SINA5_ARATH
ID SINA5_ARATH Reviewed; 309 AA.
AC Q8S3N1; Q8GYS3; Q9FK06;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase SINAT5 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:12226665};
DE AltName: Full=RING-type E3 ubiquitin transferase SINAT5 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 5 {ECO:0000305};
GN Name=SINAT5 {ECO:0000303|PubMed:24350984}; OrderedLocusNames=At5g53360;
GN ORFNames=K19E1.16;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP HOMODIMERIZATION, INTERACTION WITH UBC28 AND NAC021/NAC022, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF CYS-49 AND
RP HIS-64.
RX PubMed=12226665; DOI=10.1038/nature00998;
RA Xie Q., Guo H.-S., Dallman G., Fang S., Weissman A.M., Chua N.-H.;
RT "SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin
RT signals.";
RL Nature 419:167-170(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
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 [7]
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 [8]
RP 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 [9]
RP FUNCTION, INTERACTION WITH FREE1, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins
CC (PubMed:12226665). 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:12226665). Mediates the ubiquitination and proteasomal-
CC dependent degradation of NAC021/NAC022, a transcription activator that
CC functions downstream of the auxin signals, thereby acting as a down-
CC regulator of auxin signals (PubMed:12226665). Involved in the formation
CC of lateral roots (PubMed:12226665). Is antagonist to SINAT1, SINAT2,
CC SINAT3 and SINAT4 by suppressing FREE1 ubiquitination and degradation
CC mediated by SINAT1, SINAT2, SINAT3 and SINAT4, and promoting FREE1
CC accumulation (PubMed:32786047). {ECO:0000269|PubMed:12226665,
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:12226665};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer; homodimerization is essential for its function.
CC Interacts with UBC28 and NAC021/NAC022 (PubMed:12226665). Interacts
CC with SINAT6 (PubMed:24350984). Interacts with ATG6 and TRAF1A
CC (PubMed:28351989). Interacts with WAV3 (PubMed:22122664). Interacts
CC with FREE1 (PubMed:32786047). {ECO:0000269|PubMed:12226665,
CC ECO:0000269|PubMed:22122664, ECO:0000269|PubMed:24350984,
CC ECO:0000269|PubMed:28351989, ECO:0000269|PubMed:32786047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12226665}. Cytoplasm
CC {ECO:0000269|PubMed:12226665}. Note=Predominantly nuclear. Partially
CC cytoplasmic. Multivesicular body (PubMed:32786047).
CC {ECO:0000269|PubMed:12226665, ECO:0000269|PubMed:32786047}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S3N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S3N1-2; Sequence=VSP_010169, VSP_010170;
CC -!- TISSUE SPECIFICITY: Expressed at low level in the vascular tissue of
CC mature roots. Expressed in lateral roots and in elongation zone of the
CC main root upon stimulation by auxin. Colocalizes with NAC021/NAC022.
CC {ECO:0000269|PubMed:12226665}.
CC -!- INDUCTION: By auxin (PubMed:12226665). Induced by salt stress
CC (PubMed:24350984). {ECO:0000269|PubMed:12226665,
CC 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=BAB09798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF480944; AAM11573.1; -; mRNA.
DR EMBL; AB013388; BAB09798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96344.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69124.1; -; Genomic_DNA.
DR EMBL; AK117423; BAC42088.1; -; mRNA.
DR EMBL; BT005507; AAO63927.1; -; mRNA.
DR RefSeq; NP_001330825.1; NM_001345051.1. [Q8S3N1-2]
DR RefSeq; NP_200148.2; NM_124715.4. [Q8S3N1-2]
DR AlphaFoldDB; Q8S3N1; -.
DR SMR; Q8S3N1; -.
DR BioGRID; 20662; 6.
DR IntAct; Q8S3N1; 2.
DR STRING; 3702.AT5G53360.1; -.
DR PaxDb; Q8S3N1; -.
DR PRIDE; Q8S3N1; -.
DR EnsemblPlants; AT5G53360.1; AT5G53360.1; AT5G53360. [Q8S3N1-2]
DR EnsemblPlants; AT5G53360.3; AT5G53360.3; AT5G53360. [Q8S3N1-2]
DR GeneID; 835417; -.
DR Gramene; AT5G53360.1; AT5G53360.1; AT5G53360. [Q8S3N1-2]
DR Gramene; AT5G53360.3; AT5G53360.3; AT5G53360. [Q8S3N1-2]
DR KEGG; ath:AT5G53360; -.
DR Araport; AT5G53360; -.
DR TAIR; locus:2154267; AT5G53360.
DR eggNOG; KOG3002; Eukaryota.
DR InParanoid; Q8S3N1; -.
DR OMA; YIMPPIM; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q8S3N1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8S3N1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S3N1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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: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; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..309
FT /note="E3 ubiquitin-protein ligase SINAT5"
FT /id="PRO_0000056184"
FT ZN_FING 46..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 99..159
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 96..289
FT /note="SBD"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
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 VAR_SEQ 1..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_010169"
FT VAR_SEQ 77..91
FT /note="RCPTCRQELGDIRCL -> MDILYVQPVNQECII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_010170"
FT MUTAGEN 49
FT /note="C->S: Abolishes ubiquitination in vitro; acts as a
FT dominant-negative mutant."
FT /evidence="ECO:0000269|PubMed:12226665"
FT MUTAGEN 64
FT /note="H->Y: Abolishes ubiquitination in vitro."
FT /evidence="ECO:0000269|PubMed:12226665"
FT CONFLICT 268
FT /note="R -> K (in Ref. 1; AAM11573 and 5; AAO63927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35037 MW; 39162D09D6B57AAF CRC64;
METDSIDSVI DDDEIHQKHQ FSSTKSQGGA TVVISPATSV YELLECPVCT NSMYPPIHQC
HNGHTLCSTC KSRVHNRCPT CRQELGDIRC LALEKVAESL ELPCKYYNLG CLGIFPYYSK
LKHESQCNFR PYSCPYAGSE CAAVGDITFL VAHLRDDHKV DMHTGCTFNH RYVKSNPREV
ENATWMLTVF QCFGQYFCLH FEAFQLGMAP VYMAFLRFMG DEDDARNYTY SLEVGGSGRK
QTWEGTPRSV RDSHRKVRDS HDGLIIQRNM ALFFSGGDKK ELKLRVTGRI WKEQQNPDSG
VCITSMCSS
