EG1_ORYSJ
ID EG1_ORYSJ Reviewed; 435 AA.
AC Q8S1D9; A0A0P0VBM5; Q0JGV9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phospholipase A1 EG1, chloroplastic/mitochondrial {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000305|PubMed:27367609};
DE AltName: Full=Protein EXTRA GLUME 1 {ECO:0000303|PubMed:18980657};
DE Flags: Precursor;
GN Name=EG1 {ECO:0000303|PubMed:18980657};
GN OrderedLocusNames=Os01g0900400 {ECO:0000312|EMBL:BAS75742.1},
GN LOC_Os01g67430 {ECO:0000305};
GN ORFNames=P0035F12.8 {ECO:0000312|EMBL:BAB89948.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND MUTAGENESIS OF VAL-178.
RX PubMed=18980657; DOI=10.1111/j.1365-313x.2008.03710.x;
RA Li H., Xue D., Gao Z., Yan M., Xu W., Xing Z., Huang D., Qian Q., Xue Y.;
RT "A putative lipase gene EXTRA GLUME1 regulates both empty-glume fate and
RT spikelet development in rice.";
RL Plant J. 57:593-605(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP VAL-178 AND GLY-216.
RX PubMed=24647160; DOI=10.1038/ncomms4476;
RA Cai Q., Yuan Z., Chen M., Yin C., Luo Z., Zhao X., Liang W., Hu J.,
RA Zhang D.;
RT "Jasmonic acid regulates spikelet development in rice.";
RL Nat. Commun. 5:3476-3476(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION BY HIGH
RP TEMPERATURE.
RX PubMed=27367609; DOI=10.1371/journal.pgen.1006152;
RA Zhang B., Wu S., Zhang Y., Xu T., Guo F., Tang H., Li X., Wang P., Qian W.,
RA Xue Y.;
RT "A high temperature-dependent mitochondrial lipase EXTRA GLUME1 promotes
RT floral phenotypic robustness against temperature fluctuation in rice (Oryza
RT sativa L.).";
RL PLoS Genet. 12:E1006152-E1006152(2016).
CC -!- FUNCTION: Phospholipase that releases free fatty acids from
CC phospholipids. Catalyzes the initial step of jasmonate (JA)
CC biosynthesis. Required for the biosynthesis of endogenous JA in
CC seedling, inflorescence and spikelets. Not essential for JA
CC biosynthesis after wounding (PubMed:24647160). Mediates spikelet
CC development and specification of empty-glume identity (PubMed:18980657,
CC PubMed:24647160). Functions in a high temperature-dependent manner to
CC maintain floral developmental robustness under heat stress conditions.
CC Functions by safeguarding the expression of several floral identity
CC genes, such as MADS1, MADS6 and G1 (PubMed:27367609).
CC {ECO:0000269|PubMed:18980657, ECO:0000269|PubMed:24647160,
CC ECO:0000269|PubMed:27367609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000305|PubMed:27367609};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27367609}.
CC Plastid, chloroplast {ECO:0000269|PubMed:24647160}. Note=Localizes
CC predominantly in mitochondrion. {ECO:0000269|PubMed:27367609}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, inflorescence
CC meristem, spikelet meristem and floral organs.
CC {ECO:0000269|PubMed:24647160}.
CC -!- INDUCTION: By high temperature. {ECO:0000269|PubMed:27367609}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF07019.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS75742.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP003313; BAB89948.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07019.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014957; BAS75742.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK242904; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q8S1D9; -.
DR SMR; Q8S1D9; -.
DR STRING; 4530.OS01T0900400-01; -.
DR ESTHER; orysa-Q8S1D9; Plant_phospholipase.
DR PaxDb; Q8S1D9; -.
DR PRIDE; Q8S1D9; -.
DR EnsemblPlants; Os01t0900400-01; Os01t0900400-01; Os01g0900400.
DR Gramene; Os01t0900400-01; Os01t0900400-01; Os01g0900400.
DR eggNOG; KOG4569; Eukaryota.
DR InParanoid; Q8S1D9; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0010582; P:floral meristem determinacy; IMP:UniProtKB.
DR GO; GO:0048449; P:floral organ formation; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Mitochondrion;
KW Plastid; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..435
FT /note="Phospholipase A1 EG1, chloroplastic/mitochondrial"
FT /id="PRO_0000434871"
FT MOTIF 264..268
FT /note="GXSXG"
FT /evidence="ECO:0000305|PubMed:24647160"
FT ACT_SITE 266
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 178
FT /note="V->D: In eg1-2; increased root length, extra glume-
FT like structures and altered floral organ numbers and
FT identities."
FT /evidence="ECO:0000269|PubMed:18980657,
FT ECO:0000269|PubMed:24647160"
FT MUTAGEN 216
FT /note="G->R: In eg1-3; increased root length, extra glume-
FT like structures and altered floral organ numbers and
FT identities."
FT /evidence="ECO:0000269|PubMed:24647160"
SQ SEQUENCE 435 AA; 46011 MW; 658FB5E4F3F2BC9B CRC64;
MTLPRQCAAA CRTGGGGGGV VRCRAVAAAG GAVAVRDAVV APVARRGAAR KTAETVAGMW
REVQGCGDWE GMLEPAPHPV LRGEVARYGE LVGACYKAFD LDPASRRYLN CKYGRERMLE
EVGMGGAGYE VTRYIYAAAD VSVPTMEPST SGRGRWIGYV AVSTDEMSRR LGRRDVLVSF
RGTVTPAEWM ANLMSSLEAA RLDPCDPRPD VKVESGFLSL YTSADKTCRF GGAGSCREQL
LREVSRLVAA YSGGGEDVSV TLAGHSMGSA LALLSAYDLA ELGLNRAAPV TVFSFGGPRV
GNAAFKARCD ELGVKALRVT NVHDPITKLP GVFLNEATAG VLRPWRHSCY THVGVELPLD
FFKVGDLASV HDLATYISLL RGADKKQPAA AAADAGGVLA KVMDFVGRRR GGGALPWHDA
AMIQMGGLVQ TLGLI
