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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
 
 
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