ADRM1_BOVIN
ID ADRM1_BOVIN Reviewed; 407 AA.
AC A1L5A6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE AltName: Full=Rpn13 homolog;
GN Name=ADRM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. Engages and activates 19S-associated deubiquitinases UCHL5
CC and PSMD14 during protein degradation. UCHL5 reversibly associate with
CC the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of
CC the proteasome lid subcomplex. {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). 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:0000250|UniProtKB:Q16186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16186}. Nucleus
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- DOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain
CC mediates interactions with PSMD1 and ubiquitin. Preferential binding to
CC the proximal subunit of 'Lys-48'-linked diubiquitin allows UCHL5 access
CC to the distal subunit. {ECO:0000250|UniProtKB:Q16186}.
CC -!- PTM: Ubiquitinated by UBE3C in response to proteotoxic stress.
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR EMBL; BT029893; ABM21559.1; -; mRNA.
DR RefSeq; NP_001073751.1; NM_001080282.1.
DR AlphaFoldDB; A1L5A6; -.
DR SMR; A1L5A6; -.
DR STRING; 9913.ENSBTAP00000003974; -.
DR PaxDb; A1L5A6; -.
DR PeptideAtlas; A1L5A6; -.
DR PRIDE; A1L5A6; -.
DR Ensembl; ENSBTAT00000003974; ENSBTAP00000003974; ENSBTAG00000003058.
DR GeneID; 519729; -.
DR KEGG; bta:519729; -.
DR CTD; 11047; -.
DR VEuPathDB; HostDB:ENSBTAG00000003058; -.
DR VGNC; VGNC:25699; ADRM1.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; A1L5A6; -.
DR OMA; SNQRHFF; -.
DR OrthoDB; 1479349at2759; -.
DR TreeFam; TF313410; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000003058; Expressed in spermatid and 105 other tissues.
DR ExpressionAtlas; A1L5A6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0002020; F:protease binding; IEA:Ensembl.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
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 Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT CHAIN 2..407
FT /note="Proteasomal ubiquitin receptor ADRM1"
FT /id="PRO_0000286070"
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 277..391
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 2..132
FT /note="Interaction with PSMD1"
FT /evidence="ECO:0000250"
FT REGION 196..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..407
FT /note="Interaction with UCHL5"
FT /evidence="ECO:0000250"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB5"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
SQ SEQUENCE 407 AA; 41955 MW; 622F17326AD66E64 CRC64;
MTTSGALFPS LVPGSRGSSN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNEYLNN PPMPGALGAS GSGGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSGGP PASSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT
SPSPAPSSGD GASTAASPAQ PIQLSDLQSI LATMSVPAGP GGGQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNSASPEQQ EGDGKDKKDE EEDMSLD
