SINL1_ARATH
ID SINL1_ARATH Reviewed; 366 AA.
AC Q9C6H4; Q1PFG0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase SINA-like 1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SINA-like 1 {ECO:0000305};
DE AltName: Full=Seven in absentia-like protein 1;
GN OrderedLocusNames=At1g66610; ORFNames=T12I7.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C6H4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C6H4-2; Sequence=VSP_027589, VSP_027590;
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; AC079285; AAG51177.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34535.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34536.1; -; Genomic_DNA.
DR EMBL; DQ446403; ABE65747.1; -; mRNA.
DR PIR; A96692; A96692.
DR RefSeq; NP_001185331.1; NM_001198402.1. [Q9C6H4-2]
DR RefSeq; NP_176834.1; NM_105332.1. [Q9C6H4-1]
DR AlphaFoldDB; Q9C6H4; -.
DR STRING; 3702.AT1G66610.1; -.
DR iPTMnet; Q9C6H4; -.
DR PaxDb; Q9C6H4; -.
DR PRIDE; Q9C6H4; -.
DR EnsemblPlants; AT1G66610.1; AT1G66610.1; AT1G66610. [Q9C6H4-1]
DR EnsemblPlants; AT1G66610.2; AT1G66610.2; AT1G66610. [Q9C6H4-2]
DR GeneID; 842979; -.
DR Gramene; AT1G66610.1; AT1G66610.1; AT1G66610. [Q9C6H4-1]
DR Gramene; AT1G66610.2; AT1G66610.2; AT1G66610. [Q9C6H4-2]
DR KEGG; ath:AT1G66610; -.
DR Araport; AT1G66610; -.
DR TAIR; locus:2195170; AT1G66610.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_040603_2_2_1; -.
DR InParanoid; Q9C6H4; -.
DR OMA; MSINRNI; -.
DR OrthoDB; 1334337at2759; -.
DR PhylomeDB; Q9C6H4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9C6H4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6H4; baseline and differential.
DR Genevisible; Q9C6H4; 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; -; 2.
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; 3.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..366
FT /note="E3 ubiquitin-protein ligase SINA-like 1"
FT /id="PRO_0000299190"
FT ZN_FING 56..92
FT /note="RING-type; degenerate"
FT ZN_FING 109..232
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..354
FT /note="SBD"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 175..237
FT /note="QSLFLAKRQNGCTETFSYGNELVHEKKCSFALCYCPAPNCNYAGVYKDLYSH
FT YAANHKKLWTR -> CDNGHVACSSCCIELRYKCPSCSLPIGNYRCIIMEKVVKAIIVP
FT CQTPKWLHRDILLWQRVSP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027589"
FT VAR_SEQ 238..366
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027590"
SQ SEQUENCE 366 AA; 40788 MW; 93AD2D38EF0B3A5C CRC64;
MVKGTNAEQA LAREEASSSR PKRQRVPSIV EEEGENGGGD VVVRSGTLFE LDLLDCPICC
NALTIPIFQC DKGHIACSSC CTNVSNKCPY CSLAIGNYRS RIMERVVEAF IVRCPIVAGE
ASSSRQKRLR VPSIDEENGE NGGRDVVVPS GTLSQLDLLD CPVCSKALKI SIFQQSLFLA
KRQNGCTETF SYGNELVHEK KCSFALCYCP APNCNYAGVY KDLYSHYAAN HKKLWTRFSC
GYSMHVCMDF ESKSLVLQQY SDGPLVVLQC FKEPPQGLFW TVNCIAPSAP GVGKFSYELS
YSTAGNTLTF RSSEMNRIQK VSFQTPEKDF MFIPEYILCP MGLYKGTYIC IRSLEEEEEE
EEDNED
