ADRM1_RAT
ID ADRM1_RAT Reviewed; 407 AA.
AC Q9JMB5; Q6P795;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE AltName: Full=110 kDa cell membrane glycoprotein;
DE Short=Gp110;
DE AltName: Full=Adhesion-regulating molecule 1;
DE Short=ARM-1;
DE AltName: Full=Rpn13 homolog;
GN Name=Adrm1; Synonyms=Gp110;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=11018266; DOI=10.1016/s0167-4781(00)00204-9;
RA Nakane T., Inada Y., Itoh F., Chiba S.;
RT "Rat homologue of the human Mr 110000 antigen is the protein that expresses
RT widely in various tissues.";
RL Biochim. Biophys. Acta 1493:378-382(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Widely expressed.
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}.
CC -!- CAUTION: Although initially described as a cell membrane glycoprotein,
CC ADRM1 is intracellular and non-glycosylated, and has probably no direct
CC role in cell adhesion. {ECO:0000305}.
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DR EMBL; AB032742; BAA92929.1; -; mRNA.
DR EMBL; BC061773; AAH61773.1; -; mRNA.
DR RefSeq; NP_113896.1; NM_031708.1.
DR AlphaFoldDB; Q9JMB5; -.
DR SMR; Q9JMB5; -.
DR BioGRID; 249259; 3.
DR IntAct; Q9JMB5; 1.
DR STRING; 10116.ENSRNOP00000010087; -.
DR iPTMnet; Q9JMB5; -.
DR PhosphoSitePlus; Q9JMB5; -.
DR jPOST; Q9JMB5; -.
DR PaxDb; Q9JMB5; -.
DR PRIDE; Q9JMB5; -.
DR GeneID; 65138; -.
DR KEGG; rno:65138; -.
DR CTD; 11047; -.
DR RGD; 69248; Adrm1.
DR VEuPathDB; HostDB:ENSRNOG00000055984; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; Q9JMB5; -.
DR OMA; SNQRHFF; -.
DR OrthoDB; 1479349at2759; -.
DR PhylomeDB; Q9JMB5; -.
DR TreeFam; TF313410; -.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9JMB5; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000055984; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q9JMB5; RN.
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; ISO:RGD.
DR GO; GO:0070628; F:proteasome binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; ISO:RGD.
DR GO; GO:0048477; P:oogenesis; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
DR GO; GO:0060009; P:Sertoli cell development; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:RGD.
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 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_0000020633"
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 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..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 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:0007744|PubMed:22673903"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT CONFLICT 20
FT /note="T -> I (in Ref. 1; BAA92929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 42102 MW; 811BFF38EFDE5F90 CRC64;
MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNECLNN PPMPGTLGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSSGP PASSSSSSSR SQSAAVTPSS TTSSARATPA PSAPAAASAT
SPSPAPSSGN GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGSQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE EEDMSLD
