DDI2_DANRE
ID DDI2_DANRE Reviewed; 411 AA.
AC Q6TH22; Q7SY47;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein DDI1 homolog 2 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q5TDH0};
GN Name=ddi2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6TH22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6TH22-2; Sequence=VSP_025299;
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
CC -!- CAUTION: Although this protein contains the conserved Asp-262 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; AY398334; AAQ97767.1; -; mRNA.
DR EMBL; BC055129; AAH55129.1; -; mRNA.
DR RefSeq; NP_938189.2; NM_198375.2. [Q6TH22-2]
DR RefSeq; XP_017211936.1; XM_017356447.1.
DR AlphaFoldDB; Q6TH22; -.
DR SMR; Q6TH22; -.
DR STRING; 7955.ENSDARP00000129420; -.
DR MEROPS; A28.003; -.
DR PaxDb; Q6TH22; -.
DR PRIDE; Q6TH22; -.
DR Ensembl; ENSDART00000017859; ENSDARP00000011673; ENSDARG00000006477. [Q6TH22-2]
DR Ensembl; ENSDART00000155928; ENSDARP00000129420; ENSDARG00000006477. [Q6TH22-1]
DR GeneID; 386644; -.
DR KEGG; dre:386644; -.
DR CTD; 84301; -.
DR ZFIN; ZDB-GENE-031030-15; ddi2.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_020435_1_0_1; -.
DR InParanoid; Q6TH22; -.
DR OMA; IHMVQIQ; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q6TH22; -.
DR TreeFam; TF333421; -.
DR PRO; PR:Q6TH22; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000006477; Expressed in mature ovarian follicle and 21 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 Alternative splicing; Aspartyl protease; Chromosome; Cytoplasm; Hydrolase;
KW Protease; Reference proteome.
FT CHAIN 1..411
FT /note="Protein DDI1 homolog 2"
FT /id="PRO_0000287092"
FT DOMAIN 1..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 82..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 387..406
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /evidence="ECO:0000305"
FT VAR_SEQ 406..411
FT /note="GKMHDM -> AGQN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025299"
FT CONFLICT 137
FT /note="V -> I (in Ref. 2; AAH55129)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="P -> S (in Ref. 2; AAH55129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45596 MW; 17099AB0A03E1B0E CRC64;
MLLTVFCAPR DRSETTFALD VSPELELRDF LALCELESGI PAGEIQIIYA EQPLQDPTRA
LGNYGLKDGD VLVLRQAERL RAPPQPTVPG LPRIDFSSIA VPGTSSGQNR NRPQQAQRPS
TTQPPPPQAT TSPGSGVSPQ GLDNPALLRD MLLANPHELS LLKERNPPLA EALLSGDLER
FTKVLMEQQQ DRARRDQERI KLLTADPFDL DAQAKIEEEI RQHNIEENMT IAMEEAPESF
GQVVMLYINC KVNGHPVKAF VDSGAQMTIM SQACAERCNI MRLVDRRWAG IAKGVGTQKI
IGRVHLAQVQ IEGDFLPCSF SILEDQPMDM LLGLDMLKRH QCSIDLKKNV LLIGTTGTET
RFLPEAELPE CARLAYGPEG REEPRPDEIA DRELAEAIQR SVQDSGKMHD M
