BRIZ2_ARATH
ID BRIZ2_ARATH Reviewed; 479 AA.
AC O80996; A0A178W1J8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=BRAP2 RING ZnF UBP domain-containing protein 2 {ECO:0000303|PubMed:20810661};
DE EC=2.3.2.27 {ECO:0000269|PubMed:20810661};
GN Name=BRIZ2 {ECO:0000303|PubMed:20810661};
GN OrderedLocusNames=At2g26000 {ECO:0000312|Araport:AT2G26000};
GN ORFNames=T19L18.19 {ECO:0000312|EMBL:AAC31235.1};
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], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, SUBUNIT, AND PATHWAY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=20810661; DOI=10.1074/jbc.m110.168021;
RA Hsia M.M., Callis J.;
RT "BRIZ1 and BRIZ2 proteins form a heteromeric E3 ligase complex required for
RT seed germination and post-germination growth in Arabidopsis thaliana.";
RL J. Biol. Chem. 285:37070-37081(2010).
RN [2]
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 [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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
CC -!- FUNCTION: RING-type ubiquitin E3 ligase that binds ubiquitin and is
CC required for seed germination and post-germination growth.
CC {ECO:0000269|PubMed:20810661}.
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; Evidence={ECO:0000269|PubMed:20810661};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:20810661}.
CC -!- SUBUNIT: Component of the heteromeric E3 ligase complex made of BRIZ1
CC and BRIZ2 (PubMed:20810661). Forms heterooligomers with BRIZ1 via
CC coiled-coil domains (PubMed:20810661). {ECO:0000269|PubMed:20810661}.
CC -!- DISRUPTION PHENOTYPE: Viable heterozygous plants seeds are slow to
CC emerge from the seed coat; emerged embryos remains white with
CC unexpanded cotyledons thus leading to growth-arrested seedlings.
CC {ECO:0000269|PubMed:20810661}.
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DR EMBL; HQ127734; ADQ57815.1; -; mRNA.
DR EMBL; AC004747; AAC31235.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07782.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61430.1; -; Genomic_DNA.
DR EMBL; BT015082; AAT71954.1; -; mRNA.
DR EMBL; BT015905; AAU95441.1; -; mRNA.
DR PIR; T02623; T02623.
DR RefSeq; NP_001031419.1; NM_001036342.3.
DR RefSeq; NP_001323647.1; NM_001336033.1.
DR AlphaFoldDB; O80996; -.
DR SMR; O80996; -.
DR STRING; 3702.AT2G26000.2; -.
DR PaxDb; O80996; -.
DR PRIDE; O80996; -.
DR ProteomicsDB; 181691; -.
DR EnsemblPlants; AT2G26000.2; AT2G26000.2; AT2G26000.
DR EnsemblPlants; AT2G26000.3; AT2G26000.3; AT2G26000.
DR GeneID; 817141; -.
DR Gramene; AT2G26000.2; AT2G26000.2; AT2G26000.
DR Gramene; AT2G26000.3; AT2G26000.3; AT2G26000.
DR KEGG; ath:AT2G26000; -.
DR Araport; AT2G26000; -.
DR TAIR; locus:2057469; AT2G26000.
DR eggNOG; KOG0804; Eukaryota.
DR HOGENOM; CLU_009969_1_0_1; -.
DR InParanoid; O80996; -.
DR OMA; GIIHLYK; -.
DR OrthoDB; 659103at2759; -.
DR PhylomeDB; O80996; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O80996; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80996; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IC:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..479
FT /note="BRAP2 RING ZnF UBP domain-containing protein 2"
FT /id="PRO_0000447001"
FT ZN_FING 167..207
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 201..294
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 434..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..442
FT /evidence="ECO:0000255"
FT COMPBIAS 447..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 479 AA; 53777 MW; 094DA74F741AD8DB CRC64;
MNSASVSGES SLSDMIQTVH FSSGNPRIGE TRGVMHLISD NAVSSSSSSS SSNLPIGRNP
LVCVLGVPNH MTYADFCQFC GSFIQHILDM RTVRNDDIEN RYSILIRFDS QESTDTFFQH
FRGKQFNSLD EDVCRLLFAL DVQFTGYSGS IDHTQPSAAG PIEQPTCPVC LERLDQDTGG
ILTTMCNHSF HCSCISNWPD SSCPVCRYCQ QQPENSVCCV CQTTENLWMC VICGVVGCGR
YKEGHARRHW EETEHCYSLE LETQRVWDYA GDNYVHRLIQ SKTDGKLVEL NSHGSLSKDG
CGSCEYSDSG MTDALLNSKV DMIISEYNEL LQAQLENQKQ YFEKLLQNVK EETEQKISEA
ASKAISQRLQ KLQTRFDRCV KEKQFLEDLN ENLVKNKDVW STKITEMKER EKKAVRAKDE
KIQGLEEQLG NLMAQMDGES EVSETKEVQD ATVSTTNTSS SGAGNVIHAN KKKSNRRKG
