RMA3_ARATH
ID RMA3_ARATH Reviewed; 243 AA.
AC Q8GUK7; Q9SZS2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase RMA3;
DE EC=2.3.2.27;
DE AltName: Full=Protein RING membrane-anchor 3;
DE AltName: Full=RING-type E3 ubiquitin transferase RMA3 {ECO:0000305};
GN Name=RMA3; OrderedLocusNames=At4g27470; ORFNames=F27G19.70;
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 TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
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 FUNCTION, MUTAGENESIS OF CYS-59, 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 [6]
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000269|PubMed:19224217}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19224217}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:19224217}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in roots.
CC {ECO:0000269|PubMed:19224217}.
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 RMA2.
CC {ECO:0000269|PubMed:19234086}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81397.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ059124; AAY57610.1; -; mRNA.
DR EMBL; AL078467; CAB43879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81397.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85346.1; -; Genomic_DNA.
DR EMBL; BT002429; AAO00789.1; -; mRNA.
DR EMBL; BT006285; AAP13393.1; -; mRNA.
DR PIR; T08939; T08939.
DR RefSeq; NP_194477.2; NM_118882.3.
DR AlphaFoldDB; Q8GUK7; -.
DR STRING; 3702.AT4G27470.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q8GUK7; -.
DR PRIDE; Q8GUK7; -.
DR EnsemblPlants; AT4G27470.1; AT4G27470.1; AT4G27470.
DR GeneID; 828856; -.
DR Gramene; AT4G27470.1; AT4G27470.1; AT4G27470.
DR KEGG; ath:AT4G27470; -.
DR Araport; AT4G27470; -.
DR TAIR; locus:2124004; AT4G27470.
DR eggNOG; KOG0823; Eukaryota.
DR HOGENOM; CLU_055198_1_0_1; -.
DR InParanoid; Q8GUK7; -.
DR OMA; EMVLTRI; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q8GUK7; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GUK7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUK7; baseline and differential.
DR Genevisible; Q8GUK7; 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:0071456; P:cellular response to hypoxia; HEP: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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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..243
FT /note="E3 ubiquitin-protein ligase RMA3"
FT /id="PRO_0000395675"
FT TRANSMEM 223..243
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT ZN_FING 44..92
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 110..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 59
FT /note="C->S: Strong reduction of ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19224217"
SQ SEQUENCE 243 AA; 26984 MW; 707894C1C74D167B CRC64;
MEGNFFIRSD AQRAHDNGFI AKQKPNLTTA PTAGQANESG CFDCNICLDT AHDPVVTLCG
HLFCWPCIYK WLHVQLSSVS VDQHQNNCPV CKSNITITSL VPLYGRGMSS PSSTFGSKKQ
DALSTDIPRR PAPSALRNPI TSASSLNPSL QHQTLSPSFH NHQYSPRGFT TTESTDLANA
VMMSFLYPVI GMFGDLVYTR IFGTFTNTIA QPYQSQRMMQ REKSLNRVSI FFLCCIILCL
LLF
