SINA2_ARATH
ID SINA2_ARATH Reviewed; 308 AA.
AC Q9M2P4; Q0WNH5; Q1ECQ0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=E3 ubiquitin-protein ligase SINAT2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:28351989};
DE AltName: Full=RING-type E3 ubiquitin transferase SINAT2 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 2 {ECO:0000305};
GN Name=SINAT2 {ECO:0000303|PubMed:24350984}; OrderedLocusNames=At3g58040;
GN ORFNames=T10K17.250;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP INTERACTION WITH RAP2-2, AND DISRUPTION PHENOTYPE.
RX PubMed=17873090; DOI=10.1104/pp.107.104828;
RA Welsch R., Maass D., Voegel T., Dellapenna D., Beyer P.;
RT "Transcription factor RAP2.2 and its interacting partner SINAT2: stable
RT elements in the carotenogenesis of Arabidopsis leaves.";
RL Plant Physiol. 145:1073-1085(2007).
RN [7]
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [10]
RP FUNCTION, INTERACTION WITH FREE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-78.
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 [11]
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 (PubMed:28351989,
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:28351989, PubMed:32786047). It probably triggers the ubiquitin-
CC mediated degradation of different substrates (PubMed:28351989,
CC PubMed:32786047). Mediates the proteasomal-dependent degradation of
CC ATG6, a component of the autophagosome complex (PubMed:28351989).
CC Requires TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for
CC ubiquitination and subsequent regulation of autophagosome assembly
CC (PubMed:28351989). Modulates directly the ubiquitination and
CC proteasomal-dependent degradation of FREE1, a component of the ESCRT-I
CC complex (PubMed:32786047, PubMed:32753431). Modulates directly the
CC ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a
CC component of the ESCRT-I complex (PubMed:32753431).
CC {ECO:0000269|PubMed:28351989, 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:28351989};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with RAP2-2 (PubMed:17873090). Interacts with SINAT6
CC (PubMed:24350984). Interacts with ATG6 and TRAF1A (PubMed:28351989).
CC Interacts with WAV3 (PubMed:22122664). Interacts with FREE1
CC (PubMed:32786047, PubMed:32753431). Interacts with ELC/VPS23A
CC (PubMed:32753431). {ECO:0000269|PubMed:17873090,
CC ECO:0000269|PubMed:22122664, ECO:0000269|PubMed:24350984,
CC ECO:0000269|PubMed:28351989, ECO:0000269|PubMed:32753431,
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M2P4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M2P4-2; Sequence=VSP_027587, VSP_027588;
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 -!- DISRUPTION PHENOTYPE: No visible phenotype, may be due to the existence
CC of 4 homologous proteins. {ECO:0000269|PubMed:17873090}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
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DR EMBL; AL132977; CAB67632.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79735.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64730.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64731.1; -; Genomic_DNA.
DR EMBL; BT025655; ABF74716.1; -; mRNA.
DR EMBL; AK229466; BAF01324.1; -; mRNA.
DR EMBL; AY087768; AAM65304.1; -; mRNA.
DR PIR; T46026; T46026.
DR RefSeq; NP_001326739.1; NM_001339903.1. [Q9M2P4-1]
DR RefSeq; NP_001326740.1; NM_001339902.1. [Q9M2P4-2]
DR RefSeq; NP_191363.1; NM_115666.2. [Q9M2P4-1]
DR AlphaFoldDB; Q9M2P4; -.
DR SMR; Q9M2P4; -.
DR BioGRID; 10288; 2.
DR IntAct; Q9M2P4; 1.
DR STRING; 3702.AT3G58040.1; -.
DR PaxDb; Q9M2P4; -.
DR PRIDE; Q9M2P4; -.
DR ProteomicsDB; 234551; -. [Q9M2P4-1]
DR EnsemblPlants; AT3G58040.1; AT3G58040.1; AT3G58040. [Q9M2P4-1]
DR EnsemblPlants; AT3G58040.2; AT3G58040.2; AT3G58040. [Q9M2P4-2]
DR EnsemblPlants; AT3G58040.3; AT3G58040.3; AT3G58040. [Q9M2P4-1]
DR GeneID; 824973; -.
DR Gramene; AT3G58040.1; AT3G58040.1; AT3G58040. [Q9M2P4-1]
DR Gramene; AT3G58040.2; AT3G58040.2; AT3G58040. [Q9M2P4-2]
DR Gramene; AT3G58040.3; AT3G58040.3; AT3G58040. [Q9M2P4-1]
DR KEGG; ath:AT3G58040; -.
DR Araport; AT3G58040; -.
DR TAIR; locus:2095848; AT3G58040.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_1_1_1; -.
DR InParanoid; Q9M2P4; -.
DR OMA; TSIAQFC; -.
DR PhylomeDB; Q9M2P4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M2P4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2P4; baseline and differential.
DR Genevisible; Q9M2P4; AT.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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 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 Alternative splicing; Cytoplasmic vesicle; Endosome; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..308
FT /note="E3 ubiquitin-protein ligase SINAT2"
FT /id="PRO_0000056181"
FT ZN_FING 60..96
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 113..173
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 110..303
FT /note="SBD"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
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 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 204..219
FT /note="FNCFGRQFCLHFEAFQ -> KLSFDMFSSFYQRFLI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_027587"
FT VAR_SEQ 220..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_027588"
FT MUTAGEN 78
FT /note="H->Y: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:32786047"
SQ SEQUENCE 308 AA; 34993 MW; 0FC9C2933DFB957E CRC64;
MAPGGSALKE VMESNSTGMD YEVKTAKVEV NNNKPTKPGS AGIGKYGIHS NNGVYELLEC
PVCTNLMYPP IHQCPNGHTL CSNCKLRVQN TCPTCRYELG NIRCLALEKV AESLEVPCRY
QNLGCHDIFP YYSKLKHEQH CRFRPYTCPY AGSECSVTGD IPTLVVHLKD DHKVDMHDGC
TFNHRYVKSN PHEVENATWM LTVFNCFGRQ FCLHFEAFQL GMAPVYMAFL RFMGDENEAK
KFSYSLEVGA HGRKLTWQGI PRSIRDSHRK VRDSQDGLII PRNLALYFSG GDRQELKLRV
TGRIWKEE
