DIS1_ORYSJ
ID DIS1_ORYSJ Reviewed; 301 AA.
AC Q10L91;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase DIS1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:21719639};
DE AltName: Full=Drought-induced SINA protein 1 {ECO:0000303|PubMed:21719639};
DE Short=OsDIS1 {ECO:0000303|PubMed:21719639};
DE AltName: Full=RING-type E3 ubiquitin transferase DIS1 {ECO:0000305};
GN Name=DIS1 {ECO:0000303|PubMed:21719639};
GN OrderedLocusNames=Os03g0356414 {ECO:0000312|EMBL:BAH92148.1},
GN LOC_Os03g24040 {ECO:0000312|EMBL:ABF96019.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NEK6, SUBCELLULAR LOCATION,
RP INDUCTION BY DROUGHT STRESS, AND MUTAGENESIS OF HIS-71.
RX PubMed=21719639; DOI=10.1104/pp.111.180893;
RA Ning Y., Jantasuriyarat C., Zhao Q., Zhang H., Chen S., Liu J., Liu L.,
RA Tang S., Park C.H., Wang X., Liu X., Dai L., Xie Q., Wang G.L.;
RT "The SINA E3 ligase OsDIS1 negatively regulates drought response in rice.";
RL Plant Physiol. 157:242-255(2011).
RN [7]
RP INTERACTION WITH SKIPA.
RX PubMed=22067990; DOI=10.4161/psb.6.11.17916;
RA Ning Y., Xie Q., Wang G.L.;
RT "OsDIS1-mediated stress response pathway in rice.";
RL Plant Signal. Behav. 6:1684-1686(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates (Probable). Plays a negative role in drought stress
CC tolerance through transcriptional and post-translational regulation of
CC diverse stress-related genes. Interacts with the serine/threonine-
CC protein kinase NEK6 and promotes its degradation via the 26S
CC proteasome-dependent pathway (PubMed:21719639).
CC {ECO:0000269|PubMed:21719639, ECO:0000305|PubMed:21719639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:21719639};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with NEK6 (PubMed:21719639).
CC Interacts with SKIPA (PubMed:22067990). {ECO:0000269|PubMed:21719639,
CC ECO:0000269|PubMed:22067990, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21719639}. Cytoplasm
CC {ECO:0000269|PubMed:21719639}. Note=Predominantly nuclear. Partially
CC cytoplasmic. {ECO:0000269|PubMed:21719639}.
CC -!- INDUCTION: Induced by drought stress. {ECO:0000269|PubMed:21719639}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000305}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC homodimerization and the interaction with substrate proteins. It is
CC related to the TRAF family. {ECO:0000250}.
CC -!- MISCELLANEOUS: Plants overexpressing DIS1 exhibit reduced drought
CC tolerance. Plants silencing DIS1 show enhanced drought tolerance.
CC {ECO:0000269|PubMed:21719639}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
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DR EMBL; DP000009; ABF96019.1; -; Genomic_DNA.
DR EMBL; AP008209; BAH92148.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS84239.1; -; Genomic_DNA.
DR EMBL; AK058336; BAG86666.1; -; mRNA.
DR RefSeq; XP_015628073.1; XM_015772587.1.
DR RefSeq; XP_015628074.1; XM_015772588.1.
DR RefSeq; XP_015628076.1; XM_015772590.1.
DR AlphaFoldDB; Q10L91; -.
DR SMR; Q10L91; -.
DR STRING; 4530.OS03T0356414-01; -.
DR PaxDb; Q10L91; -.
DR PRIDE; Q10L91; -.
DR EnsemblPlants; Os03t0356414-01; Os03t0356414-01; Os03g0356414.
DR GeneID; 9266295; -.
DR Gramene; Os03t0356414-01; Os03t0356414-01; Os03g0356414.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_1_0_1; -.
DR InParanoid; Q10L91; -.
DR OMA; ADHEDAC; -.
DR OrthoDB; 780610at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0080148; P:negative regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Stress response;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..301
FT /note="E3 ubiquitin-protein ligase DIS1"
FT /id="PRO_0000442185"
FT ZN_FING 53..89
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 106..166
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT MUTAGEN 71
FT /note="H->Y: Loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:21719639"
SQ SEQUENCE 301 AA; 34075 MW; 94D559E3937218F7 CRC64;
MASVTYIDDS GSEVIDPPKT EVLDVTELAG DPVPHSPKPN VVVSSSVREL LECPVCLSAM
YPPIHQCSNG HTLCSGCKPR VHNRCPTCRH ELGNIRCLAL EKVAASLELP CKYQNFGCVG
IYPYYCKLKH ESQCQYRPYS CPYAGSECTV AGDIPYLVNH LKDDHKVDMH NGCTFNHRYV
KSNPHEVENA TWMLTVFSCF GQYFCLHFEA FQLGMAPVYI AFLRFMGDDL EAKNYSYSLE
VGGTGRKMIW QGVPRSIRDS HRKVRDSYDG LIIQRNMALF FSGGERKELK LRVTGRIWKE
Q
