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ADRM1_CAEEL
ID   ADRM1_CAEEL             Reviewed;         374 AA.
AC   Q09289;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000305};
DE   AltName: Full=Proteasome non-ATPase regulatory particle-like protein 13 {ECO:0000312|WormBase:C56G2.7a};
GN   Name=rpn-13 {ECO:0000312|WormBase:C56G2.7a};
GN   ORFNames=C56G2.7 {ECO:0000312|WormBase:C56G2.7a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   INTERACTION WITH UBH-4.
RX   PubMed=23770237; DOI=10.1016/j.celrep.2013.05.012;
RA   Matilainen O., Arpalahti L., Rantanen V., Hautaniemi S., Holmberg C.I.;
RT   "Insulin/IGF-1 signaling regulates proteasome activity through the
RT   deubiquitinating enzyme UBH-4.";
RL   Cell Rep. 3:1980-1995(2013).
CC   -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC       the deubiquitinating activity associated with the 26S proteasome.
CC       {ECO:0000250|UniProtKB:Q16186}.
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 deubiquitinase ubh-4 (PubMed:23770237).
CC       {ECO:0000250|UniProtKB:Q16186, ECO:0000269|PubMed:23770237}.
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 rpn-2 and ubiquitin. Preferential binding to
CC       the proximal subunit of K48-linked diubiquitin allows ubh-4 access to
CC       the distal subunit. {ECO:0000250|UniProtKB:Q16186}.
CC   -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR   EMBL; BX284603; CCD66338.1; -; Genomic_DNA.
DR   RefSeq; NP_498387.2; NM_065986.6.
DR   AlphaFoldDB; Q09289; -.
DR   SMR; Q09289; -.
DR   BioGRID; 533206; 41.
DR   IntAct; Q09289; 5.
DR   STRING; 6239.C56G2.7; -.
DR   iPTMnet; Q09289; -.
DR   EPD; Q09289; -.
DR   PaxDb; Q09289; -.
DR   PeptideAtlas; Q09289; -.
DR   EnsemblMetazoa; C56G2.7a.1; C56G2.7a.1; WBGene00016981.
DR   GeneID; 3565888; -.
DR   KEGG; cel:CELE_C56G2.7; -.
DR   UCSC; C56G2.7; c. elegans.
DR   CTD; 3565888; -.
DR   WormBase; C56G2.7a; CE30640; WBGene00016981; rpn-13.
DR   eggNOG; KOG3037; Eukaryota.
DR   GeneTree; ENSGT00390000013839; -.
DR   HOGENOM; CLU_041798_0_0_1; -.
DR   InParanoid; Q09289; -.
DR   OMA; SNQRHFF; -.
DR   PhylomeDB; Q09289; -.
DR   Reactome; R-CEL-5689603; UCH proteinases.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   PRO; PR:Q09289; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00016981; Expressed in adult organism and 4 other tissues.
DR   ExpressionAtlas; Q09289; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR   GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
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   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Proteasomal ubiquitin receptor ADRM1 homolog"
FT                   /id="PRO_0000065257"
FT   DOMAIN          13..131
FT                   /note="Pru"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT   DOMAIN          239..346
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT   REGION          126..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  39773 MW;  FD37CFC6EB991044 CRC64;
     MAAMFSNTRS VASSSGHIVE FKAGRSRLEA GSGDTMRKVV AEPKKGLVFI KQSNDMLIHF
     CWKDRETGAV VDDLIIFPDD AEFKAVPGCP DGKVYMLKFK SGDMKLFWIQ DSTPDVDKDL
     VKKVTDALNK PPTSRPAASR SAGSNANTDR QSAGGSLISS SDMNAPLGGI DQGQLMSLIQ
     SLQGGNSDTL PISSVPRGED ASSEADCEPS TNAAEEGSSN PLSLNNPAIQ QIFNNLGRSQ
     KKEVAVSLAT ALSNETVAEV ARNHAEELAP HLPTSDDPAR ELSETVRTPQ FRQAADTLGH
     ALQTGQLGPV VAQFGMDEAT VGSANQGDIR GFAANLTKAE GGEDAAKTQN SDDDATREPE
     PKRNRPDNED MDVD
 
 
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