DDI1_ARATH
ID DDI1_ARATH Reviewed; 414 AA.
AC Q1EBV4; A0A178VJ92; Q8LF25; Q9LTU5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein DNA-DAMAGE INDUCIBLE 1 {ECO:0000303|PubMed:21764993};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
GN Name=DDI1 {ECO:0000303|PubMed:21764993};
GN OrderedLocusNames=At3g13235 {ECO:0000312|Araport:AT3G13235};
GN ORFNames=MDC11.6 {ECO:0000312|EMBL:BAB02792.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF 386-LEU-GLY-387.
RX PubMed=21764993; DOI=10.1105/tpc.111.086702;
RA Lin Y.-L., Sung S.-C., Tsai H.-L., Yu T.-T., Radjacommare R., Usharani R.,
RA Fatimababy A.S., Lin H.-Y., Wang Y.-Y., Fu H.;
RT "The defective proteasome but not substrate recognition function is
RT responsible for the null phenotypes of the Arabidopsis proteasome subunit
RT RPN10.";
RL Plant Cell 23:2754-2773(2011).
CC -!- FUNCTION: Receptor of ubiquitinated protein targeted to
CC ubiquitin/proteasome-mediated proteolysis (UPP). Relatively weak
CC affinity for both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains with a
CC slight preference for 'Lys-48-'linked chains of three or more ubiquitin
CC units. {ECO:0000269|PubMed:21764993}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5TDH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5TDH0}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02792.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024034; BAB02792.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75323.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75325.1; -; Genomic_DNA.
DR EMBL; BT025980; ABG25069.1; -; mRNA.
DR EMBL; AK226800; BAE98897.1; -; mRNA.
DR EMBL; AY085083; AAM61638.1; -; mRNA.
DR RefSeq; NP_001189877.1; NM_001202948.2.
DR RefSeq; NP_566451.1; NM_112168.5.
DR AlphaFoldDB; Q1EBV4; -.
DR SMR; Q1EBV4; -.
DR STRING; 3702.AT3G13235.1; -.
DR MEROPS; A28.A03; -.
DR iPTMnet; Q1EBV4; -.
DR PaxDb; Q1EBV4; -.
DR PRIDE; Q1EBV4; -.
DR ProteomicsDB; 224692; -.
DR EnsemblPlants; AT3G13235.1; AT3G13235.1; AT3G13235.
DR EnsemblPlants; AT3G13235.2; AT3G13235.2; AT3G13235.
DR GeneID; 820522; -.
DR Gramene; AT3G13235.1; AT3G13235.1; AT3G13235.
DR Gramene; AT3G13235.2; AT3G13235.2; AT3G13235.
DR KEGG; ath:AT3G13235; -.
DR Araport; AT3G13235; -.
DR TAIR; locus:505006342; AT3G13235.
DR eggNOG; KOG0012; Eukaryota.
DR InParanoid; Q1EBV4; -.
DR OMA; IHMVQIQ; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q1EBV4; -.
DR PRO; PR:Q1EBV4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1EBV4; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..414
FT /note="Protein DNA-DAMAGE INDUCIBLE 1"
FT /id="PRO_0000445396"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 213..292
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 374..414
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 332..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT MUTAGEN 386..387
FT /note="LG->AA: Impaired binding to Lys-48- and Lys-63-
FT linked ubiquitin chains."
FT /evidence="ECO:0000269|PubMed:21764993"
FT CONFLICT 206..210
FT /note="MEVNG -> IEVNS (in Ref. 5; AAM61638)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="T -> M (in Ref. 5; AAM61638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45359 MW; C0AA6EBCD6B685D1 CRC64;
MRITVMTAGE QIITLDVDSQ ETVENVKALL EVESNVPIQQ QQLLYNGNEM GNSDKLSALG
VKDDDLLMMM VSNASSGSAT SAAGNDLGMN PDGSALNPAA FQQHIRGDSN LMGQLFQNDP
ELAQVISGSD LNKLQDVLRA RHRQRSVLQR QKEEELALLY ADPFDVEAQR KIEAAIRQKG
IDENWEAALE HNPEGFARVI MLYVDMEVNG VPLKAFVDSG AQSTIISKSC AERCGLLRLM
DQRYKGIAHG VGQTEILGRI HVAPIKIGNN FYPCSFVVLD SPNMEFLFGL DMLRKHQCTI
DLKENVMTVG GGEVSVPFLQ EKDIPSRFLD EERVPNDASS SGATVPSGFT EKKNNTVANP
TSQQPKRQNT SEGPEFEAKI AKLVELGFSR DSVIQALKLF EGNEEQAAGF LFGG
