activity; ISS:UniProtKB.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.2020.20; -; 1.
DR   Gene3D; 2.30.29.70; -; 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; PTHR12225; 1.
DR   Pfam; PF04683; Proteasom_Rpn13; 1.
DR   Pfam; PF16550; RPN13_C; 1.
DR   PROSITE; PS51916; DEUBAD; 1.
DR   PROSITE; PS51917; PRU; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..406
FT                   /note="Proteasomal ubiquitin receptor ADRM1"
FT                   /id="PRO_5000067932"
FT   DOMAIN          18..131
FT                   /note="Pru"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT   DOMAIN          277..390
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT   REGION          198..260
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        198..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  42367 MW;  CEADAE3260745B48 CRC64;
     MTTSGALFPS LVPGSRGSSS KYLVEFRAGK MSLKGSTVTP DKRKGLVYIQ QTDDSLIHFC
     WKDRTSGNVE DDLIIFPDDC EFKRVPQCTT GRVYVLKFKA GSKRLFFWMQ EPKTDKDEEH
     CRKVNEYLNN PPMPGALGGN ASGGHELSAL GGEGGLQSLL GNMSHNQLMQ LIGPTGLGGL
     GGLGALTGPG LASLLGSGGF PTSSSSSSSR SQSAAVTPSS TTSSTHVTPA PAVPAAASVT
     SPSPVPSSGS GTSSATSPTQ PIQLSDLQNI LATMNVPSGA GGQQVDLATV LTPEIMAPIL
     ANAEVQERLM PYLPSGESLP QTAEEIQNTL TSPQFQQALS MFSAALASGQ HGPLMSQFGL
     PAEAIDAANK GDVEAFAKAM QNSVKSDQKE GDSKDKKDEE EDMSLD