SINL5_ARATH
ID SINL5_ARATH Reviewed; 328 AA.
AC Q7XA77; Q9C511;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=E3 ubiquitin-protein ligase SINA-like 5;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SINA-like 5 {ECO:0000305};
DE AltName: Full=Seven in absentia-like protein 5;
GN OrderedLocusNames=At1g66660; ORFNames=F4N21_20, T12I7.11;
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;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7XA77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7XA77-2; Sequence=VSP_027591, VSP_027592;
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=AAG51171.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG60077.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013288; AAG60077.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079285; AAG51171.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34541.1; -; Genomic_DNA.
DR EMBL; BT010157; AAQ22626.1; -; mRNA.
DR RefSeq; NP_176839.2; NM_105337.2. [Q7XA77-2]
DR AlphaFoldDB; Q7XA77; -.
DR STRING; 3702.AT1G66660.2; -.
DR PRIDE; Q7XA77; -.
DR EnsemblPlants; AT1G66660.1; AT1G66660.1; AT1G66660. [Q7XA77-2]
DR EnsemblPlants; AT1G66660.2; AT1G66660.2; AT1G66660.
DR GeneID; 842984; -.
DR Gramene; AT1G66660.1; AT1G66660.1; AT1G66660. [Q7XA77-2]
DR Gramene; AT1G66660.2; AT1G66660.2; AT1G66660.
DR KEGG; ath:AT1G66660; -.
DR Araport; AT1G66660; -.
DR eggNOG; KOG3002; Eukaryota.
DR InParanoid; Q7XA77; -.
DR PhylomeDB; Q7XA77; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7XA77; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7XA77; 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 Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..328
FT /note="E3 ubiquitin-protein ligase SINA-like 5"
FT /id="PRO_0000299194"
FT ZN_FING 86..122
FT /note="RING-type; degenerate"
FT ZN_FING 139..197
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..324
FT /note="SBD"
FT /evidence="ECO:0000250"
FT COMPBIAS 13..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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="1"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_027591"
FT VAR_SEQ 105..121
FT /note="LACSSCCQKLNKKCSFC -> MFSIVLLVVNHSRDQSI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_027592"
SQ SEQUENCE 328 AA; 37320 MW; 4923E529C2F7EA71 CRC64;
MARSGGNDGH EEELDPELFE EPSNLEGYED GEFEEDEEEF EEEEEELEEE EDEEEEEEEN
VTTDEQSGSP KSSQPVKLQS SDVLDCPTCC EPLKRPIYQC SNGHLACSSC CQKLNKKCSF
CRCNIGDIRC RAMEKVIEAS IVPCPNAKHG CKETTTYCNQ SSHEKVCKFV RCSCPVSNCN
YVSSYSNLKS HACSTAHVWG EDDIHFQLVI DRPRIFNMNL GRKKTVVFKE EKEGDLIVVQ
AFKGLEGVYV TVNRIAHMAP GIRDLSCSLA KLNEYSTLRS GSLVKKIQKV REKMHLEDDL
MWIPPKMLSG DHWKMQICIA YGYKFIHI
