SDIR1_ARATH
ID SDIR1_ARATH Reviewed; 273 AA.
AC Q9M2S6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=E3 ubiquitin-protein ligase SDIR1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:17573536};
DE AltName: Full=Protein SALT- AND DROUGHT-INDUCED RING FINGER 1 {ECO:0000303|PubMed:17573536};
DE AltName: Full=RING-type E3 ubiquitin transferase SDIR1 {ECO:0000305};
GN Name=SDIR1 {ECO:0000303|PubMed:17573536}; OrderedLocusNames=At3g55530;
GN ORFNames=T22E16.190;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, INDUCTION BY DROUGHT AND SALT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, DOMAIN, MUTAGENESIS OF HIS-234, AND DISRUPTION PHENOTYPE.
RX PubMed=17573536; DOI=10.1105/tpc.106.048488;
RA Zhang Y., Yang C., Li Y., Zheng N., Chen H., Zhao Q., Gao T., Guo H.,
RA Xie Q.;
RT "SDIR1 is a RING finger E3 ligase that positively regulates stress-
RT responsive abscisic acid signaling in Arabidopsis.";
RL Plant Cell 19:1912-1929(2007).
RN [6]
RP FUNCTION.
RX PubMed=18685183; DOI=10.1271/bbb.80286;
RA Zhang Y.Y., Li Y., Gao T., Zhu H., Wang D.J., Zhang H.W., Ning Y.S.,
RA Liu L.J., Wu Y.R., Chu C.C., Guo H.S., Xie Q.;
RT "Arabidopsis SDIR1 enhances drought tolerance in crop plants.";
RL Biosci. Biotechnol. Biochem. 72:2251-2254(2008).
RN [7]
RP INDUCTION BY DROUGHT.
RX PubMed=18624643; DOI=10.1094/mpmi-21-6-0799;
RA Sherameti I., Tripathi S., Varma A., Oelmuller R.;
RT "The root-colonizing endophyte Pirifomospora indica confers drought
RT tolerance in Arabidopsis by stimulating the expression of drought stress-
RT related genes in leaves.";
RL Mol. Plant Microbe Interact. 21:799-807(2008).
RN [8]
RP FUNCTION, INTERACTION WITH ATP1/SDIRIP1, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=25616872; DOI=10.1105/tpc.114.134163;
RA Zhang H., Cui F., Wu Y., Lou L., Liu L., Tian M., Ning Y., Shu K., Tang S.,
RA Xie Q.;
RT "The RING finger ubiquitin E3 ligase SDIR1 targets SDIR1-INTERACTING
RT PROTEIN1 for degradation to modulate the salt stress response and ABA
RT signaling in Arabidopsis.";
RL Plant Cell 27:214-227(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a positive regulator
CC of abscisic acid-related stress signal transduction (PubMed:17573536,
CC PubMed:18685183). Interacts with and ubiquitinates ATP1/SDIRIP1 to
CC modulate ATP1/SDIRIP1 stability through the 26S proteasome pathway.
CC Regulates abscisic acid (ABA) and salt stress responses by negatively
CC affecting ATP1/SDIRIP1 stability. The SDIR1-ATP1/SDIRIP1 complex plays
CC an important role in ABA signaling through the ubiquitination pathway
CC (PubMed:25616872). {ECO:0000269|PubMed:17573536,
CC ECO:0000269|PubMed:18685183, ECO:0000269|PubMed:25616872}.
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:17573536};
CC -!- SUBUNIT: Interacts with ATP1/SDIRIP1. {ECO:0000269|PubMed:25616872}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25616872}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17573536}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages.
CC {ECO:0000269|PubMed:17573536}.
CC -!- INDUCTION: Up-regulated by salt and drought stress, but not by abscisic
CC acid. The up-regulation is stronger and earlier when the roots are
CC colonized by the endophytic fungus P.indica.
CC {ECO:0000269|PubMed:17573536, ECO:0000269|PubMed:18624643}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000305|PubMed:17573536}.
CC -!- DISRUPTION PHENOTYPE: Longer primary root and NaCl and ABA
CC insensitivity. {ECO:0000269|PubMed:17573536}.
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DR EMBL; AL132975; CAB75911.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79397.1; -; Genomic_DNA.
DR EMBL; AF386995; AAK62440.1; -; mRNA.
DR EMBL; BT006305; AAP13413.1; -; mRNA.
DR EMBL; AK317055; BAH19748.1; -; mRNA.
DR PIR; T47692; T47692.
DR RefSeq; NP_191112.1; NM_115410.3.
DR AlphaFoldDB; Q9M2S6; -.
DR SMR; Q9M2S6; -.
DR BioGRID; 10034; 3.
DR IntAct; Q9M2S6; 3.
DR STRING; 3702.AT3G55530.1; -.
DR PaxDb; Q9M2S6; -.
DR PRIDE; Q9M2S6; -.
DR ProteomicsDB; 232947; -.
DR EnsemblPlants; AT3G55530.1; AT3G55530.1; AT3G55530.
DR GeneID; 824718; -.
DR Gramene; AT3G55530.1; AT3G55530.1; AT3G55530.
DR KEGG; ath:AT3G55530; -.
DR Araport; AT3G55530; -.
DR TAIR; locus:2100021; AT3G55530.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_071713_0_0_1; -.
DR InParanoid; Q9M2S6; -.
DR OMA; CKFRAHS; -.
DR OrthoDB; 1140592at2759; -.
DR PhylomeDB; Q9M2S6; -.
DR PRO; PR:Q9M2S6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2S6; baseline and differential.
DR Genevisible; Q9M2S6; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..273
FT /note="E3 ubiquitin-protein ligase SDIR1"
FT /id="PRO_0000395672"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25616872"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..56
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25616872"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25616872"
FT ZN_FING 211..252
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 234
FT /note="H->Y: Loss of ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:17573536"
SQ SEQUENCE 273 AA; 30184 MW; B239A052A89B22F4 CRC64;
MSFVFRGSRG DLESGFSGGF LPERRAMRVH GARPVNSNSL AFLVTVLLLF MILNSHQMPP
NFLLWLVLGV FLMATTLRMY ATCQQLQAHA QAQAAAASGL FSHTELRLHV PPSIALATRG
RLQGLRLQLA LLDREFDDLD YETLRALDSD NVSTTSMSEE EINALPVHKY KVLDPENGCS
LAKQASTSSS AEKMLDSANE SKKGTEDELT CSVCLEQVTV GEIVRTLPCL HQFHAGCIDP
WLRQQGTCPV CKFRAHSGWQ EQDEIDDDAS DMV
