ID   DDI2_XENTR              Reviewed;         394 AA.
AC   Q497D6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, 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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2005) 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-247 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; BC100609; AAI00610.1; -; mRNA.
DR   RefSeq; NP_001029120.1; NM_001033948.1.
DR   AlphaFoldDB; Q497D6; -.
DR   SMR; Q497D6; -.
DR   MEROPS; A28.003; -.
DR   PaxDb; Q497D6; -.
DR   DNASU; 619368; -.
DR   GeneID; 619368; -.
DR   KEGG; xtr:619368; -.
DR   CTD; 84301; -.
DR   Xenbase; XB-GENE-6073016; ddi2.
DR   eggNOG; KOG0012; Eukaryota.
DR   InParanoid; Q497D6; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000013448; Expressed in neurula embryo and 12 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..394
FT                   /note="Protein DDI1 homolog 2"
FT                   /id="PRO_0000287094"
FT   DOMAIN          1..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          82..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           371..390
FT                   /note="Ubiquitin-binding"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        106..123
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  43898 MW;  E49D80D956A9F27C CRC64;
     MLITVYCVRR DLSEVTFSLE VDGDFELENF RALCELESGI PASETLIVYA ERPLTNNQRS
     LASYGLKDGD VVILRQRETP EARPAAPFPG LDFSTIAVPG SSSQPAPSQP QAPPPPPPDT
     SSFPQGLDNP ALLREMLLAN PHELSLLKER NPPLAEALLS GDLEKFTKVL LEQQQERARR
     EQERIRLYSA DPFDLEAQAK IEEDIRQQNI EENMTIAMEE APESFGQVVM LYINCKVNGY
     PVKAFVDSGA QMTIMSQACA ERCHIMRLVD RRWAGIAKGV GTQKIIGRVH LAQVQIEGDF
     LPCSFSILEE QPMDMLLGLD MLKRHQCSID LEKNVLVIGT TGTRTSFLPE GELPECARLA
     YGPGREEVRP EEIADRELAE VLQKSAEEAD QQKP