MBR1_ARATH
ID MBR1_ARATH Reviewed; 704 AA.
AC Q9ZQF9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=E3 ubiquitin-protein ligase MBR1;
DE EC=2.3.2.27;
DE AltName: Full=MED25-binding RING-H2 protein 1;
DE AltName: Full=RING-H2 finger MBR1;
DE AltName: Full=RING-type E3 ubiquitin transferase MBR1 {ECO:0000305};
GN Name=MBR1; OrderedLocusNames=At2g15530; ORFNames=F9O13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, INTERACTION WITH MED25 AND UBC11, 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. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZQF9-1; Sequence=Displayed;
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; AC006248; AAD17397.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06411.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06412.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06413.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62927.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62928.1; -; Genomic_DNA.
DR EMBL; BX820346; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B84530; B84530.
DR RefSeq; NP_001118324.1; NM_001124852.5. [Q9ZQF9-1]
DR RefSeq; NP_001325050.1; NM_001335453.1. [Q9ZQF9-1]
DR RefSeq; NP_001325051.1; NM_001335455.1. [Q9ZQF9-1]
DR RefSeq; NP_179155.1; NM_127113.4. [Q9ZQF9-1]
DR RefSeq; NP_973470.1; NM_201741.2. [Q9ZQF9-1]
DR AlphaFoldDB; Q9ZQF9; -.
DR SMR; Q9ZQF9; -.
DR BioGRID; 1404; 1.
DR STRING; 3702.AT2G15530.4; -.
DR iPTMnet; Q9ZQF9; -.
DR PaxDb; Q9ZQF9; -.
DR ProteomicsDB; 238695; -. [Q9ZQF9-1]
DR EnsemblPlants; AT2G15530.1; AT2G15530.1; AT2G15530. [Q9ZQF9-1]
DR EnsemblPlants; AT2G15530.2; AT2G15530.2; AT2G15530. [Q9ZQF9-1]
DR EnsemblPlants; AT2G15530.3; AT2G15530.3; AT2G15530. [Q9ZQF9-1]
DR EnsemblPlants; AT2G15530.5; AT2G15530.5; AT2G15530. [Q9ZQF9-1]
DR EnsemblPlants; AT2G15530.7; AT2G15530.7; AT2G15530. [Q9ZQF9-1]
DR GeneID; 816045; -.
DR Gramene; AT2G15530.1; AT2G15530.1; AT2G15530. [Q9ZQF9-1]
DR Gramene; AT2G15530.2; AT2G15530.2; AT2G15530. [Q9ZQF9-1]
DR Gramene; AT2G15530.3; AT2G15530.3; AT2G15530. [Q9ZQF9-1]
DR Gramene; AT2G15530.5; AT2G15530.5; AT2G15530. [Q9ZQF9-1]
DR Gramene; AT2G15530.7; AT2G15530.7; AT2G15530. [Q9ZQF9-1]
DR KEGG; ath:AT2G15530; -.
DR Araport; AT2G15530; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_024479_0_0_1; -.
DR OMA; YMEPCCI; -.
DR PhylomeDB; Q9ZQF9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZQF9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQF9; baseline and differential.
DR Genevisible; Q9ZQF9; 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: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 Alternative splicing; Flowering; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..704
FT /note="E3 ubiquitin-protein ligase MBR1"
FT /id="PRO_0000429416"
FT ZN_FING 656..697
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 76019 MW; ABA3DE71D2A4626D CRC64;
MNPMQGPRSI GGSSTEVNQV DGESIYCTET SLNTMLNPAD TGFPNNSTPS GRPTYASSSS
HAAQDHTWWR FGESSSIPGP SDQVNSIGIK TSHQLPQDGT HHFVGYGSEG RQTGLNGMMV
DGGVHAGSHI RNVPSFLRGS SSNPMPQHVD MSMDMDSDNC NAQTSGVVIR HNSYGSSLGS
SVQAAGESSS GPASPFGGWG SSCKRKALEG SPSHYFSGET PNRIVQTENS ASHASLSQYG
ASSSLSLATP SQSSPNVTNH FGRTEQMFGS GGGRAVAASA FHSTRNTDTL SRAGRRLNPR
QPQESVAFSV SHGGTSVRPT GSLQQNLPLN SPFVDPPDVR SSSITSGSNT GENQTNIVHL
PALTRNIHQY AWDASFSSRA SNPSGIGMPA ERLGPQWETP RSNQEQPLFA PATDMRQPVH
DLWNFARGSP GSSVDSLFVP RAGPSSAIHT PQPNPTWIPP QNAPPHNPSR TSELSPWSLF
PSIESPSASH GGPLPLLPAG PSVSSNEVTM PSSSNSRSHR SRHRRSGLLL ERQNELLHLR
HIGRSLAADG NGRNQIISEI RQVLHAMRRG ENLRVEDYMV FDPLIYQGMT DMHDRHREMR
LDVDNMSYEE LLALGERIGD VSTGLSEEVI LKAMKQHKHT SSSPSSVELH QNIEPCCICQ
EEYVEGDNLG TLKCGHEFHK DCIKQWVMIK NLCPICKTEA LKTP
