ORTHL_ARATH
ID ORTHL_ARATH Reviewed; 465 AA.
AC Q681I0; O22280; O81463; Q500W6; Q709F3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase ORTHRUS-LIKE 1;
DE Short=ORTH-LIKE 1;
DE EC=2.3.2.27;
DE AltName: Full=Protein VARIANT IN METHYLATION 6;
DE AltName: Full=RING-type E3 ubiquitin transferase ORTHRUS-LIKE 1 {ECO:0000305};
GN Name=ORTHL; Synonyms=ORL1, VIM6; OrderedLocusNames=At4g08590;
GN ORFNames=T15F16.7, T3F12.10;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 284-464 (ISOFORMS 1/2).
RX PubMed=15208421; DOI=10.1104/pp.104.040030;
RA Boivin K., Acarkan A., Mbulu R.S., Clarenz O., Schmidt R.;
RT "The Arabidopsis genome sequence as a tool for genome analysis in the
RT Brassicaceae: a comparison of the Arabidopsis thaliana and Capsella rubella
RT genomes.";
RL Plant Physiol. 135:735-744(2004).
RN [6]
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 [7]
RP FUNCTION, 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 methylation-
CC dependent transcriptional regulation. Mediates ubiquitination with the
CC E2 ubiquitin-conjugating enzyme UBC11. {ECO:0000269|PubMed:18643997}.
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 Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q681I0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q681I0-2; Sequence=VSP_039619;
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=AAB81879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC28190.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002983; AAB81879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF076275; AAC28190.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161512; CAB77984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82661.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82662.1; -; Genomic_DNA.
DR EMBL; AK175637; BAD43400.1; -; mRNA.
DR EMBL; BT022101; AAY34162.1; -; mRNA.
DR EMBL; AJ608275; CAE55215.1; -; mRNA.
DR PIR; T00949; T00949.
DR PIR; T01825; T01825.
DR RefSeq; NP_001078357.1; NM_001084888.1. [Q681I0-2]
DR RefSeq; NP_192599.2; NM_116928.4. [Q681I0-1]
DR AlphaFoldDB; Q681I0; -.
DR SMR; Q681I0; -.
DR BioGRID; 11720; 1.
DR STRING; 3702.AT4G08590.1; -.
DR PaxDb; Q681I0; -.
DR PRIDE; Q681I0; -.
DR ProteomicsDB; 226034; -. [Q681I0-1]
DR EnsemblPlants; AT4G08590.1; AT4G08590.1; AT4G08590. [Q681I0-1]
DR EnsemblPlants; AT4G08590.2; AT4G08590.2; AT4G08590. [Q681I0-2]
DR GeneID; 826420; -.
DR Gramene; AT4G08590.1; AT4G08590.1; AT4G08590. [Q681I0-1]
DR Gramene; AT4G08590.2; AT4G08590.2; AT4G08590. [Q681I0-2]
DR KEGG; ath:AT4G08590; -.
DR Araport; AT4G08590; -.
DR TAIR; locus:2138591; AT4G08590.
DR eggNOG; ENOG502QSQ8; Eukaryota.
DR HOGENOM; CLU_016281_1_0_1; -.
DR InParanoid; Q681I0; -.
DR OMA; MINNPRI; -.
DR OrthoDB; 1305843at2759; -.
DR PhylomeDB; Q681I0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q681I0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q681I0; baseline and differential.
DR Genevisible; Q681I0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:TAIR.
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; IDA:TAIR.
DR Gene3D; 2.30.280.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14140; PTHR14140; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..465
FT /note="E3 ubiquitin-protein ligase ORTHRUS-LIKE 1"
FT /id="PRO_0000396830"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 233..374
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT ZN_FING 109..148
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 31..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_039619"
SQ SEQUENCE 465 AA; 52308 MW; BA501A2D3BFF8150 CRC64;
MTRVNQLPCD CVSTAEESLT SGTCITPTHV TSLSSPLDRS GDVDPLPVSD ESGGSKADES
MTDADETKKR KRILSGDCEA DENNKSDGEI ASLNDGVDAF TAICEDLNCS LCNQLPDRPV
TILCGHNFCL KCFDKWIDQG NQICATCRST IPDKMAANPR VNSSLVSVIR YVKVAKTAGV
GTANFFPFTS NQDGPENAFR TKRAKIGEEN AARIYVTVPF DHFGPIPAEH DPVRNQGVLV
GESWENRVEC RQWGVHLPHV SCIAGQEDYG AQSVVISGGY KDDEDHGEWF LYTGRSRGRH
FANEDQEFED LNEALRVSCE MGYPVRVVRS YKDRYSAYAP KEGVRYDGVY RIEKCWRKAR
FPDSFKVCRY LFVRCDNEPA PWNSDESGDR PRPLPNIPEL ETASDLFERK ESPSWDFDEA
EGRWRWMKPP PANHEQRERM KMAMTCLLLF VLIILVGSSS ILYQY
