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   03-AUG-2022, entry version 84.
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   GeneID; 379186; -.
DR   CTD; 379186; -.
DR   Xenbase; XB-GENE-6073074; ddi2.L.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 379186; Expressed in neurula embryo and 19 other 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; -; 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   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   SUPFAM; SSF54236; SSF54236; 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