ID DDI2_XENLA Reviewed; 393 AA.
AC Q7ZYA7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Protein DDI1 homolog 2 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q5TDH0};
GN Name=ddi2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Aspartic protease that mediates the cleavage of NFE2L1/NRF1
CC at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the
CC endoplasmic reticulum membrane. Ubiquitination of NFE2L1/NRF1 is a
CC prerequisite for cleavage, suggesting that DDI2 specifically recognizes
CC and binds ubiquitinated NFE2L1/NRF1. Seems to act as a proteasomal
CC shuttle which links the proteasome and replication fork proteins like
CC RTF2. Required for cellular survival following replication stress.
CC {ECO:0000250|UniProtKB:Q5TDH0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5TDH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5TDH0}. Chromosome
CC {ECO:0000250|UniProtKB:Q5TDH0}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
CC -!- CAUTION: Although this protein contains the conserved Asp-246 that
CC functions as an active site, this protein does not have proteolytic
CC activity, and may therefore be catalytically inactive.
CC {ECO:0000250|UniProtKB:Q5TDH0}.
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DR EMBL; BC043869; AAH43869.1; -; mRNA.
DR RefSeq; NP_001079499.1; NM_001086030.1.
DR AlphaFoldDB; Q7ZYA7; -.
DR SMR; Q7ZYA7; -.
DR MEROPS; A28.003; -.
DR MaxQB; Q7ZYA7; -.
DR DNASU; 379186; -.
DR AGR; Xenbase:XB-GENE-6073074; -.
DR Xenbase; XB-GENE-6073074; ddi2.L.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 379186; Expressed in neurula embryo and 19 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0097752; P:regulation of DNA stability; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd01796; Ubl_Ddi1_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR033882; DDI1_N.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15397:SF3; DNA DAMAGE-INDUCIBLE 1 HOMOLOG 2; 1.
DR PANTHER; PTHR15397; SODIUM-GLUCOSE COTRANSPORTER REGULATORY PROTEIN -RELATED; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Chromosome; Cytoplasm; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..393
FT /note="Protein DDI1 homolog 2"
FT /id="PRO_0000287093"
FT DOMAIN 1..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 82..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 370..389
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 106..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43733 MW; AD1789173F2A34AE CRC64;
MLITVYCVRR DLSEITFSLE VDGDFELENF RALCELESGI PASDTLIVYA ERPLTDNQRS
LASYGLKDGD VVILRQKEAP ETRPAAPFPG LDFSTIAVPG ASSQPDPSQP QAPPPPPDTS
SFPQGLDNPA LLRQMLLANP HELSLLKERN PPLAEALLSG DLEKFTKVLQ EQQQERARRE
QERIRLYSAD PFDLDAQAKI EEDIRQHNIE ENMTIAMEEA PESFGQVVML YINCKVNGYP
VKAFVDSGAQ MTIMSQACAE RCHIMRLVDR RWAGIAKGVG TQKIIGRVHL AQVQIEGDFL
PCSFSILEEQ PMDMLLGLDM LKRHQCSIDL EKNVLVIGTT GTHTTFLPEG ELPECARLAY
GPGREEVPPE EIADRELAEV LQKSADEADQ QKP
//
