DA2_ARATH
ID DA2_ARATH Reviewed; 401 AA.
AC Q93YV5; Q9M9F8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein ligase DA2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:24045020};
DE AltName: Full=RING-type E3 ubiquitin transferase DA2 {ECO:0000305};
GN Name=DA2 {ECO:0000303|PubMed:24045020};
GN OrderedLocusNames=At1g78420 {ECO:0000312|Araport:AT1G78420};
GN ORFNames=F3F9.7 {ECO:0000312|EMBL:AAF71811.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=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 [4]
RP FUNCTION, INTERACTION WITH DA1, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-59
RP AND ASN-91, AND DISRUPTION PHENOTYPE.
RX PubMed=24045020; DOI=10.1105/tpc.113.115063;
RA Xia T., Li N., Dumenil J., Li J., Kamenski A., Bevan M.W., Gao F., Li Y.;
RT "The ubiquitin receptor DA1 interacts with the E3 ubiquitin ligase DA2 to
RT regulate seed and organ size in Arabidopsis.";
RL Plant Cell 25:3347-3359(2013).
RN [5]
RP FUNCTION.
RX PubMed=28167503; DOI=10.1101/gad.292235.116;
RA Dong H., Dumenil J., Lu F.H., Na L., Vanhaeren H., Naumann C., Klecker M.,
RA Prior R., Smith C., McKenzie N., Saalbach G., Chen L., Xia T., Gonzalez N.,
RA Seguela M., Inze D., Dissmeyer N., Li Y., Bevan M.W.;
RT "Ubiquitylation activates a peptidase that promotes cleavage and
RT destabilization of its activating E3 ligases and diverse growth regulatory
RT proteins to limit cell proliferation in Arabidopsis.";
RL Genes Dev. 31:197-208(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC organ and seed size. Acts synergistically with DA1 to regulate seed
CC size. Functions synergistically with DA1 to restrict cell proliferation
CC in the maternal integuments of ovules and developing seeds. Seems to
CC function independently of BB. Possesses E3 ubiquitin-protein ligase
CC activity in vitro (PubMed:24045020). Polyubiquitinates DA1, DAR1 and
CC DAR2, but not DAR3 (PubMed:28167503). {ECO:0000269|PubMed:24045020,
CC ECO:0000269|PubMed:28167503}.
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:24045020};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with DA1 (via C-terminus).
CC {ECO:0000269|PubMed:24045020}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early stages of petal,
CC stamen, carpel and ovule development, and expression decreases at the
CC later stages of organ development. {ECO:0000269|PubMed:24045020}.
CC -!- DISRUPTION PHENOTYPE: Increased organ size, biomass, and seed size and
CC weight. {ECO:0000269|PubMed:24045020}.
CC -!- MISCELLANEOUS: 'Da' means 'large' in Chinese (PubMed:24045020). Plants
CC overexpressing DA2 exhibit reduced organ size, biomass, and seed size
CC and weight (PubMed:24045020). {ECO:0000269|PubMed:24045020,
CC ECO:0000303|PubMed:24045020}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013430; AAF71811.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36103.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36104.1; -; Genomic_DNA.
DR EMBL; AY059751; AAL24099.1; -; mRNA.
DR EMBL; AY091398; AAM14337.1; -; mRNA.
DR RefSeq; NP_001185425.1; NM_001198496.1.
DR RefSeq; NP_565180.1; NM_106489.3.
DR AlphaFoldDB; Q93YV5; -.
DR STRING; 3702.AT1G78420.2; -.
DR iPTMnet; Q93YV5; -.
DR PaxDb; Q93YV5; -.
DR PRIDE; Q93YV5; -.
DR ProteomicsDB; 224705; -.
DR EnsemblPlants; AT1G78420.1; AT1G78420.1; AT1G78420.
DR EnsemblPlants; AT1G78420.2; AT1G78420.2; AT1G78420.
DR GeneID; 844178; -.
DR Gramene; AT1G78420.1; AT1G78420.1; AT1G78420.
DR Gramene; AT1G78420.2; AT1G78420.2; AT1G78420.
DR KEGG; ath:AT1G78420; -.
DR Araport; AT1G78420; -.
DR TAIR; locus:2032110; AT1G78420.
DR eggNOG; KOG2789; Eukaryota.
DR HOGENOM; CLU_032010_0_0_1; -.
DR InParanoid; Q93YV5; -.
DR OMA; GFHNFPP; -.
DR OrthoDB; 945534at2759; -.
DR PhylomeDB; Q93YV5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q93YV5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93YV5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0046620; P:regulation of organ growth; IMP:UniProtKB.
DR GO; GO:0080113; P:regulation of seed growth; IMP:UniProtKB.
DR InterPro; IPR039301; Sip5/DA2.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR31315; PTHR31315; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..401
FT /note="E3 ubiquitin-protein ligase DA2"
FT /id="PRO_0000444877"
FT ZN_FING 59..102
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 59
FT /note="C->S: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24045020"
FT MUTAGEN 91
FT /note="N->L: No effect on E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24045020"
SQ SEQUENCE 401 AA; 45049 MW; 98E7484DA9C2C35F CRC64;
MGNKLGRKRQ VVEERYTKPQ GLYVNKDVDV KKLRKLIVES KLAPCYPGDD ESCHDLEECP
ICFLYYPSLN RSRCCMKSIC TECFLQMKNP NSARPTQCPF CKTPNYAVEY RGVKSKEEKG
IEQVEEQRVI EAKIRMRQKE MQDDEEKMQK RLESCSSSTS AMTGEMEYGS TSAISYNSLM
DDGEIAPSQN ASVVRQHSRP RGNREDEVDV DLEELMVMEA IWLSVQETGT QRNSASGEIT
SSRQYVTDNH SYVSSPPRVT PIVEPATPSS SSGGLSCAIS ALAERQMVGE SSSHNHNHNV
NVSSYSMLPG NCDSYYDIEQ EVDGIDNHHH HRHHYEMGET GSSNSYVSSY MTGEGFHNFP
PPPPLVIVPE SFEEQMMMAM AVSMAEVHAT TTCAPTEVTW Q
