MBR2_ARATH
ID MBR2_ARATH Reviewed; 666 AA.
AC O49500;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=E3 ubiquitin-protein ligase MBR2;
DE EC=2.3.2.27;
DE AltName: Full=HAL3-interacting protein 1 homolog;
DE Short=AtHIP1;
DE AltName: Full=MED25-binding RING-H2 protein 2;
DE AltName: Full=RING-H2 finger MBR2;
DE AltName: Full=RING-type E3 ubiquitin transferase MBR2 {ECO:0000305};
GN Name=MBR2; Synonyms=HIP1; OrderedLocusNames=At4g34040;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=19543273; DOI=10.1038/ncb1892;
RA Sun S.Y., Chao D.Y., Li X.M., Shi M., Gao J.P., Zhu M.Z., Yang H.Q.,
RA Luan S., Lin H.X.;
RT "OsHAL3 mediates a new pathway in the light-regulated growth of rice.";
RL Nat. Cell Biol. 11:845-851(2009).
RN [6]
RP FUNCTION, INTERACTION WITH MED25 AND UBC11, MUTAGENESIS OF HIS-639 AND
RP HIS-642, AND DISRUPTION PHENOTYPE.
RX PubMed=22992513; DOI=10.1104/pp.112.205500;
RA Inigo S., Giraldez A.N., Chory J., Cerdan P.D.;
RT "Proteasome-mediated turnover of Arabidopsis MED25 is coupled to the
RT activation of FLOWERING LOCUS T transcription.";
RL Plant Physiol. 160:1662-1673(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that functions as regulator of
CC MED25 stability by targeting MED25 for degradation in a RING-H2-
CC dependent way. Proteasome-dependent degradation of MED25 seems to
CC activate its function as positive regulator of FLOWERING LOCUS T (FT)
CC and is important to induce the expression of FT and consequently to
CC promote flowering. May function downstream of HAL3 and be required for
CC HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the
CC degradation of cell cycle suppressors, resulting in enhancement of cell
CC division and plant growth. {ECO:0000269|PubMed:19543273,
CC ECO:0000269|PubMed:22992513}.
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 MED25 and UBC11. {ECO:0000269|PubMed:22992513}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants mbr1-1 and mbr2-1 show delayed
CC flowering. {ECO:0000269|PubMed:22992513}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. {ECO:0000305}.
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DR EMBL; AL021961; CAA17568.1; -; Genomic_DNA.
DR EMBL; AL161584; CAB80121.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86313.1; -; Genomic_DNA.
DR EMBL; BT015366; AAU05489.1; -; mRNA.
DR EMBL; BT020341; AAV85696.1; -; mRNA.
DR EMBL; AK229265; BAF01129.1; -; mRNA.
DR PIR; T05432; T05432.
DR RefSeq; NP_195130.1; NM_119565.4.
DR AlphaFoldDB; O49500; -.
DR SMR; O49500; -.
DR BioGRID; 14832; 1.
DR STRING; 3702.AT4G34040.1; -.
DR iPTMnet; O49500; -.
DR PaxDb; O49500; -.
DR PRIDE; O49500; -.
DR ProteomicsDB; 238356; -.
DR EnsemblPlants; AT4G34040.1; AT4G34040.1; AT4G34040.
DR GeneID; 829550; -.
DR Gramene; AT4G34040.1; AT4G34040.1; AT4G34040.
DR KEGG; ath:AT4G34040; -.
DR Araport; AT4G34040; -.
DR TAIR; locus:2124271; AT4G34040.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_024479_0_0_1; -.
DR InParanoid; O49500; -.
DR OMA; DMEPCCV; -.
DR OrthoDB; 301445at2759; -.
DR PhylomeDB; O49500; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O49500; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49500; baseline and differential.
DR Genevisible; O49500; 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:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; PTHR22937; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Flowering; Growth regulation; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..666
FT /note="E3 ubiquitin-protein ligase MBR2"
FT /id="PRO_0000429417"
FT ZN_FING 619..660
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 639
FT /note="H->A: Unable to promote MED25 degradation; when
FT associated with A-642."
FT /evidence="ECO:0000269|PubMed:22992513"
FT MUTAGEN 642
FT /note="H->A: Unable to promote MED25 degradation; when
FT associated with A-639."
FT /evidence="ECO:0000269|PubMed:22992513"
SQ SEQUENCE 666 AA; 71539 MW; 6A6794EC7275BFBB CRC64;
MQGPRSTGDS STGINYADGE PICSTNSETT SNNILNPVDV QFPNNTTGSG RPTYASSSSH
VVQNHNWWSF GESSSRLGPS DHLNSNGSKT DRQLLSDGYG FEEGQSGMLL PGESFLRGSS
SSHMLSHVNL GKDMDIGSGL QTSGVVIRHN NCETSLGSSS QTAEERSSGP GSSLGGLGSS
CKRKALEGAP SHSFPGESHG CFFQTENGAW NEGLAQYDAS SSLSLSMPSQ NSPNVNNQSG
LPEPRFGLGG GRAVTASAFP STRSTETISR PGRRLNPGQP PESVAFSFTQ SGSSVRQQQQ
LPATSPFVDP LDARAIPVTG SSSSGDGQPS MIHLPALTRN IHQFAWSASS SSRANSMPEE
GLSPWDAPRI NSEQPVFTTP ANETRNPVQD QFCWSFTRGN PSTSGDSPFV PRAGSSSGIH
GLQPNPTWVT PHNQSRISEV APWSLFPSIE SESATHGASL PLLPTGPSVS SNEAAAPSGS
SSRSHRSRQR RSGLLLERQN DHLHLRHLGR SLAADNDGRN RLISEIRQVL SAMRRGENLR
FEDYMVFDPL IYQGMAEMHD RHRDMRLDVD NMSYEELLAL GERIGDVSTG LSEEVILKVM
KQHKHTSSAA GSHQDMEPCC VCQEEYAEGD DLGTLGCGHE FHTACVKQWL MLKNLCPICK
TVALST
