ADRM1_DROME
ID ADRM1_DROME Reviewed; 389 AA.
AC Q7K2G1; B7YZG7; B7YZG8; Q86NT4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog;
DE AltName: Full=Regulatory particle non-ATPase 13 protein;
DE AltName: Full=p42E;
GN Name=Rpn13; ORFNames=CG13349;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Berkeley; TISSUE=Head, and Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=11301252; DOI=10.1016/s0960-9822(01)00124-5;
RA Kraut R., Menon K., Zinn K.;
RT "A gain-of-function screen for genes controlling motor axon guidance and
RT synaptogenesis in Drosophila.";
RL Curr. Biol. 11:417-430(2001).
RN [5]
RP INTERACTION WITH 26S PROTEASOME, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14652013; DOI=10.1016/j.bbrc.2003.11.074;
RA Suemegi M., Hunyadi-Gulyas E., Medzihradszky K.F., Udvardy A.;
RT "26S proteasome subunits are O-linked N-acetylglucosamine-modified in
RT Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 312:1284-1289(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-185; SER-217; SER-218
RP AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-196; THR-205; SER-207;
RP SER-217; SER-219 AND THR-367, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC the deubiquitinating activity associated with the 26S proteasome (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the 26S proteasome.
CC {ECO:0000269|PubMed:14652013}.
CC -!- INTERACTION:
CC Q7K2G1; Q9V3I9: BG:DS07851.5; NbExp=3; IntAct=EBI-88589, EBI-115777;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A, B, F;
CC IsoId=Q7K2G1-1; Sequence=Displayed;
CC Name=2; Synonyms=D, E;
CC IsoId=Q7K2G1-2; Sequence=VSP_024972;
CC -!- DEVELOPMENTAL STAGE: In larvae, expressed in the central nervous
CC system. {ECO:0000269|PubMed:11301252}.
CC -!- DOMAIN: The PH domain mediates interactions with PSMD1 and ubiquitin.
CC Preferential binding to the proximal subunit of K48-linked diubiquitin
CC allows UCHL5 access to the distal subunit (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58312.1; -; Genomic_DNA.
DR EMBL; AE013599; AAG22269.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83116.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83117.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83118.1; -; Genomic_DNA.
DR EMBL; AY061027; AAL28575.1; -; mRNA.
DR EMBL; BT003652; AAO39656.1; -; mRNA.
DR RefSeq; NP_001137662.1; NM_001144190.2. [Q7K2G1-2]
DR RefSeq; NP_001137663.1; NM_001144191.2. [Q7K2G1-2]
DR RefSeq; NP_001137664.1; NM_001144192.2. [Q7K2G1-1]
DR RefSeq; NP_001286397.1; NM_001299468.1. [Q7K2G1-2]
DR RefSeq; NP_610917.1; NM_137073.3. [Q7K2G1-1]
DR RefSeq; NP_725346.1; NM_166025.2. [Q7K2G1-1]
DR AlphaFoldDB; Q7K2G1; -.
DR SMR; Q7K2G1; -.
DR BioGRID; 62299; 45.
DR IntAct; Q7K2G1; 12.
DR iPTMnet; Q7K2G1; -.
DR PRIDE; Q7K2G1; -.
DR DNASU; 36545; -.
DR EnsemblMetazoa; FBtr0087610; FBpp0086736; FBgn0033886. [Q7K2G1-1]
DR EnsemblMetazoa; FBtr0087611; FBpp0086737; FBgn0033886. [Q7K2G1-1]
DR EnsemblMetazoa; FBtr0114493; FBpp0112985; FBgn0033886. [Q7K2G1-2]
DR EnsemblMetazoa; FBtr0114494; FBpp0112986; FBgn0033886. [Q7K2G1-2]
DR EnsemblMetazoa; FBtr0114495; FBpp0112987; FBgn0033886. [Q7K2G1-1]
DR EnsemblMetazoa; FBtr0339958; FBpp0308980; FBgn0033886. [Q7K2G1-2]
DR GeneID; 36545; -.
DR KEGG; dme:Dmel_CG13349; -.
DR CTD; 36545; -.
DR FlyBase; FBgn0033886; Rpn13.
DR VEuPathDB; VectorBase:FBgn0033886; -.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; Q7K2G1; -.
DR OMA; SNQRHFF; -.
DR PhylomeDB; Q7K2G1; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR SignaLink; Q7K2G1; -.
DR BioGRID-ORCS; 36545; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36545; -.
DR PRO; PR:Q7K2G1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033886; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; Q7K2G1; baseline and differential.
DR Genevisible; Q7K2G1; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0000502; C:proteasome complex; IDA:FlyBase.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:FlyBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; ISS:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:FlyBase.
DR GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:FlyBase.
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 Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT CHAIN 1..389
FT /note="Proteasomal ubiquitin receptor ADRM1 homolog"
FT /id="PRO_0000286075"
FT DOMAIN 12..125
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 16..124
FT /note="PH"
FT DOMAIN 237..351
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 238
FT /note="P -> PGKNSTTSTTTASKSTGAYANPFQAYLSNLSPEHGA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_024972"
SQ SEQUENCE 389 AA; 42013 MW; 260F2383BF6C7BFF CRC64;
MFGRQSGLGS SSNSSNLVEF RAGRMNMVGK MVHPDPRKGL VYMTQSDDGL MHFCWKDRTS
GKVEDDLIVF PDDFEYKRVD QCKTGRVYVL KFKSSTRRMF FWMQEPKTDK DDEQCRRINE
LLNNPPSAHQ RGGGGSNDGD LQYMLNNMSQ QQLMQLFGGV GQMGGLSSLL GQMNSRTPSS
RNTSSSGGGG ASALQTPENV SVPRTPSAPS KSGSSRSSSN VNSQVGEGAG SSVDADAPGR
SLNIDLSTAL PGADAINQII ADPEHVKTLI VHLPESEDVD DDRKQQIKDN ITSPQFQQAL
AQFSSALQSA QLGPVIKQFE LSNEAVAAAF SGNLEDFVRA LEKSLPPGAT MGGKPSASEK
KASDPETPTS VARDENTDPA TEKQEEKQK
