PLA19_ARATH
ID PLA19_ARATH Reviewed; 414 AA.
AC O82274;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phospholipase A1-IIbeta;
DE EC=3.1.1.-;
GN OrderedLocusNames=At2g31100; ORFNames=T16B12.9;
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 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 [4]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phospholipids
CC at the sn-1 position. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63840.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005311; AAC63840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08493.2; -; Genomic_DNA.
DR PIR; E84716; E84716.
DR RefSeq; NP_180668.6; NM_128666.5.
DR AlphaFoldDB; O82274; -.
DR SMR; O82274; -.
DR BioGRID; 1868; 7.
DR ESTHER; arath-PLA19; Plant_phospholipase.
DR iPTMnet; O82274; -.
DR PaxDb; O82274; -.
DR PeptideAtlas; O82274; -.
DR PRIDE; O82274; -.
DR ProteomicsDB; 235005; -.
DR DNASU; 816513; -.
DR GeneID; 817666; -.
DR KEGG; ath:AT2G31100; -.
DR Araport; AT2G31100; -.
DR TAIR; locus:2055884; AT2G31100.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR InParanoid; O82274; -.
DR OrthoDB; 612344at2759; -.
DR BioCyc; ARA:AT2G31100-MON; -.
DR PRO; PR:O82274; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82274; baseline and differential.
DR Genevisible; O82274; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS: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 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 Coiled coil; Cytoplasm; Hydrolase; Isopeptide bond; Lipid degradation;
KW Lipid metabolism; Reference proteome; Ubl conjugation.
FT CHAIN 1..414
FT /note="Phospholipase A1-IIbeta"
FT /id="PRO_0000409359"
FT REGION 386..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..217
FT /evidence="ECO:0000255"
FT COILED 390..410
FT /evidence="ECO:0000255"
FT COMPBIAS 390..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 414 AA; 47581 MW; 1C3AA79044CFF6BB CRC64;
MVGDIATRWK ELSGSSKWKD LLDPLDLDLR RYILHYGDMA EVGYLAFNSD RRSKYVGDSC
YTKEELFART GYLKANPFRY EVTKYIYGTS SIRLPECFII KSLSREAWNK ESNWLGYIAV
ATDEGKKLLG RRGIVVAWRG TIQLYEWAND FDFPLESAVM VFPGANPNDE PRVANGWLSL
YTSTDPRSRF DKTSAQEQVQ EELKRLLELY KNEDVTITLT GHSLGAVMSI LSAADFLHNE
WPKITPSLQH SLCVTVFAFG SPQIGDRSFK RLVESLEHLH ILRVTNVPDL IPRYPVFRFT
DIGEELQINT LKSEYLKRSL NLGHFHNLEA YLHGVAGTQH NQGEFKLEIN RDIALVNKGL
DALEDKYLVP GHWWVLENKG MVQSDDGTWK LNGDRSKKKQ EEEDEKEENN CKFP
