RHY1A_ARATH
ID RHY1A_ARATH Reviewed; 250 AA.
AC Q852U6; Q8LD21; Q9C6C9; Q9ZT39;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHY1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger Y1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHY1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHY1A {ECO:0000305};
GN Name=RHY1A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At1g49850 {ECO:0000312|Araport:AT1G49850};
GN ORFNames=F10F5.8 {ECO:0000312|EMBL:AAG51778.1};
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].
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).
RN [4]
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-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-250.
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that may possess E3
CC ubiquitin ligase activity in vitro. {ECO:0000250|UniProtKB:Q9ZT50}.
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. {ECO:0000305}.
CC -!- INTERACTION:
CC Q852U6; Q17TI5: BRX; NbExp=4; IntAct=EBI-4428791, EBI-4426649;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51778.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079674; AAG51778.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32483.1; -; Genomic_DNA.
DR EMBL; BT004600; AAO42846.1; -; mRNA.
DR EMBL; AK227950; BAE99918.1; -; mRNA.
DR EMBL; AY086250; AAM64325.1; -; mRNA.
DR EMBL; AF079185; AAC69859.1; -; mRNA.
DR PIR; D96535; D96535.
DR PIR; T51856; T51856.
DR RefSeq; NP_564556.1; NM_103872.4.
DR AlphaFoldDB; Q852U6; -.
DR SMR; Q852U6; -.
DR IntAct; Q852U6; 32.
DR STRING; 3702.AT1G49850.1; -.
DR PaxDb; Q852U6; -.
DR PRIDE; Q852U6; -.
DR EnsemblPlants; AT1G49850.1; AT1G49850.1; AT1G49850.
DR GeneID; 841408; -.
DR Gramene; AT1G49850.1; AT1G49850.1; AT1G49850.
DR KEGG; ath:AT1G49850; -.
DR Araport; AT1G49850; -.
DR TAIR; locus:2007273; AT1G49850.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_066967_1_0_1; -.
DR InParanoid; Q852U6; -.
DR OMA; NASHREH; -.
DR OrthoDB; 1365955at2759; -.
DR PhylomeDB; Q852U6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q852U6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q852U6; baseline and differential.
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 Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..250
FT /note="Probable E3 ubiquitin-protein ligase RHY1A"
FT /id="PRO_0000436418"
FT ZN_FING 203..244
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 64
FT /note="L -> I (in Ref. 5; AAM64325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28447 MW; 6CA758A824172AA9 CRC64;
MTSASELFST RRSRPGRSDP ALESDTSSYR HHSHHHHRRH GVHHHNQRHD SDGCDPLRRP
TPRLRRFFHH PIQERSRPIR DVQGTSQYLN TDSTDTETQS SSFVNLNGSE RLPGAVLLAR
DRLFERLRGV SLSSNSRSNR VSLDDQRESS FHSIDGDPIF QLAGLQVTYE CNKKPQGLTQ
DAINCLHRQT FSSAEVKSEM RDCSICLESF TKGDMLISLP CTHSFHSSCL NPWLRACGDC
PCCRRAIAKE
