SIL11_ARATH
ID SIL11_ARATH Reviewed; 314 AA.
AC Q9FM14; F4K7T7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=E3 ubiquitin-protein ligase SINA-like 11;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SINA-like 11 {ECO:0000305};
DE AltName: Full=Seven in absentia-like protein 11;
GN OrderedLocusNames=At5g62800; ORFNames=MQB2.12;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000250}.
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}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED97659.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10849.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB009053; BAB10849.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97659.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM69719.1; -; Genomic_DNA.
DR RefSeq; NP_001331378.1; NM_001345561.1.
DR RefSeq; NP_201086.1; NM_125675.2.
DR AlphaFoldDB; Q9FM14; -.
DR SMR; Q9FM14; -.
DR STRING; 3702.AT5G62800.1; -.
DR PRIDE; Q9FM14; -.
DR ProteomicsDB; 232556; -.
DR EnsemblPlants; AT5G62800.2; AT5G62800.2; AT5G62800.
DR GeneID; 836401; -.
DR Gramene; AT5G62800.2; AT5G62800.2; AT5G62800.
DR KEGG; ath:AT5G62800; -.
DR Araport; AT5G62800; -.
DR eggNOG; KOG3002; Eukaryota.
DR InParanoid; Q9FM14; -.
DR OMA; LYNSTIC; -.
DR OrthoDB; 1334337at2759; -.
DR PhylomeDB; Q9FM14; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FM14; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM14; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 3.30.40.10; -; 1.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..314
FT /note="E3 ubiquitin-protein ligase SINA-like 11"
FT /id="PRO_0000299200"
FT ZN_FING 43..81
FT /note="RING-type; degenerate"
FT ZN_FING 98..156
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..280
FT /note="SBD"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 110
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 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 150
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"
SQ SEQUENCE 314 AA; 35880 MW; 8AEF52BE2E55D964 CRC64;
MEDSNSHPQN QTSKRKSSHP QKKQRMENET RSAKLLDLDV LDCPVCFEPL TIPTFQCDDG
HIVCNFCFAK VSNKCPGPGC DLPIGNKRCF AMERVLESAF VPCQNTEFGC TKSVSYEKVS
SHEKECNYSQ CSCPNLECNY TGSYNIIYGH FMRRHLYNST IVSSKWGYST VDVLINIKEK
VSVLWESRQK LLFVVQCFKE RHGVYVTVRR IAPPASEFKK FSYRLSYSID GHNVTYESPE
VKRLLEVNSQ IPDDSFMFVP NCLLHGFLIK PANEVQQVTI AQETVMEDPP TSLFKNSVPI
REDQIQNAIT NSIR
