SINA6_ARATH
ID SINA6_ARATH Reviewed; 216 AA.
AC Q93WE4; Q9LID2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable inactive E3 ubiquitin-protein ligase SINAT6 {ECO:0000305};
DE AltName: Full=Protein SEVEN IN ABSENTIA 2 {ECO:0000303|PubMed:24350984};
DE AltName: Full=Seven in absentia homolog 6 {ECO:0000305|PubMed:28351989};
GN Name=SINAT6 {ECO:0000303|PubMed:28351989};
GN Synonyms=SINA2 {ECO:0000303|PubMed:24350984};
GN OrderedLocusNames=At3g13672 {ECO:0000312|Araport:AT3G13672};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, HOMODIMERIZATION, INTERACTION WITH SINAT1; SINAT2; SINAT3; SINAT4
RP AND SINAT5, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24350984; DOI=10.1111/nph.12644;
RA Bao Y., Wang C., Jiang C., Pan J., Zhang G., Liu H., Zhang H.;
RT "The tumor necrosis factor receptor-associated factor (TRAF)-like family
RT protein SEVEN IN ABSENTIA 2 (SINA2) promotes drought tolerance in an ABA-
RT dependent manner in Arabidopsis.";
RL New Phytol. 202:174-187(2014).
RN [5]
RP FUNCTION, AND INTERACTION WITH ATG6 AND TRAF1A.
RX PubMed=28351989; DOI=10.1105/tpc.17.00056;
RA Qi H., Xia F.N., Xie L.J., Yu L.J., Chen Q.F., Zhuang X.H., Wang Q., Li F.,
RA Jiang L., Xie Q., Xiao S.;
RT "TRAF family proteins regulate autophagy dynamics by modulating AUTOPHAGY
RT PROTEIN6 stability in Arabidopsis.";
RL Plant Cell 29:890-911(2017).
CC -!- FUNCTION: Probable inactive E3 ubiquitin-protein ligase that plays a
CC role in regulation of autophagy. Upon starvation, involved in
CC maintaining ATG6 homeostasis by competitively associating with ATG6, a
CC component of the autophagosome complex (PubMed:28351989). Acts as
CC positive regulator of drought stress response. Functions as positive
CC regulator of abscisic acid-mediated stomatal closure (PubMed:24350984).
CC {ECO:0000269|PubMed:24350984, ECO:0000269|PubMed:28351989}.
CC -!- SUBUNIT: Homodimer (PubMed:24350984). Interacts with SINAT1, SINAT2,
CC SINAT3, SINAT4 and SINAT5 (PubMed:24350984). Interacts with ATG6 and
CC TRAF1A (PubMed:28351989). {ECO:0000269|PubMed:24350984,
CC ECO:0000269|PubMed:28351989}.
CC -!- INTERACTION:
CC Q93WE4; O80575: At2g44050; NbExp=3; IntAct=EBI-4446419, EBI-4473692;
CC Q93WE4; O23160: MYB73; NbExp=3; IntAct=EBI-4446419, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24350984}. Nucleus
CC {ECO:0000269|PubMed:24350984}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC guard cells and flowers. {ECO:0000269|PubMed:24350984}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) and salt stress.
CC {ECO:0000269|PubMed:24350984}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are hypersensitive to drought stress.
CC {ECO:0000269|PubMed:24350984}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the RING-type zinc finger domain that is essential for
CC ubiquitin ligase activity. May not possess E3 ubiquitin-protein ligase
CC activity by itself. {ECO:0000305|PubMed:24350984}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01915.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001307; BAB01915.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75391.1; -; Genomic_DNA.
DR EMBL; AF370175; AAK43990.1; -; mRNA.
DR EMBL; AY059135; AAL15241.1; -; mRNA.
DR RefSeq; NP_187978.1; NM_112215.2.
DR AlphaFoldDB; Q93WE4; -.
DR SMR; Q93WE4; -.
DR IntAct; Q93WE4; 5.
DR STRING; 3702.AT3G13672.2; -.
DR PRIDE; Q93WE4; -.
DR EnsemblPlants; AT3G13672.1; AT3G13672.1; AT3G13672.
DR GeneID; 820573; -.
DR Gramene; AT3G13672.1; AT3G13672.1; AT3G13672.
DR KEGG; ath:AT3G13672; -.
DR Araport; AT3G13672; -.
DR eggNOG; KOG3002; Eukaryota.
DR PhylomeDB; Q93WE4; -.
DR PRO; PR:Q93WE4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93WE4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR008974; TRAF-like.
DR Pfam; PF03145; Sina; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..216
FT /note="Probable inactive E3 ubiquitin-protein ligase
FT SINAT6"
FT /id="PRO_0000442355"
FT ZN_FING 5..74
FT /note="SIAH-type"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 25140 MW; 2A8D7A17B2CAC361 CRC64;
MEPRINDLQV ESRVHELLDF PVHTNQISSA IYECPNDHIE NPKKKPYNCP HSGAKCDVTG
DIQRLLLHLR NDHNVEMSDG RSFSHRYVHH DPKHLHHATW MLTLLDCCGR KFCLYFEAFH
LRKTPMYMAF MQFMGDEEEA MSFSYSLQVG GNGRKLTWQG VPRSIRDSHK TVRDSQDGLI
ITRKLALFFS TDNNTTDKEL KLKVSGRVWR EQPVSI
