RHA1A_ARATH
ID RHA1A_ARATH Reviewed; 159 AA.
AC Q9SUS4; Q9ZT52;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable E3 ubiquitin-protein ligase RHA1A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger A1a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHA1a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHA1A {ECO:0000305};
GN Name=RHA1A {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At4g11370;
GN ORFNames=F8L21.160;
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], AND TISSUE SPECIFICITY.
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=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 [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].
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}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in stems.
CC {ECO:0000269|PubMed:9781696}.
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DR EMBL; AF078683; AAC68664.1; -; mRNA.
DR EMBL; AL096882; CAB51421.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81238.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83002.1; -; Genomic_DNA.
DR EMBL; AY086119; AAM63325.1; -; mRNA.
DR PIR; T13028; T13028.
DR PIR; T51840; T51840.
DR RefSeq; NP_192876.1; NM_117208.4.
DR AlphaFoldDB; Q9SUS4; -.
DR SMR; Q9SUS4; -.
DR BioGRID; 12038; 11.
DR IntAct; Q9SUS4; 10.
DR STRING; 3702.AT4G11370.1; -.
DR PaxDb; Q9SUS4; -.
DR PRIDE; Q9SUS4; -.
DR EnsemblPlants; AT4G11370.1; AT4G11370.1; AT4G11370.
DR GeneID; 826739; -.
DR Gramene; AT4G11370.1; AT4G11370.1; AT4G11370.
DR KEGG; ath:AT4G11370; -.
DR Araport; AT4G11370; -.
DR TAIR; locus:2128303; AT4G11370.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_18_2_1; -.
DR InParanoid; Q9SUS4; -.
DR OMA; FPIGYWD; -.
DR OrthoDB; 472012at2759; -.
DR PhylomeDB; Q9SUS4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SUS4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUS4; baseline and differential.
DR Genevisible; Q9SUS4; AT.
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; 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 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="Probable E3 ubiquitin-protein ligase RHA1A"
FT /id="PRO_0000056033"
FT ZN_FING 86..130
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 15
FT /note="S -> G (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="I -> M (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="R -> S (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="A -> G (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="L -> P (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Y -> H (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="S -> C (in Ref. 1; AAC68664 and 4; AAM63325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18309 MW; 10E928A3976E4215 CRC64;
MGLPEDFITE LQIPSYILKI LYVIGFFRDI VDALCPYIGL PRFLDHNETS APDLTRHALS
TSASLANELI PVVRFSDLPT DPEDCCTVCL SDFESDDKVR QLPKCGHVFH HYCLDRWIVD
YNKMKCPVCR HRFLPKEKYT QSDWGSGSDW FSDEVESTN
