ID   DDI1_RAT                Reviewed;         408 AA.
AC   A0JPP7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein DDI1 homolog 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=Ddi1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Probable aspartic protease (By similarity). Seems to act as a
CC       proteasomal shuttle which links the proteasome and replication fork
CC       proteins like RTF2. Required, with DDI2, for cellular survival
CC       following replication stress. Together or redudantly with DDI2, removes
CC       RTF2 from stalled forks to allow cell cycle progression after
CC       replication stress and maintains genome integrity (By similarity).
CC       {ECO:0000250|UniProtKB:I7HUG0, ECO:0000250|UniProtKB:Q8WTU0}.
CC   -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC127531; AAI27532.1; -; mRNA.
DR   RefSeq; NP_001078944.1; NM_001085475.1.
DR   AlphaFoldDB; A0JPP7; -.
DR   SMR; A0JPP7; -.
DR   BioGRID; 266267; 1.
DR   MEROPS; A28.A01; -.
DR   PhosphoSitePlus; A0JPP7; -.
DR   PeptideAtlas; A0JPP7; -.
DR   PRIDE; A0JPP7; -.
DR   Ensembl; ENSRNOT00000039868; ENSRNOP00000091127; ENSRNOG00000022081.
DR   GeneID; 367012; -.
DR   KEGG; rno:367012; -.
DR   UCSC; RGD:1559430; rat.
DR   CTD; 414301; -.
DR   RGD; 1559430; Ddi1.
DR   GeneTree; ENSGT00950000182999; -.
DR   InParanoid; A0JPP7; -.
DR   OrthoDB; 817208at2759; -.
DR   PhylomeDB; A0JPP7; -.
DR   TreeFam; TF333421; -.
DR   PRO; PR:A0JPP7; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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: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   1: Evidence at protein level;
KW   Aspartyl protease; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..408
FT                   /note="Protein DDI1 homolog 1"
FT                   /id="PRO_0000287089"
FT   DOMAIN          1..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          77..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  45451 MW;  3A1C2E8FB1AF437C CRC64;
     MLITVYCVRR DLTEVTFSLQ VNPDFELSNF RVLCELESGV PAEEAQIVYM EQLLTDDHCS
     LGSYGLKDGD MVVLLQKDNV GPRPPGRAPN HPRTDFTGSG SAVPGTSSSR HPHPHQHHHH
     QHQRIPSTQQ AHGLASGENM AFAQDLNSPA LIRSMLLSNP HDLSLLKERN PALAEALLSG
     NLETFSQVLV EQQRERAMRE QEMFRLYSAD PFDQETQARI EEEIRQQNIE ENMNIAMEEA
     PESFGQVAML YINCKVNGHP LKAFVDSGAQ MTIMSQACAE RCNIMRLVDR RWAGVAKGVG
     TQRIMGRVHL AQIQIEGDFL QCSFSILEEQ PMDILLGLDM LRRHQCSIDL KKNVLVIGTT
     GSQTHFLPEG ELPLCAKLLS GAVQEDSSDK EVAGSIKHPV KGPGRKKH