RHC1A_ARATH
ID RHC1A_ARATH Reviewed; 328 AA.
AC O22197;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHC1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger C1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHC1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHC1A {ECO:0000305};
GN Name=RHC1A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At2g40830 {ECO:0000312|Araport:AT2G40830};
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 [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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).
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}.
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DR EMBL; AF079180; AAC69854.1; -; mRNA.
DR EMBL; AC002409; AAB86443.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09886.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09887.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09888.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62005.1; -; Genomic_DNA.
DR EMBL; AY139987; AAM98130.1; -; mRNA.
DR EMBL; BT008726; AAP42739.1; -; mRNA.
DR PIR; T00747; T00747.
DR RefSeq; NP_001324188.1; NM_001336872.1.
DR RefSeq; NP_565942.1; NM_129646.5.
DR RefSeq; NP_973651.1; NM_201922.3.
DR RefSeq; NP_973652.1; NM_201923.4.
DR AlphaFoldDB; O22197; -.
DR SMR; O22197; -.
DR STRING; 3702.AT2G40830.2; -.
DR PaxDb; O22197; -.
DR PRIDE; O22197; -.
DR ProteomicsDB; 236932; -.
DR EnsemblPlants; AT2G40830.1; AT2G40830.1; AT2G40830.
DR EnsemblPlants; AT2G40830.2; AT2G40830.2; AT2G40830.
DR EnsemblPlants; AT2G40830.3; AT2G40830.3; AT2G40830.
DR EnsemblPlants; AT2G40830.4; AT2G40830.4; AT2G40830.
DR GeneID; 818680; -.
DR Gramene; AT2G40830.1; AT2G40830.1; AT2G40830.
DR Gramene; AT2G40830.2; AT2G40830.2; AT2G40830.
DR Gramene; AT2G40830.3; AT2G40830.3; AT2G40830.
DR Gramene; AT2G40830.4; AT2G40830.4; AT2G40830.
DR KEGG; ath:AT2G40830; -.
DR Araport; AT2G40830; -.
DR TAIR; locus:2058465; AT2G40830.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034892_1_2_1; -.
DR InParanoid; O22197; -.
DR OMA; AQTDSNP; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; O22197; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O22197; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22197; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8LPN7"
FT CHAIN 2..328
FT /note="Probable E3 ubiquitin-protein ligase RHC1A"
FT /id="PRO_0000436415"
FT ZN_FING 190..231
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 233..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LPN7"
SQ SEQUENCE 328 AA; 36577 MW; 1DB0EF6486F55437 CRC64;
MSSSRNTHWC HRCQRAVRLH GQEPVCFYCG GGFVEELDMA QASPFDMFRS HRGVVERDQT
FDLMDAFSVF MRNRLAERSH DREIRGRTIS SGPENFPGLA PLLIFGGQVP YRLTGDNAVE
ALFNGGSPGI GITRGNTGDY FFGPGLEELF EQLSAGTTRR GPPPAPRSAI DALPTIKIAQ
RHLRSSDSNC PVCKDEFELG SEAKQMPCNH IYHSDCIVPW LVQHNSCPVC RQELPSASGP
SSSQNRTTPT RNYRSSSSSS SSNSRENGNE RRNPFSSFWP FRSSGSSSSS TQNRGGTRNS
DTSDENHNYH QQQHQQSYMG YSGWPFDY
