ADRM1_DANRE
ID ADRM1_DANRE Reviewed; 410 AA.
AC Q6NZ09;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1;
GN Name=adrm1b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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; BC066391; AAH66391.1; -; mRNA.
DR RefSeq; XP_005162020.1; XM_005161963.3.
DR AlphaFoldDB; Q6NZ09; -.
DR SMR; Q6NZ09; -.
DR STRING; 7955.ENSDARP00000075874; -.
DR iPTMnet; Q6NZ09; -.
DR PaxDb; Q6NZ09; -.
DR Ensembl; ENSDART00000180014; ENSDARP00000150387; ENSDARG00000058560.
DR ZFIN; ZDB-GENE-040426-905; adrm1.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR InParanoid; Q6NZ09; -.
DR Reactome; R-DRE-5689603; UCH proteinases.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR PRO; PR:Q6NZ09; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000058560; Expressed in muscle tissue and 23 other tissues.
DR ExpressionAtlas; Q6NZ09; baseline and differential.
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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..410
FT /note="Proteasomal ubiquitin receptor ADRM1"
FT /id="PRO_0000286071"
FT DOMAIN 17..130
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 281..395
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 191..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 410 AA; 42596 MW; 0DF487D721BDF6A7 CRC64;
MSSGALFPSL VSGSRSSSSK YLVEFRAGKM TLKGSTVTPD KRKGTVYIQQ TDDSLIHFCW
KDRTSGNVED DLIIFPDDCE FKRVNQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDDEYC
RKVNEYLNNP PMPGALGSGG GGGHELSALG EGGLQSLLGN MSHNQLMQLI GPTGLGGLGA
LAGPGLASLL GSGGPATSSS TSSSRSQSAA ATPSSGSAAR LSSTQAPTTP VTPAATSSGS
PTVTPTTPAA QTPSLPAGPA SSTQPIQLSD LQSILATMNV PAMPTEGSGV DLASVLTPDV
MAPILANPEV QQRLLPYLPS GESLPQSAEE IQNTLTSPQF QQAMSMFSSA LASGQLGPLM
NQFGLPSEAV DAANKGDVEA FAKAMEGSDS KTDDGDSKDK KDDDEDMSLD
