DDI1_CAEEL
ID DDI1_CAEEL Reviewed; 389 AA.
AC Q17569;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein DDI1 homolog 1 {ECO:0000250|UniProtKB:Q8WTU0};
DE EC=3.4.23.- {ECO:0000305|PubMed:27528192};
GN Name=ddi-1 {ECO:0000303|PubMed:27528192, ECO:0000312|WormBase:C01G5.6};
GN ORFNames=C01G5.6 {ECO:0000312|WormBase:C01G5.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-244; LEU-245;
RP 261-ASP--GLY-263; CYS-277; GLY-293 AND LEU-334.
RX PubMed=27528192; DOI=10.7554/elife.17721;
RA Lehrbach N.J., Ruvkun G.;
RT "Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic
RT protease DDI-1.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Aspartic protease. Required for the cleavage and activation
CC of transcription factors such as isoform a of the transcription factor
CC skn-1, which in turn regulates the expression of proteasomal subunits
CC such as rpt-3. {ECO:0000269|PubMed:27528192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27528192}. Nucleus
CC {ECO:0000269|PubMed:27528192}. Note=Mainly localizes to the nucleus
CC during proteasomal disruption. {ECO:0000269|PubMed:27528192}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues.
CC {ECO:0000269|PubMed:27528192}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to low doses of bortezomib
CC which causes proteasome dysfunction. Double knockout with proteasomal
CC subunit pbs-5 or with rpt-5 knockdown results in failed expression of
CC the proteasomal subunit rpt-3. Double knockout with pbs-5 also results
CC in the occasional mis-localization of the transcription factor skn-1a
CC within gut nuclei. {ECO:0000269|PubMed:27528192}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR EMBL; BX284604; CCD62447.1; -; Genomic_DNA.
DR PIR; T30993; T30993.
DR RefSeq; NP_500992.1; NM_068591.3.
DR AlphaFoldDB; Q17569; -.
DR SMR; Q17569; -.
DR IntAct; Q17569; 2.
DR MINT; Q17569; -.
DR STRING; 6239.C01G5.6; -.
DR MEROPS; A28.A02; -.
DR EPD; Q17569; -.
DR PaxDb; Q17569; -.
DR PeptideAtlas; Q17569; -.
DR EnsemblMetazoa; C01G5.6.1; C01G5.6.1; WBGene00015308.
DR GeneID; 177413; -.
DR KEGG; cel:CELE_C01G5.6; -.
DR UCSC; C01G5.6; c. elegans.
DR CTD; 177413; -.
DR WormBase; C01G5.6; CE23513; WBGene00015308; ddi-1.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_726138_0_0_1; -.
DR InParanoid; Q17569; -.
DR OMA; MARREMD; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q17569; -.
DR PRO; PR:Q17569; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015308; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IMP:WormBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05479; RP_DDI; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Reference proteome.
FT CHAIN 1..389
FT /note="Protein DDI1 homolog 1"
FT /id="PRO_0000442727"
FT REGION 109..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /evidence="ECO:0000305"
FT MUTAGEN 244
FT /note="M->I: In mg543; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
FT MUTAGEN 245
FT /note="L->F: In mg563; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
FT MUTAGEN 261..263
FT /note="DSG->NSA: In mg572; fails to cleave isoform a of the
FT transcription factor skn-1 (skn-1a). Defective expression
FT of the proteasomal subunit rpt-3 in a pbs-5 (proteasomal
FT subunit) mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
FT MUTAGEN 277
FT /note="C->S: In mg555; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
FT MUTAGEN 293
FT /note="G->R: In mg544; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
FT MUTAGEN 334
FT /note="L->F: In mg557; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
SQ SEQUENCE 389 AA; 43716 MW; CC148E3255C06E40 CRC64;
MSFQVSVAVN DGPFQKKSVT PNTTIGDLNN DAILIWKDTA IVYDISDESK NFGPTVTLEQ
LGVTQISMVY IYTTAFPCPS GDLRSIVPAQ VRLISQFASA ASSIFNGQSS SSAQSAQRTR
RVEQDDEGEK SMFSRKLLDS PATFKALSEN MFFRLKNEPH KLGYGLPELV ERFLAKKDMT
YKEFEQMFRS YVEEEVHKEE IIKNNPNSAE AKMFLEAKRN KELIDEQYLH SMTHHPEDMI
AVTMLYINLT INGVPVKAFI DSGAQKSIMS MACAERCGLN GLIDRRFQSM ARGVGGTEKI
EGKIHLCDVK VEDAHFSCPF EVMARREMDL LIGLNVLRKH GCCINLKTSR LEFGNGTTTP
FLQSNEIDSH LKEIMALPEE EMQFEDGST
