GW2_ORYSI
ID GW2_ORYSI Reviewed; 425 AA.
AC A4GWX9; B8AEX0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=E3 ubiquitin-protein ligase GW2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:17417637};
DE AltName: Full=Protein GRAIN WIDTH AND WEIGHT 2 {ECO:0000303|PubMed:17417637};
DE AltName: Full=RING-type E3 ubiquitin transferase GW2 {ECO:0000305};
GN Name=GW2 {ECO:0000303|PubMed:17417637};
GN ORFNames=OsI_06523 {ECO:0000312|EMBL:EEC72814.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17417637; DOI=10.1038/ng2014;
RA Song X.J., Huang W., Shi M., Zhu M.Z., Lin H.X.;
RT "A QTL for rice grain width and weight encodes a previously unknown RING-
RT type E3 ubiquitin ligase.";
RL Nat. Genet. 39:623-630(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC grain size. May limit grain width and weight by restricting cell
CC proliferation of the spikelet hull. Possesses E3 ubiquitin-protein
CC ligase activity in vitro. {ECO:0000269|PubMed:17417637}.
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:17417637};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17417637}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, inflorescence
CC meristems, stamens, pistils, spikelet hulls and endosperms 4 days after
CC fertilization. {ECO:0000269|PubMed:17417637}.
CC -!- MISCELLANEOUS: Plants silencing GW2 produce grains with increased
CC width, resulting in enhanced grain weight, whereas overexpression of
CC GW2 decreases grain size and weight. The naturally occurring WY3 allele
CC of GW2, which encodes a truncated version of the protein with a 310-
CC amino acid deletion, increases the number of cells of the spikelet
CC hull, resulting in a wider spikelet hull, and subsequently accelerates
CC the grain milk filling rate, resulting in increased grain width, weight
CC and yield. {ECO:0000269|PubMed:17417637}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC72814.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF447275; ABO31101.1; -; mRNA.
DR EMBL; CM000127; EEC72814.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A4GWX9; -.
DR STRING; 39946.A4GWX9; -.
DR HOGENOM; CLU_032010_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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 Cytoplasm; Developmental protein; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..425
FT /note="E3 ubiquitin-protein ligase GW2"
FT /id="PRO_0000444875"
FT ZN_FING 62..105
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 425 AA; 47399 MW; 9FB16AB6E21EF09C CRC64;
MGNRIGGRRK AGVEERYTRP QGLYEHRDID QKKLRKLILE AKLAPCYMGA DDAAAAADLE
ECPICFLYYP SLNRSKCCSK GICTECFLQM KPTHTAQPTQ CPFCKTPSYA VEYRGVKTKE
ERSIEQFEEQ KVIEAQMRMR QQALQDEEDK MKRKQNRCSS SRTITPTKEV EYRDICSTSF
SVPSYRCAEQ ETECCSSEPS CSAQTSMRPF HSRHNRDDNI DMNIEDMMVM EAIWRSIQEQ
GSIGNPVCGN FMPVTEPSPR ERQPFVPAAS LEIPHGGGFS CAVAAMAEHQ PPSMDFSYMA
GSSAFPVFDM FRRPCNIAGG SMCNLESSPE SWSGIAPSCS REVVREEGEC SADHWSEGAE
AGTSYAGSDI VADAGTMPQL PFAENFAMAP SHFRPESIEE QMMFSMALSL ADGHGRTHSQ
GLAWL
