SINA4_ARATH
ID SINA4_ARATH Reviewed; 327 AA.
AC Q9STN8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein ligase SINAT4 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:32786047};
DE AltName: Full=RING-type E3 ubiquitin transferase SINAT4 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 4 {ECO:0000305};
GN Name=SINAT4 {ECO:0000303|PubMed:24350984}; OrderedLocusNames=At4g27880;
GN ORFNames=T27E11.120;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FREE1, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF HIS-82.
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 [7]
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}.
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DR EMBL; AL078579; CAB43976.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81437.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85404.1; -; Genomic_DNA.
DR EMBL; BX826742; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T09027; T09027.
DR RefSeq; NP_194517.1; NM_118926.3.
DR AlphaFoldDB; Q9STN8; -.
DR SMR; Q9STN8; -.
DR BioGRID; 14188; 2.
DR STRING; 3702.AT4G27880.1; -.
DR PaxDb; Q9STN8; -.
DR PRIDE; Q9STN8; -.
DR ProteomicsDB; 232653; -.
DR EnsemblPlants; AT4G27880.1; AT4G27880.1; AT4G27880.
DR GeneID; 828901; -.
DR Gramene; AT4G27880.1; AT4G27880.1; AT4G27880.
DR KEGG; ath:AT4G27880; -.
DR Araport; AT4G27880; -.
DR TAIR; locus:2137395; AT4G27880.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_1_1_1; -.
DR InParanoid; Q9STN8; -.
DR OMA; TDSMECV; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q9STN8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9STN8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STN8; baseline and differential.
DR Genevisible; Q9STN8; AT.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IPI:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IPI:TAIR.
DR GO; GO:0005886; C:plasma membrane; IPI:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
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..327
FT /note="E3 ubiquitin-protein ligase SINAT4"
FT /id="PRO_0000056183"
FT ZN_FING 64..100
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 117..177
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..307
FT /note="SBD"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 82
FT /note="H->Y: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:32786047"
FT CONFLICT 166
FT /note="P -> L (in Ref. 3; BX826742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36574 MW; 0724A09157567F0C CRC64;
METDSMECVS STGNEIHQNG NGHQSYQFSS TKTHGGAAAA AVVTNIVGPT ATAPATSVYE
LLECPVCTYS MYPPIHQCHN GHTLCSTCKV RVHNRCPTCR QELGDIRCLA LEKVAESLEL
PCKFYNLGCP EIFPYYSKLK HESLCNFRPY SCPYAGSECG IVGDIPFLVA HLRDDHKVDM
HAGSTFNHRY VKSNPREVEN ATWMLTVFHC FGQYFCLHFE AFQLGMGPVY MAFLRFMGDE
EDARSYSYSL EVGGSGRKLT WEGTPRSIRD SHRKVRDSND GLIIQRNMAL FFSGGDRKEL
KLRVTGKIWK EQHSPDSGLS IPNLSSS
