BRIZ1_ARATH
ID BRIZ1_ARATH Reviewed; 488 AA.
AC E5KGE0; O48524; Q8GWY2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=BRAP2 RING ZnF UBP domain-containing protein 1 {ECO:0000303|PubMed:20810661};
DE EC=2.3.2.27 {ECO:0000269|PubMed:20810661};
GN Name=BRIZ1 {ECO:0000303|PubMed:20810661};
GN Synonyms=RING-HCa {ECO:0000303|PubMed:15644464};
GN OrderedLocusNames=At2g42160 {ECO:0000312|Araport:AT2G42160};
GN ORFNames=T24P15.7 {ECO:0000312|EMBL:AAB88642.1};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP GENE FAMILY.
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).
CC -!- FUNCTION: RING-type ubiquitin E3 ligase required for seed germination
CC and post-germination growth. {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 BRIZ2 via
CC coiled-coil domains (PubMed:20810661). {ECO:0000269|PubMed:20810661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E5KGE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E5KGE0-2; Sequence=VSP_060129;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ127733; ADQ57814.1; -; mRNA.
DR EMBL; AC002561; AAB88642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10081.1; -; Genomic_DNA.
DR EMBL; AK118562; BAC43163.1; -; mRNA.
DR EMBL; BT004716; AAO42962.1; -; mRNA.
DR PIR; T00926; T00926.
DR RefSeq; NP_181746.2; NM_129779.4. [E5KGE0-1]
DR AlphaFoldDB; E5KGE0; -.
DR SMR; E5KGE0; -.
DR STRING; 3702.AT2G42160.1; -.
DR iPTMnet; E5KGE0; -.
DR PaxDb; E5KGE0; -.
DR PRIDE; E5KGE0; -.
DR ProteomicsDB; 191336; -. [E5KGE0-1]
DR EnsemblPlants; AT2G42160.1; AT2G42160.1; AT2G42160. [E5KGE0-1]
DR GeneID; 818816; -.
DR Gramene; AT2G42160.1; AT2G42160.1; AT2G42160. [E5KGE0-1]
DR KEGG; ath:AT2G42160; -.
DR Araport; AT2G42160; -.
DR TAIR; locus:2060045; AT2G42160.
DR eggNOG; KOG0804; Eukaryota.
DR HOGENOM; CLU_009969_1_0_1; -.
DR InParanoid; E5KGE0; -.
DR OMA; YIEHASD; -.
DR OrthoDB; 659103at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:E5KGE0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; E5KGE0; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; 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; -; 1.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR033273; BRIZ1/BRIZ2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR24007:SF10; PTHR24007:SF10; 1.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF02148; zf-UBP; 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 Alternative splicing; Coiled coil; Hydrolase; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..488
FT /note="BRAP2 RING ZnF UBP domain-containing protein 1"
FT /id="PRO_0000447000"
FT ZN_FING 174..214
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 208..301
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 453..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 370..418
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT VAR_SEQ 1..376
FT /note="Missing (in isoform 2)"
FT /id="VSP_060129"
FT CONFLICT 396
FT /note="E -> G (in Ref. 4; BAC43163 and 5; AAO42962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55215 MW; 24D6C257B2BC8169 CRC64;
MFILRVHSVD SERPISVEEE ESGFTYASKR AQPPLKLIQP SLKLTDRKGL IHLYRKSSHS
SLPNPSSRST TLFIVAVPNY LSSLDFIRFC DSRISQVSDI LFIRNDGMED RYSVLITFSD
QSEADGFYNN LNGKKFAPSE AEVCHILYVM SVEHTEFDEV AAEAPTGFTE LPTCPICLER
LDPDTSGIVS TLCDHSFQCS CTSKWTYLSC QVCRLCQQQD EILNCSICGK TENVWACLVC
GFVGCGRYKE GHSIRHWKET HHCYSLDLRT QQIWDYVGDS YVHRLNHSKI DGKSVEMSTS
CLSHQGDCGL CECSEDTGIS GAIFNSKVDS IVIEYNDLLA SQLKGQRQYY ESLIVEARSK
QESSIAEAVE QIVVNTMQEL QNKIEKCEEE KSGITEVNTK LIKEQDTWRK KAKEIEEREA
ALLGSKDEMI TDLQEQIRDI TVFIEAKKTL KKMSSDTDGI REGTVLPVPI SPEPVSSVRR
QKKSNRRK
