ORTH3_ARATH
ID ORTH3_ARATH Reviewed; 660 AA.
AC Q9FVS2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=E3 ubiquitin-protein ligase ORTHRUS 3;
DE EC=2.3.2.27;
DE AltName: Full=Protein VARIANT IN METHYLATION 5;
DE AltName: Full=RING-type E3 ubiquitin transferase ORTHRUS 3 {ECO:0000305};
GN Name=ORTH3; Synonyms=VIM5; OrderedLocusNames=At1g57800; ORFNames=F12K22.15;
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 GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18643997; DOI=10.1111/j.1365-313x.2008.03631.x;
RA Kraft E., Bostick M., Jacobsen S.E., Callis J.;
RT "ORTH/VIM proteins that regulate DNA methylation are functional ubiquitin
RT E3 ligases.";
RL Plant J. 56:704-715(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. May participate in CpG
CC methylation-dependent transcriptional regulation (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}.
CC -!- DOMAIN: The RING fingers are required for ubiquitin ligase activity.
CC {ECO:0000250}.
CC -!- DOMAIN: The YDG domain mediates the interaction with histone H3.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29230.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079732; AAG29230.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33468.1; -; Genomic_DNA.
DR PIR; D96612; D96612.
DR RefSeq; NP_176091.2; NM_104575.3.
DR AlphaFoldDB; Q9FVS2; -.
DR SMR; Q9FVS2; -.
DR STRING; 3702.AT1G57800.1; -.
DR PaxDb; Q9FVS2; -.
DR PRIDE; Q9FVS2; -.
DR ProteomicsDB; 248909; -.
DR EnsemblPlants; AT1G57800.1; AT1G57800.1; AT1G57800.
DR GeneID; 842155; -.
DR Gramene; AT1G57800.1; AT1G57800.1; AT1G57800.
DR KEGG; ath:AT1G57800; -.
DR Araport; AT1G57800; -.
DR TAIR; locus:2009425; AT1G57800.
DR eggNOG; ENOG502QRDQ; Eukaryota.
DR HOGENOM; CLU_016281_0_0_1; -.
DR InParanoid; Q9FVS2; -.
DR OMA; IQNPQVN; -.
DR PhylomeDB; Q9FVS2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FVS2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVS2; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0010428; F:methyl-CpNpG binding; ISS:UniProtKB.
DR GO; GO:0010429; F:methyl-CpNpN binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; ISS:UniProtKB.
DR GO; GO:0010216; P:maintenance of DNA methylation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.30.280.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; PTHR14140; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Chromatin regulator; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..660
FT /note="E3 ubiquitin-protein ligase ORTHRUS 3"
FT /id="PRO_0000396827"
FT DOMAIN 285..434
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT ZN_FING 12..63
FT /note="PHD-type"
FT ZN_FING 141..197
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 528..585
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 107..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..622
FT /evidence="ECO:0000255"
FT COMPBIAS 610..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73364 MW; 80944DE37D01CD34 CRC64;
MTPATQYPCD PEGVCMRCKS MPPPEESLTC GTCVTPWHVS CLLSPPETLS ATLQWLCPDC
SGETNPLPVS GVAAGYGSVG SDLVAAIHSI EADETLSAEE KAKKKQQLLS GKGVVDEDDE
EEKKKTSKGK KPIDVLSHFE CSFCMQSLQK PVSVRVLFAL ALMLVWFLES TPCGHNACLK
CFLKWMGQGH RSCGTCRSVI PESMVTNPRI NLSIVSAIRL ARVSEKADAR TSKVVHYVDN
EDRPDKAFTT ERAKKTGNAN ASSGKIFVTI PRDHFGPIPA ENDPVRNQGL LVGESWKGRL
ACRQWGAHFP HVSGIAGQAS YGAQSVVLAG GYDDDEDHGE WFLYTGSGGR ILKGNKRTNT
VQAFDQVFLN FNEALRLSCK LGYPVRVVRS TKDKRSPYAP QGGLLRYDGV YRIEKCWRIV
GIQMCRFLFV RCDNEPAPWT SDEHGDRPRP LPNVPELNMA TDLFERKESP SWDFDEGEDR
WRWMKPPPAS KKAVKNVLDP EERKLLREAI KSANPNTMRA RLLKEFKCQI CQKVMTNPVT
TPCAHNFCKA CLESKFAGTA LVRERGSGGR KLRSQKSVMK CPCCPTDIAE FVQNPQVNRE
VAEVIEKLKK QEEEENAKSL DEGQCSGTSH EEEDDEQPKK RIKLDTDAEV SATVVESDMK
