ID   DDI1_MOUSE              Reviewed;         408 AA.
AC   Q9DAF3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Protein DDI1 homolog 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=Ddi1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   STRUCTURE BY NMR OF 1-89.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the ubiquitin-like domain from mouse hypothetical
RT   1700011N24Rik protein.";
RL   Submitted (MAY-2004) to the PDB data bank.
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}.
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DR   EMBL; AK005882; BAB24297.1; -; mRNA.
DR   CCDS; CCDS40527.1; -.
DR   RefSeq; NP_082218.1; NM_027942.1.
DR   PDB; 1V5O; NMR; -; A=1-89.
DR   PDBsum; 1V5O; -.
DR   AlphaFoldDB; Q9DAF3; -.
DR   SMR; Q9DAF3; -.
DR   STRING; 10090.ENSMUSP00000053223; -.
DR   MEROPS; A28.A01; -.
DR   iPTMnet; Q9DAF3; -.
DR   PhosphoSitePlus; Q9DAF3; -.
DR   MaxQB; Q9DAF3; -.
DR   PaxDb; Q9DAF3; -.
DR   PeptideAtlas; Q9DAF3; -.
DR   PRIDE; Q9DAF3; -.
DR   ProteomicsDB; 279846; -.
DR   Antibodypedia; 31840; 65 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000051706; ENSMUSP00000053223; ENSMUSG00000047619.
DR   GeneID; 71829; -.
DR   KEGG; mmu:71829; -.
DR   UCSC; uc009oca.1; mouse.
DR   CTD; 414301; -.
DR   MGI; MGI:1919079; Ddi1.
DR   VEuPathDB; HostDB:ENSMUSG00000047619; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   GeneTree; ENSGT00950000182999; -.
DR   HOGENOM; CLU_020435_1_0_1; -.
DR   InParanoid; Q9DAF3; -.
DR   OMA; EQPMDIL; -.
DR   OrthoDB; 817208at2759; -.
DR   PhylomeDB; Q9DAF3; -.
DR   TreeFam; TF333421; -.
DR   BioGRID-ORCS; 71829; 2 hits in 72 CRISPR screens.
DR   EvolutionaryTrace; Q9DAF3; -.
DR   PRO; PR:Q9DAF3; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9DAF3; protein.
DR   Bgee; ENSMUSG00000047619; Expressed in seminiferous tubule of testis and 16 other tissues.
DR   Genevisible; Q9DAF3; MM.
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   3D-structure; Aspartyl protease; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..408
FT                   /note="Protein DDI1 homolog 1"
FT                   /id="PRO_0000287088"
FT   DOMAIN          1..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          82..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        111..125
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000305"
FT   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   TURN            9..12
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:1V5O"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:1V5O"
SQ   SEQUENCE   408 AA;  45713 MW;  56A496D962DC878C CRC64;
     MLITVYCVRR DLTEVTFSLQ VNPDFELSNF RVLCELESGV PAEEAQIVYM EQLLTDDHCS
     LGSYGLKDGD MVVLLQKDNV GLRTPGRTPN HPRADFTGSG SAVPGTSSSR HPHQHQHHYH
     HHQRIPSTQQ AHGLASGENM TFAQELDSPA LIRSMLLSNP HDLSLLKERN PALAEALLSG
     NLETFSQVLM EQQRERTLRE QEMFRLYSTN PFDQETQARI EEEIRQQNIE ENMNIAMEEA
     PESFGQVAML YINCKVNGHP LKAFVDSGAQ MTIMSQACAE RCNIMRLVDR RWGGVAKGVG
     TQRIMGRVHL AQIQIEGDFL QCSFSILEEQ PMDILLGLDM LRRHQCSIDL KKNVLVIGTT
     GSQTHFLPEG ELPLCAKLLS GTVQEESSDR EVGGTIKHPV KGPGRKKH