ORTH4_ARATH
ID ORTH4_ARATH Reviewed; 622 AA.
AC Q9C8E1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative E3 ubiquitin-protein ligase ORTHRUS 4;
DE EC=2.3.2.27;
DE AltName: Full=Protein VARIANT IN METHYLATION 4;
DE AltName: Full=RING-type E3 ubiquitin transferase ORTHRUS 4 {ECO:0000305};
GN Name=ORTH4; Synonyms=VIM4; OrderedLocusNames=At1g66040; ORFNames=F15E12.8;
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}.
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DR EMBL; AC026480; AAG51294.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34454.1; -; Genomic_DNA.
DR PIR; H96684; H96684.
DR RefSeq; NP_176778.1; NM_105275.2.
DR AlphaFoldDB; Q9C8E1; -.
DR SMR; Q9C8E1; -.
DR STRING; 3702.AT1G66040.1; -.
DR iPTMnet; Q9C8E1; -.
DR PaxDb; Q9C8E1; -.
DR PRIDE; Q9C8E1; -.
DR EnsemblPlants; AT1G66040.1; AT1G66040.1; AT1G66040.
DR GeneID; 842917; -.
DR Gramene; AT1G66040.1; AT1G66040.1; AT1G66040.
DR KEGG; ath:AT1G66040; -.
DR Araport; AT1G66040; -.
DR TAIR; locus:2013800; AT1G66040.
DR eggNOG; ENOG502QRDQ; Eukaryota.
DR HOGENOM; CLU_016281_0_0_1; -.
DR InParanoid; Q9C8E1; -.
DR OMA; TDMTERK; -.
DR OrthoDB; 1469576at2759; -.
DR PhylomeDB; Q9C8E1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9C8E1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8E1; baseline and differential.
DR Genevisible; Q9C8E1; AT.
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; 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; 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..622
FT /note="Putative E3 ubiquitin-protein ligase ORTHRUS 4"
FT /id="PRO_0000396828"
FT DOMAIN 258..407
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT ZN_FING 12..62
FT /note="PHD-type"
FT ZN_FING 129..169
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 498..555
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 579..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..602
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 68663 MW; 0D7FB9B699D642A9 CRC64;
MAIQTQLPCD GDGVCMRCQV TPPSEETLTC GTCVTPWHVS CLLPESLASS TGDWECPDCS
GVVVPSAAPG TGISGPESSG SVLVAAIRAI QADVTLTEAE KAKKRQRLMS GGGDDGVDDE
EKKKLEIFCS ICIQLPERPV TTPCGHNFCL KCFEKWAVGQ GKLTCMICRS KIPRHVAKNP
RINLALVSAI RLANVTKCSG EATAAKVHHI IRNQDRPDKA FTTERAVKTG KANAASGKFF
VTIPRDHFGP IPAANDVTRN QGVLVGESWE DRQECRQWGV HFPHVAGIAG QAAVGAQSVA
LSGGYDDDED HGEWFLYTGS GGRDLSGNKR VNKIQSSDQA FKNMNEALRL SCKMGYPVRV
VRSWKEKRSA YAPAEGVRYD GVYRIEKCWS NVGVQGLHKM CRYLFVRCDN EPAPWTSDEH
GDRPRPLPDV PELENATDLF VRKESPSWGF DEAEGRWKWM KSPPVSRMAL DTEERKKNKR
AKKGNNAMKA RLLKEFSCQI CRKVLSLPVT TPCAHNFCKA CLEAKFAGIT QLRDRSNGVR
KLRAKKNIMT CPCCTTDLSE FLQNPQVNRE MMEIIENFKK SEEEAEVAES SNISEEEEEE
SEPPTKKIKM DNNSVGDTSL SA
