SINA3_ARATH
ID SINA3_ARATH Reviewed; 326 AA.
AC Q84JL3; Q8LFQ3; Q9M359;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=E3 ubiquitin-protein ligase SINAT3 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:32786047};
DE AltName: Full=RING-type E3 ubiquitin transferase SINAT3 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 3 {ECO:0000305};
GN Name=SINAT3 {ECO:0000303|PubMed:24350984}; OrderedLocusNames=At3g61790;
GN ORFNames=F15G16.180;
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].
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 [5]
RP INTERACTION WITH WAV3.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22122664; DOI=10.1111/j.1365-313x.2011.04870.x;
RA Sakai T., Mochizuki S., Haga K., Uehara Y., Suzuki A., Harada A., Wada T.,
RA Ishiguro S., Okada K.;
RT "The wavy growth 3 E3 ligase family controls the gravitropic response in
RT Arabidopsis roots.";
RL Plant J. 70:303-314(2012).
RN [6]
RP INTERACTION WITH SINAT6, AND INDUCTION.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FREE1, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF HIS-81.
RX PubMed=32786047; DOI=10.1111/jipb.13005;
RA Xiao Z., Yang C., Liu C., Yang L., Yang S., Zhou J., Li F., Jiang L.,
RA Xiao S., Gao C., Shen W.;
RT "SINAT E3 ligases regulate the stability of the ESCRT component FREE1 in
RT response to iron deficiency in plants.";
RL J. Integr. Plant Biol. 62:1399-1417(2020).
RN [8]
RP FUNCTION, INTERACTION WITH FREE1 AND ELC/VPS23A, AND SUBCELLULAR LOCATION.
RX PubMed=32753431; DOI=10.1105/tpc.20.00267;
RA Xia F.N., Zeng B., Liu H.S., Qi H., Xie L.J., Yu L.J., Chen Q.F., Li J.F.,
RA Chen Y.Q., Jiang L., Xiao S.;
RT "SINAT E3 ubiquitin ligases mediate FREE1 and VPS23A degradation to
RT modulate abscisic acid signaling.";
RL Plant Cell 32:3290-3310(2020).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins
CC (PubMed:32786047). E3 ubiquitin ligases accept ubiquitin from an E2
CC ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates
CC (PubMed:32786047). It probably triggers the ubiquitin-mediated
CC degradation of different substrates (PubMed:32786047). Modulates
CC directly the ubiquitination and proteasomal-dependent degradation of
CC FREE1, a component of the ESCRT-I complex (PubMed:32786047,
CC PubMed:32753431). Modulates directly the ubiquitination and
CC proteasomal-dependent degradation of ELC/VPS23A, a component of the
CC ESCRT-I complex (PubMed:32753431). {ECO:0000269|PubMed:32753431,
CC ECO:0000269|PubMed:32786047}.
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:32786047};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with SINAT6 (PubMed:24350984). Interacts with WAV3
CC (PubMed:22122664). Interacts with FREE1 (PubMed:32786047,
CC PubMed:32753431). Interacts with ELC/VPS23A (PubMed:32753431).
CC {ECO:0000269|PubMed:22122664, ECO:0000269|PubMed:24350984,
CC ECO:0000269|PubMed:32753431, ECO:0000269|PubMed:32786047}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body
CC {ECO:0000269|PubMed:32753431, ECO:0000269|PubMed:32786047}. Cytoplasmic
CC vesicle, autophagosome {ECO:0000269|PubMed:32753431}.
CC -!- INDUCTION: Induced by drought stress, salt stress, osmotic shock and
CC abscisic acid (ABA). {ECO:0000269|PubMed:24350984}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000250|UniProtKB:Q8IUQ4}.
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|UniProtKB:Q8IUQ4}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71109.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL132959; CAB71109.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE80257.1; -; Genomic_DNA.
DR EMBL; BT003967; AAO42011.1; -; mRNA.
DR EMBL; BT005079; AAO50612.1; -; mRNA.
DR EMBL; AY084712; AAM61286.1; -; mRNA.
DR PIR; T47971; T47971.
DR RefSeq; NP_567118.1; NM_116044.4.
DR AlphaFoldDB; Q84JL3; -.
DR SMR; Q84JL3; -.
DR BioGRID; 10666; 24.
DR IntAct; Q84JL3; 18.
DR STRING; 3702.AT3G61790.1; -.
DR PaxDb; Q84JL3; -.
DR PRIDE; Q84JL3; -.
DR ProteomicsDB; 234584; -.
DR EnsemblPlants; AT3G61790.1; AT3G61790.1; AT3G61790.
DR GeneID; 825352; -.
DR Gramene; AT3G61790.1; AT3G61790.1; AT3G61790.
DR KEGG; ath:AT3G61790; -.
DR Araport; AT3G61790; -.
DR TAIR; locus:2076810; AT3G61790.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_1_1_1; -.
DR InParanoid; Q84JL3; -.
DR OMA; HEAQCMF; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q84JL3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84JL3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84JL3; baseline and differential.
DR Genevisible; Q84JL3; AT.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Cytoplasmic vesicle; Endosome; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..326
FT /note="E3 ubiquitin-protein ligase SINAT3"
FT /id="PRO_0000056182"
FT ZN_FING 63..99
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 116..176
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..306
FT /note="SBD"
FT COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 81
FT /note="H->Y: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:32786047"
FT CONFLICT 228
FT /note="V -> F (in Ref. 4; AAM61286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36947 MW; 96653A1E8EC7F9FA CRC64;
MDLDSMDCTS TMDVTDDEEI HQDRHSYASV SKHHHTNNNT TNVNAAASGL LPTTTSVHEL
LECPVCTNSM YPPIHQCHNG HTLCSTCKAR VHNRCPTCRQ ELGDIRCLAL EKVAESLELP
CKHMSLGCPE IFPYYSKLKH ETVCNFRPYS CPYAGSECSV TGDIPFLVAH LRDDHKVDMH
SGCTFNHRYV KSNPREVENA TWMLTVFHCF GQYFCLHFEA FQLGMAPVYM AFLRFMGDET
EARNYNYSLE VGGYGRKLIW EGTPRSVRDS HRKVRDSHDG LIIQRNMALF FSGGDRKELK
LRVTGRIWKE QQQSGEGGGA CIPNLS
