ID   PLP4_ARATH              Reviewed;         401 AA.
AC   Q9FIY1;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Patatin-like protein 4;
DE            Short=AtPLP4;
DE            EC=3.1.1.-;
DE   AltName: Full=Patatin-related phospholipase A IIepsilon;
DE            Short=pPLAIIe;
DE   AltName: Full=Phospholipase A V;
DE            Short=AtPLA V;
GN   Name=PLP4; OrderedLocusNames=At5g43590; ORFNames=K9D7.9;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
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).
CC   -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC       activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC       role in disease resistance (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC       motif define the oxyanion hole, and stabilize the oxyanion that forms
CC       during the nucleophilic attack by the catalytic serine during substrate
CC       cleavage. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; AB016875; BAB11622.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94985.1; -; Genomic_DNA.
DR   RefSeq; NP_199172.1; NM_123725.2.
DR   AlphaFoldDB; Q9FIY1; -.
DR   SMR; Q9FIY1; -.
DR   STRING; 3702.AT5G43590.1; -.
DR   PaxDb; Q9FIY1; -.
DR   EnsemblPlants; AT5G43590.1; AT5G43590.1; AT5G43590.
DR   GeneID; 834379; -.
DR   Gramene; AT5G43590.1; AT5G43590.1; AT5G43590.
DR   KEGG; ath:AT5G43590; -.
DR   Araport; AT5G43590; -.
DR   TAIR; locus:2158337; AT5G43590.
DR   eggNOG; KOG0513; Eukaryota.
DR   HOGENOM; CLU_000288_144_0_1; -.
DR   InParanoid; Q9FIY1; -.
DR   OMA; HNFPGSP; -.
DR   PhylomeDB; Q9FIY1; -.
DR   BRENDA; 3.1.1.23; 399.
DR   PRO; PR:Q9FIY1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIY1; baseline and differential.
DR   Genevisible; Q9FIY1; AT.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Plant defense;
KW   Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Patatin-like protein 4"
FT                   /id="PRO_0000425816"
FT   DOMAIN          17..218
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           21..26
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           60..64
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           205..207
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   401 AA;  45393 MW;  6874E66061D697C8 CRC64;
     MFKNNKPPKY GNLVTILSLD GGGVRGIIGG VILANLEKHL QEIDNDESVR LADYFDVIAG
     TSTGGLMTAM LTAPNDSGRP LYAAKDIVPF YLEESPKIFY GSKWWDPSAL WALFRPKYNG
     EYLHTRLGEI LGETKLDQTL TNVVIPTFDI KKLQPTIFSS YHASVDPSLN AKLSDICIGT
     SAAPFYLPPY KFPENDKMRT FNLIDGGVTA NDPTLVGMTA MSRKSIIKHP DMDGFKPLEY
     EKYIVISIGT GSAKREEYYS AVEAAKWGFE NWAYNWKHKT TPILDIIFES SRDMVQYHTS
     VLFQALESED NYLRIDADTL KKDEVFMDDS ETLNLENLKN IGEKLLDTNV MRMNLDTYTY
     EPIPKTVNND QELKRFAKIL SDEKKLRNKT FKTMIDDSSN S