PLA20_ARATH
ID PLA20_ARATH Reviewed; 412 AA.
AC Q9SJI7; C0Z2D7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phospholipase A1-IIdelta;
DE EC=3.1.1.-;
GN OrderedLocusNames=At2g42690; ORFNames=F14N22.2;
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=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 [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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY UV-B RADIATION AND SENESCENCE.
RC STRAIN=cv. Columbia;
RX PubMed=15181214; DOI=10.1104/pp.103.036376;
RA Lo M., Taylor C., Wang L., Nowack L., Wang T.W., Thompson J.;
RT "Characterization of an ultraviolet B-induced lipase in Arabidopsis.";
RL Plant Physiol. 135:947-958(2004).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130548; DOI=10.1016/j.tplants.2004.03.004;
RA Ryu S.B.;
RT "Phospholipid-derived signaling mediated by phospholipase A in plants.";
RL Trends Plant Sci. 9:229-235(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of
CC phosphatidylcholine (PC) at the sn-1 position. High activity toward PC,
CC medium activity toward monogalactosyldiacylglycerol (MGDG) and low
CC activity toward triacylglycerol (TAG). Confers sensitivity to UV-B
CC radiation probably by deesterifying membrane phospholipids.
CC {ECO:0000269|PubMed:15181214}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15181214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SJI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SJI7-2; Sequence=VSP_041299, VSP_041300;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and siliques,
CC and, at low levels, in seeds and roots (at protein level).
CC {ECO:0000269|PubMed:15181214}.
CC -!- INDUCTION: Strongly induced in response to sublethal levels of UV-B
CC radiation. Down-regulated as the leaves senesce.
CC {ECO:0000269|PubMed:15181214}.
CC -!- DISRUPTION PHENOTYPE: Enhanced tolerance to UV-B stress but not osmotic
CC stress. Impaired PR-1 accumulation in response to UV-B.
CC {ECO:0000269|PubMed:15181214}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AC006931; AAD21737.1; -; Genomic_DNA.
DR EMBL; AC007087; AAM15382.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10156.1; -; Genomic_DNA.
DR EMBL; AY050998; AAK93675.1; -; mRNA.
DR EMBL; AY079356; AAL85087.1; -; mRNA.
DR EMBL; AK318751; BAH56866.1; -; mRNA.
DR PIR; A84857; A84857.
DR RefSeq; NP_181797.1; NM_129830.2. [Q9SJI7-1]
DR AlphaFoldDB; Q9SJI7; -.
DR SMR; Q9SJI7; -.
DR STRING; 3702.AT2G42690.1; -.
DR ESTHER; arath-AT2G42690; Plant_phospholipase.
DR iPTMnet; Q9SJI7; -.
DR PaxDb; Q9SJI7; -.
DR PRIDE; Q9SJI7; -.
DR ProteomicsDB; 226198; -. [Q9SJI7-1]
DR EnsemblPlants; AT2G42690.1; AT2G42690.1; AT2G42690. [Q9SJI7-1]
DR GeneID; 818869; -.
DR Gramene; AT2G42690.1; AT2G42690.1; AT2G42690. [Q9SJI7-1]
DR KEGG; ath:AT2G42690; -.
DR Araport; AT2G42690; -.
DR TAIR; locus:2041599; AT2G42690.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR InParanoid; Q9SJI7; -.
DR OMA; RNEYKDE; -.
DR PhylomeDB; Q9SJI7; -.
DR BioCyc; ARA:AT2G42690-MON; -.
DR PRO; PR:Q9SJI7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJI7; baseline and differential.
DR Genevisible; Q9SJI7; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; IEP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009650; P:UV protection; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR033556; PLA.
DR PANTHER; PTHR31828; PTHR31828; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..412
FT /note="Phospholipase A1-IIdelta"
FT /id="PRO_0000409360"
FT ACT_SITE 238
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 336
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 340..384
FT /note="AMLHVVAGWNGKKGEFKLMVKRSIALVNKSCEFLKAECLVPGSWW -> VRI
FT CEKNLSNLTQTIQSRNFYIFFPCMCAGDVTCCSWMEWEERRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041299"
FT VAR_SEQ 385..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041300"
SQ SEQUENCE 412 AA; 46057 MW; 4923CC470E4BEEF9 CRC64;
MATTTTSWEE LLGSKNWDTI LDPLDQSLRE LILRCGDFCQ ATYDAFVNDQ NSKYCGASRY
GKSSFFDKVM LENASDYEVV NFLYATARVS LPEGLLLQSQ SRDSWDRESN WFGYIAVTSD
ERSKALGRRE IYIALRGTSR NYEWVNVLGA RPTSADPLLH GPEQDGSGGV VEGTTFDSDS
EDEEGCKVML GWLTIYTSNH PESKFTKLSL RSQLLAKIKE LLLKYKDEKP SIVLTGHSLG
ATEAVLAAYD IAENGSSDDV PVTAIVFGCP QVGNKEFRDE VMSHKNLKIL HVRNTIDLLT
RYPGGLLGYV DIGINFVIDT KKSPFLSDSR NPGDWHNLQA MLHVVAGWNG KKGEFKLMVK
RSIALVNKSC EFLKAECLVP GSWWVEKNKG LIKNEDGEWV LAPVEEEPVP EF
