GenomeNet

Database: UniProt
Entry: ADRM1_RAT
LinkDB: ADRM1_RAT
Original site: 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   18-SEP-2019, entry version 112.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   expresses 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat 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
CC       proteins. This complex plays a key role in the maintenance of
CC       protein homeostasis by removing misfolded or damaged proteins,
CC       which could impair cellular functions, and by removing proteins
CC       whose functions are no longer required. Therefore, the proteasome
CC       participates in numerous cellular processes, including cell cycle
CC       progression, apoptosis, or DNA damage repair. Within the complex,
CC       functions as a proteasomal ubiquitin receptor. Engages and thus
CC       activates 19S-associated deubiquitinases UCHL5 and PSMD14 during
CC       protein degradation. UCHL5 reversibly associate with the 19S
CC       regulatory particle whereas PSMD14 is an intrinsic subunit of the
CC       proteasome lid subcomplex. {ECO:0000250|UniProtKB:Q16186}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle
CC       complex. The 26S proteasome consists of a 20S core particle (CP)
CC       and two 19S regulatory subunits (RP). Interacts with the
CC       proteasomal scaffolding protein PSMD1. Interacts with
CC       deubiquitinase UCHL5; this interaction activates the auto-
CC       inhibited UCHL5 by deoligomerizing it. Interacts with UBQLN2 and
CC       ubiquitin. {ECO:0000250|UniProtKB:Q16186}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16186}.
CC       Nucleus {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
CC       binding to the proximal subunit of K48-linked diubiquitin allows
CC       UCHL5 access to the distal subunit.
CC       {ECO:0000250|UniProtKB:Q16186}.
CC   -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
CC   -!- CAUTION: Although initially described as a cell membrane
CC       glycoprotein, ADRM1 is intracellular and non-glycosylated, and has
CC       probably no direct role in cell adhesion. {ECO:0000305}.
DR   EMBL; AB032742; BAA92929.1; -; mRNA.
DR   EMBL; BC061773; AAH61773.1; -; mRNA.
DR   RefSeq; NP_113896.1; NM_031708.1.
DR   SMR; Q9JMB5; -.
DR   BioGrid; 249259; 2.
DR   IntAct; Q9JMB5; 1.
DR   STRING; 10116.ENSRNOP00000010087; -.
DR   iPTMnet; Q9JMB5; -.
DR   PhosphoSitePlus; Q9JMB5; -.
DR   jPOST; Q9JMB5; -.
DR   PaxDb; Q9JMB5; -.
DR   PRIDE; Q9JMB5; -.
DR   Ensembl; ENSRNOT00000091941; ENSRNOP00000074216; ENSRNOG00000055984.
DR   GeneID; 65138; -.
DR   KEGG; rno:65138; -.
DR   CTD; 11047; -.
DR   RGD; 69248; Adrm1.
DR   eggNOG; KOG3037; Eukaryota.
DR   eggNOG; ENOG410XSJJ; LUCA.
DR   GeneTree; ENSGT00390000013839; -.
DR   HOGENOM; HOG000005947; -.
DR   InParanoid; Q9JMB5; -.
DR   KO; K06691; -.
DR   OMA; HCRRINE; -.
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 10 organ(s), highest expression level in skeletal muscle tissue.
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; 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; 2.30.29.70; -; 1.
DR   Gene3D; 3.40.190.140; -; 1.
DR   InterPro; IPR006773; Rpn13/ADRM1.
DR   InterPro; IPR038633; Rpn13/ADRM1_sf.
DR   InterPro; IPR032368; RPN13_C.
DR   InterPro; IPR038108; RPN13_C_sf.
DR   PANTHER; PTHR12225; PTHR12225; 1.
DR   Pfam; PF04683; Proteasom_Rpn13; 1.
DR   Pfam; PF16550; RPN13_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q16186}.
FT   CHAIN         2    407       Proteasomal ubiquitin receptor ADRM1.
FT                                /FTId=PRO_0000020633.
FT   REGION       22    130       Pru (pleckstrin-like receptor for
FT                                ubiquitin) domain.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   REGION      362    407       Interaction with UCHL5. {ECO:0000250}.
FT   COMPBIAS    135    202       Gly-rich.
FT   COMPBIAS    193    257       Ser-rich.
FT   COMPBIAS    203    213       Poly-Ser.
FT   MOD_RES       2      2       N-acetylthreonine.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   MOD_RES      15     15       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   MOD_RES     140    140       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   MOD_RES     211    211       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   MOD_RES     217    217       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   MOD_RES     405    405       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CROSSLNK     34     34       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:Q16186}.
FT   CONFLICT     20     20       T -> I (in Ref. 1; BAA92929).
FT                                {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
//
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