SINA1_ARATH
ID SINA1_ARATH Reviewed; 305 AA.
AC P93748;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative E3 ubiquitin-protein ligase SINAT1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:28351989};
DE AltName: Full=RING-type E3 ubiquitin transferase SINAT1 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 1 {ECO:0000305};
GN Name=SINAT1 {ECO:0000303|PubMed:24350984}; OrderedLocusNames=At2g41980;
GN ORFNames=T6D20.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 [4]
RP INTERACTION WITH SINAT6.
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, 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 [6]
RP FUNCTION, INTERACTION WITH FREE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-75.
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 (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 SINAT6 (PubMed:24350984). Interacts with ATG6
CC and TRAF1A (PubMed:28351989). Interacts with WAV3 (PubMed:22122664).
CC Interacts with FREE1 (PubMed:32786047, PubMed:32753431). Interacts with
CC ELC/VPS23A (PubMed:32753431). {ECO:0000269|PubMed:22122664,
CC ECO:0000269|PubMed:24350984, ECO:0000269|PubMed:28351989,
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 -!- 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; U90439; AAB63545.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10058.1; -; Genomic_DNA.
DR PIR; E84848; E84848.
DR RefSeq; NP_181729.1; NM_129762.6.
DR AlphaFoldDB; P93748; -.
DR SMR; P93748; -.
DR STRING; 3702.AT2G41980.1; -.
DR iPTMnet; P93748; -.
DR PaxDb; P93748; -.
DR PRIDE; P93748; -.
DR ProteomicsDB; 234567; -.
DR EnsemblPlants; AT2G41980.1; AT2G41980.1; AT2G41980.
DR GeneID; 818798; -.
DR Gramene; AT2G41980.1; AT2G41980.1; AT2G41980.
DR KEGG; ath:AT2G41980; -.
DR Araport; AT2G41980; -.
DR TAIR; locus:2064642; AT2G41980.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_1_1_1; -.
DR InParanoid; P93748; -.
DR OMA; GSGRKFM; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; P93748; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P93748; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93748; baseline and differential.
DR Genevisible; P93748; 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 Cytoplasmic vesicle; Endosome; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..305
FT /note="Putative E3 ubiquitin-protein ligase SINAT1"
FT /id="PRO_0000056180"
FT ZN_FING 57..93
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 110..170
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 107..300
FT /note="SBD"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
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="1"
FT /evidence="ECO:0000250"
FT BINDING 138
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="2"
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 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 75
FT /note="H->Y: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:32786047"
SQ SEQUENCE 305 AA; 34557 MW; 85E183DD5985E116 CRC64;
MAPGGSALKE ALESNSTGVD YEVKMAKVEA NSKPTKSGSG SIGKFHSSNG VYELLECPVC
TNLMYPPIHQ CPNGHTLCSS CKLRVQNTCP TCRYELGNIR CLALEKVAES LEVPCRYQNL
GCQDIFPYYS KLKHEQHCRF RSYSCPYAGS ECSVTGDIPT LVDHLKDDHK VDMHDGCTFN
HRYVKSNPHE VENATWMLTV FNCFGRQFCL HFEAFQLGMA PVYMAFLRFM GDENEAKKFS
YSLEVGAHSR KLTWQGIPRS IRDSHRKVRD SQDGLIIPRN LALYFSGSDK EELKLRVTGR
IWKEE
