ADRM1_MOUSE
ID ADRM1_MOUSE Reviewed; 407 AA.
AC Q9JKV1; Q3UKZ8; Q8BPH8; Q922A7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10919708; DOI=10.1023/a:1006790912877;
RA Simins A.B., Weighardt H., Weidner K.M., Weidle U.H., Holzmann B.;
RT "Functional cloning of ARM-1, an adhesion-regulating molecule upregulated
RT in metastatic tumor cells.";
RL Clin. Exp. Metastasis 17:641-648(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP SUBCELLULAR LOCATION, AND LACK OF GLYCOSYLATION.
RX PubMed=15819879; DOI=10.1111/j.1742-4658.2005.04613.x;
RA Lamerant N., Kieda C.;
RT "Adhesion properties of adhesion-regulating molecule 1 protein on
RT endothelial cells.";
RL FEBS J. 272:1833-1844(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
RA Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
RT "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
RT deubiquitinating enzyme, UCH37.";
RL EMBO J. 25:5742-5753(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16815440; DOI=10.1016/j.jmb.2006.06.011;
RA Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K., Johnsen A.H.,
RA Hendil K.B., Hartmann-Petersen R.;
RT "Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-
RT associated factor.";
RL J. Mol. Biol. 360:1043-1052(2006).
RN [8]
RP STRUCTURE BY NMR OF 22-130, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-150,
RP FUNCTION, REGION, AND INTERACTION WITH UBIQUITIN; UCHL5 AND PSMD1.
RX PubMed=18497827; DOI=10.1038/nature06924;
RA Schreiner P., Chen X., Husnjak K., Randles L., Zhang N., Elsasser S.,
RA Finley D., Dikic I., Walters K.J., Groll M.;
RT "Ubiquitin docking at the proteasome through a novel pleckstrin-homology
RT domain interaction.";
RL Nature 453:548-552(2008).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins
CC (PubMed:18497827). This complex plays a key role in the maintenance of
CC protein homeostasis by removing misfolded or damaged proteins, which
CC could impair cellular functions, and by removing proteins whose
CC functions are no longer required (PubMed:18497827). Therefore, the
CC proteasome participates in numerous cellular processes, including cell
CC cycle progression, apoptosis, or DNA damage repair (PubMed:18497827).
CC Within the complex, functions as a proteasomal ubiquitin receptor
CC (PubMed:18497827). Engages and thus activates 19S-associated
CC deubiquitinases UCHL5 and PSMD14 during protein degradation (By
CC similarity). UCHL5 reversibly associate with the 19S regulatory
CC particle whereas PSMD14 is an intrinsic subunit of the proteasome lid
CC subcomplex (By similarity). {ECO:0000250|UniProtKB:Q16186,
CC ECO:0000269|PubMed:18497827}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC (By similarity). The 26S proteasome consists of a 20S core particle
CC (CP) and two 19S regulatory subunits (RP) (By similarity). Interacts
CC with the proteasomal scaffolding protein PSMD1 (PubMed:18497827).
CC Interacts with deubiquitinase UCHL5; this interaction activates the
CC auto-inhibited UCHL5 by deoligomerizing it (PubMed:18497827). Interacts
CC with UBQLN2 and ubiquitin (PubMed:18497827).
CC {ECO:0000250|UniProtKB:Q16186, ECO:0000269|PubMed:18497827}.
CC -!- INTERACTION:
CC Q9JKV1; Q99460-1: PSMD1; Xeno; NbExp=2; IntAct=EBI-8762776, EBI-15703973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15819879}. Nucleus
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- TISSUE SPECIFICITY: Present in all tissues examined (at protein level).
CC {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:17139257}.
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:0000269|PubMed:18497827}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:15819879}.
CC -!- PTM: Not O-glycosylated. {ECO:0000269|PubMed:15819879}.
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; AF225959; AAF33401.1; -; mRNA.
DR EMBL; AK075674; BAC35889.1; -; mRNA.
DR EMBL; AK145474; BAE26457.1; -; mRNA.
DR EMBL; AK145792; BAE26653.1; -; mRNA.
DR EMBL; AK166878; BAE39089.1; -; mRNA.
DR EMBL; AL663027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008974; AAH08974.1; -; mRNA.
DR EMBL; BC031517; AAH31517.1; -; mRNA.
DR CCDS; CCDS17171.1; -.
DR RefSeq; NP_062796.2; NM_019822.3.
DR PDB; 2R2Y; X-ray; 1.70 A; A=2-150.
DR PDB; 2Z59; NMR; -; A=22-130.
DR PDBsum; 2R2Y; -.
DR PDBsum; 2Z59; -.
DR AlphaFoldDB; Q9JKV1; -.
DR SMR; Q9JKV1; -.
DR BioGRID; 207978; 63.
DR DIP; DIP-60625N; -.
DR IntAct; Q9JKV1; 19.
DR STRING; 10090.ENSMUSP00000050076; -.
DR iPTMnet; Q9JKV1; -.
DR PhosphoSitePlus; Q9JKV1; -.
DR EPD; Q9JKV1; -.
DR jPOST; Q9JKV1; -.
DR MaxQB; Q9JKV1; -.
DR PaxDb; Q9JKV1; -.
DR PeptideAtlas; Q9JKV1; -.
DR PRIDE; Q9JKV1; -.
DR DNASU; 56436; -.
DR Ensembl; ENSMUST00000061437; ENSMUSP00000050076; ENSMUSG00000039041.
DR GeneID; 56436; -.
DR KEGG; mmu:56436; -.
DR UCSC; uc008oin.1; mouse.
DR CTD; 11047; -.
DR MGI; MGI:1929289; Adrm1.
DR VEuPathDB; HostDB:ENSMUSG00000039041; -.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; Q9JKV1; -.
DR OMA; SNQRHFF; -.
DR PhylomeDB; Q9JKV1; -.
DR TreeFam; TF313410; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 56436; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Adrm1; mouse.
DR EvolutionaryTrace; Q9JKV1; -.
DR PRO; PR:Q9JKV1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JKV1; protein.
DR Bgee; ENSMUSG00000039041; Expressed in hindlimb stylopod muscle and 83 other tissues.
DR Genevisible; Q9JKV1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0061133; F:endopeptidase activator activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0070628; F:proteasome binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IMP:BHF-UCL.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IMP:BHF-UCL.
DR GO; GO:0048477; P:oogenesis; IMP:BHF-UCL.
DR GO; GO:0001541; P:ovarian follicle development; IMP:BHF-UCL.
DR GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043248; P:proteasome assembly; ISO:MGI.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:BHF-UCL.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:BHF-UCL.
DR GO; GO:0060009; P:Sertoli cell development; IMP:BHF-UCL.
DR GO; GO:0007286; P:spermatid development; IMP:BHF-UCL.
DR GO; GO:0048538; P:thymus development; IMP:BHF-UCL.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
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 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; 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_0000020632"
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265,
FT ECO:0000269|PubMed:18497827"
FT DOMAIN 277..391
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
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: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"
FT CONFLICT 109
FT /note="M -> I (in Ref. 2; BAC35889)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="L -> I (in Ref. 2; BAE26653)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="R -> S (in Ref. 2; BAC35889)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="F -> I (in Ref. 1; AAF33401)"
FT /evidence="ECO:0000305"
FT STRAND 24..34
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2R2Y"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2R2Y"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2R2Y"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2R2Y"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:2R2Y"
SQ SEQUENCE 407 AA; 42060 MW; 210AFDF7379C962D CRC64;
MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNECLNN PPMPGSLGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSSGP PASSSSSSSR SQSAAVTPSS STSSARATPA PSAPAAASAT
SPSPAPSSGN GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGSQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE EEDMSLD
