RMA2_ARATH
ID RMA2_ARATH Reviewed; 193 AA.
AC P93030;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=E3 ubiquitin-protein ligase RMA2;
DE EC=2.3.2.27;
DE AltName: Full=Protein RING membrane-anchor 2;
DE AltName: Full=RING-type E3 ubiquitin transferase RMA2 {ECO:0000305};
GN Name=RMA2; Synonyms=A-RZF; OrderedLocusNames=At4g28270; ORFNames=F26K10.15;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9322769; DOI=10.1016/s0378-1119(97)00258-8;
RA Zou J., Taylor D.C.;
RT "Cloning and molecular characterization of an Arabidopsis thaliana RING
RT zinc finger gene expressed preferentially during seed development.";
RL Gene 196:291-295(1997).
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].
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].
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 [6]
RP FUNCTION, MUTAGENESIS OF CYS-36, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19224217; DOI=10.1007/s00299-009-0680-8;
RA Son O., Cho S.K., Kim E.Y., Kim W.T.;
RT "Characterization of three Arabidopsis homologs of human RING membrane
RT anchor E3 ubiquitin ligase.";
RL Plant Cell Rep. 28:561-569(2009).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=19234086; DOI=10.1105/tpc.108.061994;
RA Lee H.K., Cho S.K., Son O., Xu Z., Hwang I., Kim W.T.;
RT "Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin ligase
RT homolog, regulates aquaporin levels via ubiquitination in transgenic
RT Arabidopsis plants.";
RL Plant Cell 21:622-641(2009).
RN [8]
RP FUNCTION, AND INTERACTION WITH ERABP1.
RX PubMed=20152813; DOI=10.1016/j.bbrc.2010.02.032;
RA Son O., Cho S.K., Kim S.J., Kim W.T.;
RT "In vitro and in vivo interaction of AtRma2 E3 ubiquitin ligase and auxin-
RT binding protein 1.";
RL Biochem. Biophys. Res. Commun. 393:492-497(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC and proteasomal degradation of the auxin-binding protein ERABP1.
CC {ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:20152813}.
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 -!- SUBUNIT: Interacts with ERABP1. {ECO:0000269|PubMed:20152813}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19224217}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:19224217}.
CC -!- TISSUE SPECIFICITY: Barely detected in roots and limited to the root
CC tips. Expressed in leaf hydathodes and in siliques.
CC {ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:9322769}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed development.
CC {ECO:0000269|PubMed:9322769}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on drought
CC stress response, probably due to the redundancy with RMA1 and RMA3.
CC {ECO:0000269|PubMed:19234086}.
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DR EMBL; U81598; AAC49830.1; -; Genomic_DNA.
DR EMBL; AL161572; CAB79629.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85462.1; -; Genomic_DNA.
DR EMBL; BT003053; AAO23618.1; -; mRNA.
DR EMBL; AK227310; BAE99326.1; -; mRNA.
DR PIR; T09043; T09043.
DR RefSeq; NP_194556.1; NM_118967.3.
DR AlphaFoldDB; P93030; -.
DR BioGRID; 14229; 2.
DR IntAct; P93030; 1.
DR STRING; 3702.AT4G28270.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; P93030; -.
DR PRIDE; P93030; -.
DR ProteomicsDB; 227983; -.
DR EnsemblPlants; AT4G28270.1; AT4G28270.1; AT4G28270.
DR GeneID; 828942; -.
DR Gramene; AT4G28270.1; AT4G28270.1; AT4G28270.
DR KEGG; ath:AT4G28270; -.
DR Araport; AT4G28270; -.
DR TAIR; locus:2123663; AT4G28270.
DR eggNOG; KOG0823; Eukaryota.
DR HOGENOM; CLU_055198_1_2_1; -.
DR InParanoid; P93030; -.
DR OMA; KREPPKC; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; P93030; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:P93030; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P93030; baseline and differential.
DR Genevisible; P93030; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; PTHR12313; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..193
FT /note="E3 ubiquitin-protein ligase RMA2"
FT /id="PRO_0000395674"
FT TRANSMEM 175..192
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT ZN_FING 21..75
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 36
FT /note="C->S: Strong reduction of ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19224217"
SQ SEQUENCE 193 AA; 22178 MW; 8D2AE01F6984CD88 CRC64;
MEIEKDEDDT TLVDSGGDFD CNICLDQVRD PVVTLCGHLF CWPCIHKWTY ASNNSRQRVD
QYDHKREPPK CPVCKSDVSE ATLVPIYGRG QKAPQSGSNV PSRPTGPVYD LRGVGQRLGE
GESQRYMYRM PDPVMGVVCE MVYRRLFGES SSNMAPYRDM NVRSRRRAMQ AEESLSRVYL
FLLCFMFMCL FLF
