SINL6_ARATH
ID SINL6_ARATH Reviewed; 281 AA.
AC Q9FKD9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative E3 ubiquitin-protein ligase SINA-like 6;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SINA-like 6 {ECO:0000305};
DE AltName: Full=Seven in absentia-like protein 6;
GN OrderedLocusNames=At5g37870; ORFNames=K18L3.4;
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=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 [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}.
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DR EMBL; AB012241; BAB09033.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94243.1; -; Genomic_DNA.
DR RefSeq; NP_198603.1; NM_123146.1.
DR AlphaFoldDB; Q9FKD9; -.
DR SMR; Q9FKD9; -.
DR STRING; 3702.AT5G37870.1; -.
DR PaxDb; Q9FKD9; -.
DR PRIDE; Q9FKD9; -.
DR EnsemblPlants; AT5G37870.1; AT5G37870.1; AT5G37870.
DR GeneID; 833765; -.
DR Gramene; AT5G37870.1; AT5G37870.1; AT5G37870.
DR KEGG; ath:AT5G37870; -.
DR Araport; AT5G37870; -.
DR TAIR; locus:2153804; AT5G37870.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_040603_2_2_1; -.
DR InParanoid; Q9FKD9; -.
DR OMA; TMTYQSP; -.
DR OrthoDB; 1334337at2759; -.
DR PhylomeDB; Q9FKD9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FKD9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKD9; baseline and differential.
DR Genevisible; Q9FKD9; AT.
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; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR044286; SINL_plant.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632; PTHR46632; 1.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..281
FT /note="Putative E3 ubiquitin-protein ligase SINA-like 6"
FT /id="PRO_0000299195"
FT ZN_FING 45..81
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 98..156
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..280
FT /note="SBD"
FT /evidence="ECO:0000250"
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 281 AA; 31313 MW; 2F7D8E27F6D63A7F CRC64;
MVGVLLSERN GSQKRHCSSI SSDDGRKRVD KTRSAMLTDL DILDCPICYQ ALKIPVFQCG
NGHLACSSCC PKLRNKCPAC ALPVGHIRCR AMERVLESVL VPCRYADLGC TKTIYYGRES
THEKICNFSP CSCPVQGCNY TGSYKDLYEH YDLTHSTGST AYSFNGVSYI AAMMFISDKI
LIERVYEKKL LFVVQCFEEP CGVYVSVSCI APSAPEVGEF SYGLLYTTWE GVTMTYQSPK
VKKVLKVSSQ RPKDSFMLIP HSLLCGPLLG MMLCINELKQ M
