PLP7_ARATH
ID PLP7_ARATH Reviewed; 488 AA.
AC Q9SV43;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Patatin-like protein 7;
DE Short=AtPLP7;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIIbeta;
DE Short=pPLAIIIb;
DE AltName: Full=Phospholipase A IIIA;
DE Short=AtPLAIIIA;
GN Name=PLP7; OrderedLocusNames=At3g54950; ORFNames=F28P10.70;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION.
RX PubMed=16297072; DOI=10.1111/j.1365-313x.2005.02578.x;
RA La Camera S., Geoffroy P., Samaha H., Ndiaye A., Rahim G., Legrand M.,
RA Heitz T.;
RT "A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal
RT and bacterial host colonization in Arabidopsis.";
RL Plant J. 44:810-825(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
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. Catalyzes the hydrolysis of the galactolipids
CC monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol
CC (DGDG), and the phoshpolipids phosphatidylcholine (PC),
CC phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic
CC acid (PA), phosphatidylserine (PS). Favors the release of fatty acid at
CC the sn-2 position for PC. Possesses acyl-CoA thioesterase activity.
CC Negatively affects disease resistance to the necrotic fungal pathogen
CC Botrytis cinerea and the avirulent bacteria Pseudomonas syringae by
CC promoting cell death and reducing the efficiency of the hypersensitive
CC response, respectively. However, PLP2 contributes to resistance to
CC cucumber mosaic virus (CMV), an obligate parasite inducing
CC hypersensitive response. May negatively regulate oxylipin production,
CC possibly via participating in membrane repair that includes removal of
CC oxidatively modified lipids. Enzymatic products of PLP2 may influence
CC cellulose content and cell elongation. {ECO:0000269|PubMed:21447788}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21447788};
CC Peripheral membrane protein {ECO:0000305|PubMed:21447788}.
CC Note=Associated with the plasma membrane.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC leaves, stems, flowers and siliques. {ECO:0000269|PubMed:21447788}.
CC -!- INDUCTION: By the fungal pathogen B.cinerea and an avirulent strain of
CC P.syringae pv tomato. {ECO:0000269|PubMed:16297072,
CC 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 -!- DISRUPTION PHENOTYPE: Increased length of leaves, petioles, hypocotyls,
CC primary roots and root hairs. Changes in lipid levels and composition.
CC {ECO:0000269|PubMed:21447788}.
CC -!- MISCELLANEOUS: Plants over-expressing PLP7 have decreased cellulose
CC content and mechanical strength. {ECO:0000305|PubMed:21447788}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Asp residue expected to act as the active
CC site proton acceptor. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL049655; CAB41089.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79317.1; -; Genomic_DNA.
DR EMBL; AK229196; BAF01066.1; -; mRNA.
DR PIR; T06725; T06725.
DR RefSeq; NP_191055.1; NM_115352.4.
DR AlphaFoldDB; Q9SV43; -.
DR SMR; Q9SV43; -.
DR STRING; 3702.AT3G54950.1; -.
DR PaxDb; Q9SV43; -.
DR PRIDE; Q9SV43; -.
DR ProteomicsDB; 234971; -.
DR EnsemblPlants; AT3G54950.1; AT3G54950.1; AT3G54950.
DR GeneID; 824660; -.
DR Gramene; AT3G54950.1; AT3G54950.1; AT3G54950.
DR KEGG; ath:AT3G54950; -.
DR Araport; AT3G54950; -.
DR TAIR; locus:2082702; AT3G54950.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_1_1; -.
DR InParanoid; Q9SV43; -.
DR OMA; KPNIDAD; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; Q9SV43; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:Q9SV43; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SV43; baseline and differential.
DR Genevisible; Q9SV43; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
DR GO; GO:0019374; P:galactolipid metabolic process; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
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 2: Evidence at transcript level;
KW Cell membrane; Growth regulation; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..488
FT /note="Patatin-like protein 7"
FT /id="PRO_0000425819"
FT DOMAIN 101..301
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 23..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..110
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
SQ SEQUENCE 488 AA; 53100 MW; A214E7BE0FE8CA34 CRC64;
MHRVRNKPVK STATASVKHL IKQRGGDGAT AASKSANDYN NNDSLLTDMQ EPSIDTDKLS
YEIFSILESK FLFGYDDSKP EPANSVVAGS IKNQRGKICI LSIDGGGMRG ILPGKALAYL
EHALKSKSGD PNARIADYFD VAAGSGIGGI YTAMLFGSRD GNRPIFKADD TWQFLTRNAK
GLYGGAGILK RVLRTGSGCC SGTAKLKKVM KESFSELTLK DTLKPVLIPC YDLKSSGPFL
FSRADALETD GYDFRLSEVC RATWAEPGVF EPVEMKSVDG QTKCVAVGGG LAMSNPTAAA
ITHVLHNKQE FPFVRGVEDL LVLSLGMGQL LDVSYEYDRI IKWKAKHWAR PAALISNDGA
ADTVDQAVAM AFGHCRSSNY VRIQANGSNL GPWSPNMDTD PSGSNVNMLM GVAEEMLKQK
NVESVLFGGK RIDEQSNFEK LDWLAGELVL EHQRRNSRIA PTVAFKQSVH RADQKTSDKD
IGVTARER
