ID   PLP6_ARATH              Reviewed;         499 AA.
AC   O80959;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Patatin-like protein 6;
DE            Short=AtPLP6;
DE            EC=3.1.1.-;
DE   AltName: Full=Patatin-related phospholipase A IIIalpha;
DE            Short=pPLAIIIa;
DE   AltName: Full=Phospholipase A IIB;
DE            Short=AtPLAIIB;
GN   Name=PLP6; OrderedLocusNames=At2g39220; ORFNames=T16B24.14;
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].
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   TISSUE SPECIFICITY.
RX   PubMed=21447788; DOI=10.1105/tpc.110.081240;
RA   Li M., Bahn S.C., Guo L., Musgrave W., Berg H., Welti R., Wang X.;
RT   "Patatin-related phospholipase pPLAIIIbeta-induced changes in lipid
RT   metabolism alter cellulose content and cell elongation in Arabidopsis.";
RL   Plant Cell 23:1107-1123(2011).
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   -!- INTERACTION:
CC       O80959; Q8RXD6: HUB1; NbExp=3; IntAct=EBI-25515433, EBI-2012188;
CC   -!- TISSUE SPECIFICITY: Highly expressed in siliques and at lower levels in
CC       roots and flowers. {ECO:0000269|PubMed:21447788}.
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; AC004697; AAC28986.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09647.1; -; Genomic_DNA.
DR   EMBL; AY062648; AAL32726.1; -; mRNA.
DR   EMBL; BT000763; AAN31902.1; -; mRNA.
DR   EMBL; BT008869; AAP68308.1; -; mRNA.
DR   PIR; T02580; T02580.
DR   RefSeq; NP_181455.1; NM_129480.3.
DR   AlphaFoldDB; O80959; -.
DR   SMR; O80959; -.
DR   BioGRID; 3845; 1.
DR   IntAct; O80959; 1.
DR   STRING; 3702.AT2G39220.1; -.
DR   PaxDb; O80959; -.
DR   PRIDE; O80959; -.
DR   ProteomicsDB; 236638; -.
DR   EnsemblPlants; AT2G39220.1; AT2G39220.1; AT2G39220.
DR   GeneID; 818507; -.
DR   Gramene; AT2G39220.1; AT2G39220.1; AT2G39220.
DR   KEGG; ath:AT2G39220; -.
DR   Araport; AT2G39220; -.
DR   TAIR; locus:2056088; AT2G39220.
DR   eggNOG; KOG0513; Eukaryota.
DR   HOGENOM; CLU_000288_144_1_1; -.
DR   InParanoid; O80959; -.
DR   OMA; YNKSPPG; -.
DR   OrthoDB; 1209603at2759; -.
DR   PhylomeDB; O80959; -.
DR   BRENDA; 3.1.1.23; 399.
DR   PRO; PR:O80959; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80959; baseline and differential.
DR   Genevisible; O80959; AT.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0016787; F:hydrolase activity; IDA:TAIR.
DR   GO; GO:0016298; F:lipase activity; IDA:TAIR.
DR   GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
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   1: Evidence at protein level;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..499
FT                   /note="Patatin-like protein 6"
FT                   /id="PRO_0000425818"
FT   DOMAIN          111..314
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           116..119
FT                   /note="GGXR"
FT   MOTIF           301..303
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  54495 MW;  E6C023672BE9582D CRC64;
     MLTTMQRVHN KPIDSIGGFK HLVKQSNGGD GGVTATDMQE PSIETDKLSY EIFSILESKF
     LFGYDDDLKL MESRSRDPSP EQETASPAMV EALNGVVPGT VKNQRGKVCV LSIDSGGMRG
     IIPGKALAYL EHALKSKSGD PNARIADYFD VASGSGIGGI FTAMLFASSD GNRPIFKAED
     TWRFLAMKGK SFYNKSPPGI LNRVMKTGSG GSGGSGSKLE KAMKESFEEL TLKDTLKPVL
     IPCYDLTSSA PFLFSRADAL ETDGYDFKLW EVCRATWAEP GVFEPVEMRS VDGKTRCVAV
     DGGLAMSNPT AAAITHVLHN KQEFPFVRGV EDLLVLSLGT GQLVDVKYDC DKVMKWKAKH
     WARPAVRISA DGAADTVDQA VSMAFGQCRR SNYVRIQANG SSFGPCKPNI DTDASPSNVN
     MLVGVAEEML KQKNAESVLF GGKKINEESN YEKLDWLAGE LVLEHQRRSC RIAPTVAFKQ
     SGDRRVDQQT IFKDIDCMF