RF298_ARATH
ID RF298_ARATH Reviewed; 814 AA.
AC Q0WPJ7; Q0WVX7; Q9ZT97;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Putative E3 ubiquitin-protein ligase RF298;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 298;
DE AltName: Full=RING-type E3 ubiquitin transferase RF298 {ECO:0000305};
GN Name=RF298; OrderedLocusNames=At4g03000; ORFNames=T4I9.12;
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].
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 (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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 -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF069442; AAC79106.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161495; CAB77785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82258.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82259.1; -; Genomic_DNA.
DR EMBL; AK226608; BAE98721.1; -; mRNA.
DR EMBL; AK229071; BAF00952.1; -; mRNA.
DR PIR; T01393; T01393.
DR RefSeq; NP_192209.2; NM_116534.5.
DR RefSeq; NP_974504.1; NM_202775.1.
DR AlphaFoldDB; Q0WPJ7; -.
DR SMR; Q0WPJ7; -.
DR iPTMnet; Q0WPJ7; -.
DR PaxDb; Q0WPJ7; -.
DR PRIDE; Q0WPJ7; -.
DR ProteomicsDB; 236892; -.
DR EnsemblPlants; AT4G03000.1; AT4G03000.1; AT4G03000.
DR EnsemblPlants; AT4G03000.2; AT4G03000.2; AT4G03000.
DR GeneID; 828112; -.
DR Gramene; AT4G03000.1; AT4G03000.1; AT4G03000.
DR Gramene; AT4G03000.2; AT4G03000.2; AT4G03000.
DR KEGG; ath:AT4G03000; -.
DR Araport; AT4G03000; -.
DR TAIR; locus:2139310; AT4G03000.
DR eggNOG; ENOG502SB0J; Eukaryota.
DR HOGENOM; CLU_012143_0_1_1; -.
DR InParanoid; Q0WPJ7; -.
DR OMA; ICARFAK; -.
DR OrthoDB; 259830at2759; -.
DR PhylomeDB; Q0WPJ7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q0WPJ7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WPJ7; baseline and differential.
DR Genevisible; Q0WPJ7; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..814
FT /note="Putative E3 ubiquitin-protein ligase RF298"
FT /id="PRO_0000395978"
FT ZN_FING 760..800
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 506..710
FT /evidence="ECO:0000255"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 90159 MW; 1CE9CDBBE739FF13 CRC64;
MVEKQEEMNE FGAVNGGKVG TSSSVSPPQD KGRKNKRKLA DPSPQNAASL TEFPRYELHS
FKSQSPLCEN DSNGQLKAEE SDSVGWDDPF ACHLEGLLSS NLLTLFRSAM NQIMDCGYSE
DVVLKAISSS RFYCGGTDLV SNIVNDTLSF LKSGKKVAGS RDYVFEDLQQ LVAYSLVEKI
SLVREVRPSL STDEAMWRLL ICDLNVLKAF EVDADGLEGS SVSNASKSSE SPVAECNPPK
SSDADNPKAP VSNTQSKQSE PVKFGNFANV NNSKNPHASG ATPGKEVFSV STASGEGTKS
ASLTSVSDEK LVSCRKGRTK KEMAMLRQKS CVEKIRTYSK GGGYKTAKFG GFLVEKRGKS
ASDLLSAQAR NSSSKITTEV MKIPLAESSS TLSNSTKSDS PALDVKEHVT ALPANNAPAP
VASEKKSGSE PEEKPSVSTK PAPDYYAAIP YDATLGIYIP RNKRDELILK LVPRMKDLQK
ELQDWTDWAN QKVKQATVRL LKDQPELKAL RKEKEEAEEF RKEKQLLEEN TIKRRSEMEL
ALNNATNQLE RTNNTIRRLE LEQSLLKRER EAANIRASES AESCREAKER VQRLLKNSQS
WEGQKNLLQE ELKSQRDKVA GLQQEVAKAK TRQNQIEATW KQEKSATGKL TAQAAALKKE
RGKLEELGKA EEERIKTKAE NDVKYYIENI KRLDTEISKL KLKSDSLKIA ALKKGIDGNN
DGNKSGMNHT TNTKANSMAS AKVWENNQGA ESKIKREREC VMCLSEEMSV IFLPCAHQVL
CSKCNQLHEK EAMEDCPSCR AKIQRRIQAR FARG
