SIL10_ARATH
ID SIL10_ARATH Reviewed; 349 AA.
AC Q84K34; Q9FKD3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase SINA-like 10;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SINA-like 10 {ECO:0000305};
DE AltName: Full=Seven in absentia-like protein 10;
GN OrderedLocusNames=At5g37930; ORFNames=K18L3.13;
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=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).
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).
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=BAB09039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB012241; BAB09039.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94248.1; -; Genomic_DNA.
DR EMBL; BT004120; AAO42143.1; -; mRNA.
DR EMBL; BT004967; AAO50500.1; -; mRNA.
DR RefSeq; NP_198609.1; NM_123152.4.
DR AlphaFoldDB; Q84K34; -.
DR STRING; 3702.AT5G37930.1; -.
DR PaxDb; Q84K34; -.
DR PRIDE; Q84K34; -.
DR ProteomicsDB; 234559; -.
DR EnsemblPlants; AT5G37930.1; AT5G37930.1; AT5G37930.
DR GeneID; 833772; -.
DR Gramene; AT5G37930.1; AT5G37930.1; AT5G37930.
DR KEGG; ath:AT5G37930; -.
DR Araport; AT5G37930; -.
DR TAIR; locus:2153784; AT5G37930.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_040603_2_0_1; -.
DR InParanoid; Q84K34; -.
DR OMA; CTKVRNR; -.
DR OrthoDB; 1334337at2759; -.
DR PhylomeDB; Q84K34; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84K34; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84K34; baseline and differential.
DR Genevisible; Q84K34; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; IPR044286; SINL_plant.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632; PTHR46632; 1.
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..349
FT /note="E3 ubiquitin-protein ligase SINA-like 10"
FT /id="PRO_0000299199"
FT ZN_FING 113..149
FT /note="RING-type; degenerate"
FT ZN_FING 166..224
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..344
FT /note="SBD"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 38924 MW; 2B1504864077C6C6 CRC64;
MARFSVCGGD DGEGPSNNNH QSRKRQRLPS IDENEEDAET SDAGSSGEED EDETQNQGMR
PESEDRGSTS DDSDREVVIE ERRFGKFVNS QSSSSSKDSP LSVTLLDPDV LDCPICCEPL
KIPIFQCDNG HLACTLCCTK VRNRCPSCTL PIGYVRCRAM EKVIEASRVS CLNAKYGCKE
STSYGNRFSH EQVCVFTPCS CPILDCHYTG YYKDLNNHVR AEHKDDLISF VWNTRLTISL
DLNKKTTILQ EENDGHVIVV QVFRALHAVY VSVSCIAPLT PGVGRLSCRL AKITVDSLLK
QGFMVKNIQK VTNEHPEDGF MLIPSYLFSG NDNLNLQIWI GHGRIFVHS
