DA2L_ARATH
ID DA2L_ARATH Reviewed; 335 AA.
AC Q940G8; Q9SHH2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase DA2L {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein DA2-like {ECO:0000303|PubMed:24045020};
DE AltName: Full=RING-type E3 ubiquitin transferase DA2L {ECO:0000305};
GN Name=DA2L {ECO:0000303|PubMed:24045020};
GN OrderedLocusNames=At1g17145 {ECO:0000312|Araport:AT1G17145};
GN ORFNames=F20D23.17 {ECO:0000312|EMBL:AAD50029.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC organ and seed size. Probably functions to restrict cell proliferation
CC during organ and seed development. {ECO:0000269|PubMed:24045020}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- MISCELLANEOUS: Plants overexpressing DA2L exhibit reduced organ size,
CC biomass, and seed size and weight. {ECO:0000269|PubMed:24045020}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29549.1; -; Genomic_DNA.
DR EMBL; AY054649; AAK96840.1; -; mRNA.
DR EMBL; BT000039; AAN15358.1; -; mRNA.
DR EMBL; AY088425; AAM65962.1; -; mRNA.
DR PIR; C86307; C86307.
DR RefSeq; NP_564016.1; NM_101575.4.
DR AlphaFoldDB; Q940G8; -.
DR IntAct; Q940G8; 1.
DR STRING; 3702.AT1G17145.1; -.
DR PaxDb; Q940G8; -.
DR PRIDE; Q940G8; -.
DR ProteomicsDB; 222755; -.
DR EnsemblPlants; AT1G17145.1; AT1G17145.1; AT1G17145.
DR GeneID; 838285; -.
DR Gramene; AT1G17145.1; AT1G17145.1; AT1G17145.
DR KEGG; ath:AT1G17145; -.
DR Araport; AT1G17145; -.
DR TAIR; locus:505006125; AT1G17145.
DR eggNOG; KOG2789; Eukaryota.
DR HOGENOM; CLU_032010_0_0_1; -.
DR OMA; MKNKQTA; -.
DR OrthoDB; 945534at2759; -.
DR PhylomeDB; Q940G8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q940G8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940G8; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Developmental protein; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="E3 ubiquitin-protein ligase DA2L"
FT /id="PRO_0000444878"
FT ZN_FING 63..106
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 143..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 37696 MW; 8700475BBE13A554 CRC64;
MGNKLGRKRQ IVDERYTKPQ QGLYMSKDVD IKKLKKLILE SKLAPCYPGL EETPSSHHDL
EECPICFLYY PSLNRSRCCM KSICTECFLR MKSPNSAQPT QCPFCKTSNY AVEYRGGKTK
EEKSFEQIEE QRVIEAKIRM RQKEVEDDEE RMQKRLESYS SSSSTSAATL DTEYGSAAED
DEEIVSSQES CLPSHHPQVT RDGQFDFDLE DIMVMEAIWL SMQEPGIQRN TSPDDISEKD
RNEEPSTPSS SSPSGGLACA IAVLAERQQM VGVSSSNQNV NLASQNLVPD NGNNSHYNAI
EQDSNHYLQG AGISYTRSDM TDDSGGETSR EVTWQ
