RMA1_ARATH
ID RMA1_ARATH Reviewed; 249 AA.
AC O64425;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase RMA1;
DE EC=2.3.2.27;
DE AltName: Full=Protein RING membrane-anchor 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RMA1 {ECO:0000305};
GN Name=RMA1; OrderedLocusNames=At4g03510; ORFNames=F9H3.14;
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], MUTAGENESIS OF CYS-63, AND TISSUE SPECIFICITY.
RX PubMed=9664717; DOI=10.1093/oxfordjournals.pcp.a029403;
RA Matsuda N., Nakano A.;
RT "RMA1, an Arabidopsis thaliana gene whose cDNA suppresses the yeast sec15
RT mutation, encodes a novel protein with a RING finger motif and a membrane
RT anchor.";
RL Plant Cell Physiol. 39:545-554(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].
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, AND SUBCELLULAR LOCATION.
RX PubMed=11329381; DOI=10.1242/jcs.114.10.1949;
RA Matsuda N., Suzuki T., Tanaka K., Nakano A.;
RT "Rma1, a novel type of RING finger protein conserved from Arabidopsis to
RT human, is a membrane-bound ubiquitin ligase.";
RL J. Cell Sci. 114:1949-1957(2001).
RN [6]
RP FUNCTION, MUTAGENESIS OF CYS-63, 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 FUNCTION, SUBCELLULAR LOCATION, AND 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 that promotes the ubiquitination
CC and proteasomal degradation of aquaporin PIP2-1. Forms a ubiquitin
CC ligase complex in cooperation with the E2 enzymes UCB8/UCB10.
CC {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217,
CC ECO:0000269|PubMed:19234086}.
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:11329381, ECO:0000269|PubMed:19224217,
CC ECO:0000269|PubMed:19234086}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217,
CC ECO:0000269|PubMed:19234086}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in roots.
CC {ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:9664717}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity.
CC -!- DOMAIN: The C-terminal transmembrane is dispensable for the ubiquitin
CC ligase activity in vitro, but is critical for correct subcellular
CC localization and substrate recognition in vivo.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on drought
CC stress response, probably due to the redundancy with RMA2 and RMA3.
CC {ECO:0000269|PubMed:19234086}.
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DR EMBL; AB008518; BAA28598.1; -; mRNA.
DR EMBL; AF071527; AAD11593.1; -; Genomic_DNA.
DR EMBL; AL161497; CAB77836.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82331.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82332.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67649.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67650.1; -; Genomic_DNA.
DR EMBL; BT003833; AAO41884.1; -; mRNA.
DR EMBL; BT005188; AAO50721.1; -; mRNA.
DR PIR; T52142; T52142.
DR RefSeq; NP_001319862.1; NM_001340463.1.
DR RefSeq; NP_001329467.1; NM_001340464.1.
DR RefSeq; NP_192260.1; NM_116589.3.
DR RefSeq; NP_974506.1; NM_202777.2.
DR AlphaFoldDB; O64425; -.
DR BioGRID; 10968; 1.
DR IntAct; O64425; 1.
DR STRING; 3702.AT4G03510.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; O64425; -.
DR PaxDb; O64425; -.
DR PRIDE; O64425; -.
DR EnsemblPlants; AT4G03510.1; AT4G03510.1; AT4G03510.
DR EnsemblPlants; AT4G03510.2; AT4G03510.2; AT4G03510.
DR EnsemblPlants; AT4G03510.3; AT4G03510.3; AT4G03510.
DR EnsemblPlants; AT4G03510.4; AT4G03510.4; AT4G03510.
DR GeneID; 825654; -.
DR Gramene; AT4G03510.1; AT4G03510.1; AT4G03510.
DR Gramene; AT4G03510.2; AT4G03510.2; AT4G03510.
DR Gramene; AT4G03510.3; AT4G03510.3; AT4G03510.
DR Gramene; AT4G03510.4; AT4G03510.4; AT4G03510.
DR KEGG; ath:AT4G03510; -.
DR Araport; AT4G03510; -.
DR TAIR; locus:2128746; AT4G03510.
DR eggNOG; KOG0823; Eukaryota.
DR HOGENOM; CLU_055198_1_0_1; -.
DR InParanoid; O64425; -.
DR OMA; MMVMVGE; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; O64425; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:O64425; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O64425; baseline and differential.
DR Genevisible; O64425; 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:0016020; C:membrane; IDA:TAIR.
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:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; PTHR12313; 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..249
FT /note="E3 ubiquitin-protein ligase RMA1"
FT /id="PRO_0000395673"
FT TRANSMEM 231..248
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT ZN_FING 48..97
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 63
FT /note="C->S: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:19224217,
FT ECO:0000269|PubMed:9664717"
SQ SEQUENCE 249 AA; 28012 MW; 0477C433BA96DE4D CRC64;
MALDQSFEDA ALLGELYGEG AFCFKSKKPE PITVSVPSDD TDDSNFDCNI CLDSVQEPVV
TLCGHLFCWP CIHKWLDVQS FSTSDEYQRH RQCPVCKSKV SHSTLVPLYG RGRCTTQEEG
KNSVPKRPVG PVYRLEMPNS PYASTDLRLS QRVHFNSPQE GYYPVSGVMS SNSLSYSAVL
DPVMVMVGEM VATRLFGTRV MDRFAYPDTY NLAGTSGPRM RRRIMQADKS LGRIFFFFMC
CVVLCLLLF
