RHC2A_ARATH
ID RHC2A_ARATH Reviewed; 401 AA.
AC O22283;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHC2A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger C2a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHC2a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHC2A {ECO:0000305};
GN Name=RHC2A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At2g39720 {ECO:0000312|Araport:AT2G39720};
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).
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.
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; AF079186; AAC69860.1; -; mRNA.
DR EMBL; AC003000; AAB87121.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09711.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62301.1; -; Genomic_DNA.
DR EMBL; AY074579; AAL67118.1; -; mRNA.
DR EMBL; AY094016; AAM16172.1; -; mRNA.
DR EMBL; AY086492; AAM67317.1; -; mRNA.
DR PIR; T01001; T01001.
DR RefSeq; NP_001318385.1; NM_001336792.1.
DR RefSeq; NP_030517.1; NM_129529.4.
DR AlphaFoldDB; O22283; -.
DR SMR; O22283; -.
DR STRING; 3702.AT2G39720.1; -.
DR PaxDb; O22283; -.
DR PRIDE; O22283; -.
DR ProteomicsDB; 236904; -.
DR EnsemblPlants; AT2G39720.1; AT2G39720.1; AT2G39720.
DR EnsemblPlants; AT2G39720.2; AT2G39720.2; AT2G39720.
DR GeneID; 818556; -.
DR Gramene; AT2G39720.1; AT2G39720.1; AT2G39720.
DR Gramene; AT2G39720.2; AT2G39720.2; AT2G39720.
DR KEGG; ath:AT2G39720; -.
DR Araport; AT2G39720; -.
DR TAIR; locus:2063912; AT2G39720.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040377_0_0_1; -.
DR InParanoid; O22283; -.
DR OMA; THIHNEL; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; O22283; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O22283; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22283; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010543; DUF1117.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF06547; DUF1117; 1.
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 Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..401
FT /note="Probable E3 ubiquitin-protein ligase RHC2A"
FT /id="PRO_0000436416"
FT ZN_FING 201..242
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 41..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43109 MW; 5F9AA704D46B641F CRC64;
MASGSYWCYS CSRFVWVSDS ISCPDCDGGF LELIQEPLDF TPSDSFTTTT TTQHRSPTRF
PPPSSSSSTP SASMHADNSP TPTIVTRTRS NRSPNPVIVL RGSAAAPSSD VVSEGLDRSA
FQMYYDDGTD SGLRPLPPSM TEFLLGSGFD RLLDQISQIE LNTNRNLRSC EHPPASKSAI
EALPLIEIDP THLLSDSQSH CAVCKENFVL KSSAREMPCN HIYHPDCILP WLAIRNSCPV
CRHELPAEDL TDGTGAALTA VTATAEEEED SAAGLTIWRL PGGGFAVGRI PGGWRGGDRM
MPVVYTEVDG GRLGDERLPR RVAWGSRRGG RDGGGSRERG GGFAGRIMRL FGCFSGSSGS
IAAAAAASSG SGSRIRVTRR TRSFSMFSTA SSSSRRRNWL A
