ID ADM1B_XENLA Reviewed; 404 AA.
AC Q7ZXD6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 09-APR-2025, entry version 75.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1-B;
GN Name=adrm1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) 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; BC045042; AAH45042.1; -; mRNA.
DR EMBL; BC106295; AAI06296.1; -; mRNA.
DR RefSeq; NP_001079594.1; NM_001086125.1.
DR RefSeq; XP_018089504.1; XM_018234015.1.
DR AlphaFoldDB; Q7ZXD6; -.
DR SMR; Q7ZXD6; -.
DR DNASU; 379281; -.
DR GeneID; 379281; -.
DR KEGG; xla:379281; -.
DR AGR; Xenbase:XB-GENE-865867; -.
DR CTD; 379281; -.
DR Xenbase; XB-GENE-865867; adrm1.L.
DR OMA; SNQRHFF; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379281; Expressed in muscle tissue and 20 other cell types or tissues.
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:0043248; P:proteasome assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..404
FT /note="Proteasomal ubiquitin receptor ADRM1-B"
FT /id="PRO_0000286073"
FT DOMAIN 17..130
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 278..390
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 128..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..247
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 42047 MW; 264BEF91A087A314 CRC64;
MSSGALFPSL VPGSRGSSSK YLVEFRAGKM SLKGSTVTPD KRKGLVYIQQ TDDSLIHFCW
KDRTSGSVDD DLIIFPDDCE FKRVSQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDEEHC
RKVNEYLNNP PMPGALGGSG SGSHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
GLGALTGPGL ASLLGSGGPT TSSSSSSSRS QSAAVTPSST TSSTRTTSAP VAPAAAPATT
PSPAVSSNDG ASAATSPTQA IQLSDLQNIL ATMNVPATGE GGQQVDLASV LTPEIMAPIL
ANAEVQERLM PYLPSGESLP QTADEIQNTL TSPQFQQALS MFSAALASGQ LGPLMSQFGL
PADAVDAANK GDIEAFAKAM QSTSSQKERE SSEKKEEEED MSLD
//
