PLIP1_ARATH
ID PLIP1_ARATH Reviewed; 649 AA.
AC Q7Y220; Q9M370;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phospholipase A1 PLIP1, chloroplastic {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:28687655};
DE AltName: Full=Galactolipase PLIP1 {ECO:0000305};
DE EC=3.1.1.26 {ECO:0000269|PubMed:28687655};
DE AltName: Full=Protein PLASTID LIPASE 1 {ECO:0000303|PubMed:28687655};
DE Flags: Precursor;
GN Name=PLIP1 {ECO:0000303|PubMed:28687655};
GN OrderedLocusNames=At3g61680 {ECO:0000312|Araport:AT3G61680};
GN ORFNames=F15G16.70 {ECO:0000312|EMBL:CAB71098.1};
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;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-422
RP AND ASP-483, AND DISRUPTION PHENOTYPE.
RX PubMed=28687655; DOI=10.1105/tpc.17.00397;
RA Wang K., Froehlich J.E., Zienkiewicz A., Hersh H.L., Benning C.;
RT "A plastid phosphatidylglycerol lipase contributes to the export of acyl
RT groups from plastids for seed oil biosynthesis.";
RL Plant Cell 29:1678-1696(2017).
CC -!- FUNCTION: Sn-1-specific phospholipase A1 involved in seed oil
CC biosynthesis. Hydrolyzes polyunsaturated acyl groups from a unique
CC chloroplast-specific phosphatidylglycerol (PG) that contains 16:1 delta
CC 3-trans as its second acyl group. The polyunsaturated acyl groups
CC released by PLIP1 are exported from the chloroplast, reincorporated
CC into phosphatidylcholine (PC), and ultimately enter seed
CC triacylglycerol (TAG). In vitro, possesses broad substrate specificity.
CC Can hydrolyze the galactolipid monogalactosyldiacylglycerol (MGDG), and
CC the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine
CC (PE), phosphatidic acid (PA), phosphatidylserine (PS)
CC phosphatidylglycerol (PG) and phosphatidylinositol (PI).
CC {ECO:0000269|PubMed:28687655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:28687655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-
CC beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+);
CC Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26;
CC Evidence={ECO:0000269|PubMed:28687655};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:28687655}; Peripheral membrane protein
CC {ECO:0000305|PubMed:28687655}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of oil seeds and delay in seed
CC germination. {ECO:0000269|PubMed:28687655}.
CC -!- MISCELLANEOUS: Plants overexpressing PLIP1 exhibit stunted growth and
CC accumulate anthocyanin under normal growth conditions.
CC {ECO:0000269|PubMed:28687655}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132959; CAB71098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80240.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65459.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65460.1; -; Genomic_DNA.
DR EMBL; BT008609; AAP40434.1; -; mRNA.
DR EMBL; AK228526; BAF00448.1; -; mRNA.
DR EMBL; BT046186; ACI49785.1; -; mRNA.
DR PIR; T47960; T47960.
DR RefSeq; NP_001327423.1; NM_001340118.1.
DR RefSeq; NP_001327424.1; NM_001340117.1.
DR RefSeq; NP_191727.2; NM_116033.5.
DR AlphaFoldDB; Q7Y220; -.
DR SMR; Q7Y220; -.
DR ESTHER; arath-At3g61680; Lipase_3.
DR PaxDb; Q7Y220; -.
DR PRIDE; Q7Y220; -.
DR EnsemblPlants; AT3G61680.1; AT3G61680.1; AT3G61680.
DR EnsemblPlants; AT3G61680.2; AT3G61680.2; AT3G61680.
DR EnsemblPlants; AT3G61680.3; AT3G61680.3; AT3G61680.
DR GeneID; 825341; -.
DR Gramene; AT3G61680.1; AT3G61680.1; AT3G61680.
DR Gramene; AT3G61680.2; AT3G61680.2; AT3G61680.
DR Gramene; AT3G61680.3; AT3G61680.3; AT3G61680.
DR KEGG; ath:AT3G61680; -.
DR Araport; AT3G61680; -.
DR TAIR; locus:2076785; AT3G61680.
DR eggNOG; ENOG502QSG6; Eukaryota.
DR HOGENOM; CLU_016443_1_0_1; -.
DR InParanoid; Q7Y220; -.
DR OMA; RCYGLDF; -.
DR OrthoDB; 510921at2759; -.
DR PhylomeDB; Q7Y220; -.
DR PRO; PR:Q7Y220; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7Y220; baseline and differential.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047714; F:galactolipase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IDA:TAIR.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0015908; P:fatty acid transport; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR043367; PLIP1/2/3.
DR PANTHER; PTHR46483; PTHR46483; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..649
FT /note="Phospholipase A1 PLIP1, chloroplastic"
FT /id="PRO_0000444793"
FT MOTIF 420..424
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 422
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 483
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 593
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 422
FT /note="S->A: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:28687655"
FT MUTAGEN 483
FT /note="D->A: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:28687655"
SQ SEQUENCE 649 AA; 71735 MW; 40C5EF0CDB446127 CRC64;
MAFNTAMAST SPAAANDVLR EHIGLRRSLS GQDLVLKGGG IRRSSSDNHL CCRSGNNNNR
ILAVSVRPGM KTSRSVGVFS FQISSSIIPS PIKTLLFETD TSQDEQESDE IEIETEPNLD
GAKKANWVER LLEIRRQWKR EQKTESGNSD VAEESVDVTC GCEEEEGCIA NYGSVNGDWG
RESFSRLLVK VSWSEAKKLS QLAYLCNLAY TIPEIKGEDL RRNYGLKFVT SSLEKKAKAA
ILREKLEQDP THVPVITSPD LESEKQSQRS ASSSASAYKI AASAASYIHS CKEYDLSEPI
YKSAAAAQAA ASTMTAVVAA GEEEKLEAAR ELQSLQSSPC EWFVCDDPNT YTRCFVIQGS
DSLASWKANL FFEPTKFEDT DVLVHRGIYE AAKGIYEQFL PEITEHLSRH GDRAKFQFTG
HSLGGSLSLI VNLMLISRGL VSSEAMKSVV TFGSPFVFCG GEKILAELGL DESHVHCVMM
HRDIVPRAFS CNYPDHVALV LKRLNGSFRT HPCLNKNKLL YSPMGKVYIL QPSESVSPTH
PWLPPGNALY ILENSNEGYS PTALRAFLNR PHPLETLSQR AAYGSEGSVL RDHDSKNYVK
AVNGVLRQHT KLIVRKARIQ RRSVWPVLTS AGRGLNESLT TAEEIMTRV
