LPAI_ARATH
ID LPAI_ARATH Reviewed; 1309 AA.
AC F4HX15; O80693;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Phospholipase A I;
DE Short=AtPLA1;
DE EC=3.1.1.-;
GN Name=PLA1; OrderedLocusNames=At1g61850; ORFNames=F8K4.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 SUBCELLULAR LOCATION.
RX PubMed=12226489; DOI=10.1104/pp.006288;
RA Holk A., Rietz S., Zahn M., Quader H., Scherer G.F.;
RT "Molecular identification of cytosolic, patatin-related phospholipases A
RT from Arabidopsis with potential functions in plant signal transduction.";
RL Plant Physiol. 130:90-101(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17475618; DOI=10.1074/jbc.m700405200;
RA Yang W., Devaiah S.P., Pan X., Isaac G., Welti R., Wang X.;
RT "AtPLAI is an acyl hydrolase involved in basal jasmonic acid production and
RT Arabidopsis resistance to Botrytis cinerea.";
RL J. Biol. Chem. 282:18116-18128(2007).
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 less efficiently the phoshpolipids phosphatidylcholine
CC (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG),
CC phosphatidylserine (PS) and phosphatidylinositol (PI). Hydrolyzes
CC phospholipids at both the sn-1 and sn-2 positions. Involved in basal
CC jasmonic acid production and promotes resistance to the necrotrophic
CC fungal pathogen Botrytis cinerea. {ECO:0000269|PubMed:17475618}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:12226489}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4HX15-1; Sequence=Displayed;
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: No visible phenotype under normal growth
CC conditions, but mutant plants have reduced basal level of jasmonic acid
CC and exhibit increased susceptibility to the fungal pathogen Botrytis
CC cinerea. {ECO:0000269|PubMed:17475618}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28504.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004392; AAC28504.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T02131; T02131.
DR AlphaFoldDB; F4HX15; -.
DR SMR; F4HX15; -.
DR STRING; 3702.AT1G61850.1; -.
DR iPTMnet; F4HX15; -.
DR PaxDb; F4HX15; -.
DR PRIDE; F4HX15; -.
DR EnsemblPlants; AT1G61850.2; AT1G61850.2; AT1G61850.
DR Gramene; AT1G61850.2; AT1G61850.2; AT1G61850.
DR Araport; AT1G61850; -.
DR eggNOG; KOG4231; Eukaryota.
DR HOGENOM; CLU_006534_0_0_1; -.
DR PRO; PR:F4HX15; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HX15; baseline and differential.
DR Genevisible; F4HX15; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045217; PNPLA8-like.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Chloroplast; Hydrolase; Leucine-rich repeat;
KW Lipid degradation; Lipid metabolism; Plant defense; Plastid;
KW Reference proteome; Repeat.
FT CHAIN 1..1309
FT /note="Phospholipase A I"
FT /id="PRO_0000425828"
FT REPEAT 155..178
FT /note="LRR 1"
FT REPEAT 180..201
FT /note="LRR 2"
FT REPEAT 203..223
FT /note="LRR 3"
FT REPEAT 224..248
FT /note="LRR 4"
FT REPEAT 315..356
FT /note="ARM 1"
FT REPEAT 401..439
FT /note="ARM 2"
FT REPEAT 440..481
FT /note="ARM 3"
FT DOMAIN 502..746
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 1183..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 506..511
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 538..542
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 733..735
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 1190..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 733
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 1309 AA; 145222 MW; C47A691CB19E6C22 CRC64;
MSSTCSSPSA VEDPELGFRI DLDWTAGDSE DQVALRLESQ LMVALPAPHD TVVVELKGIG
DDDEGGLENV GLEMRVEKRR EPLRAVTLMK AVGSGQQYDG VGVLTRLMRS DMMPAAIPAP
AIDVASSCGV HWKTVTSLSL SGCGLLVMPV EVTELPLLEK LCLEHNKLSV LPPEIGKLKN
LKILRVDNNM LISVPVELRQ CVGLVELSLE HNKLVRPLLD FRAMAGLRIL RLFGNPLEFL
PEILPLHQLR HLSLVNIRIV SDENLRSVNV QIETENTSYF GASRHKLSAF SPLIFRSSSC
HHPLLASTLV KIMQDEGNRS VIGKDENAVR QLISMITSDN QHVVEQACVA LSSLARDVGV
AMQLMKCDIM KPTETVLKSS SPDEVISVLQ VVVTLAFVSD SVSQKMLTKD MLKALKSLCA
HKNPEVQRQA LLAVGNLAFC LENRRILITS ESLRELLMRL IVTPEPRVNK AAARALAILG
ENEILRRSIK GRQVPKQGLR ILTMDGGGMK GLATVQILKE IEKGSGKPIH ELFDLICGTS
TGGMLAIALG VKLMTLEQCE EIYKNLGKLV FAESVPKDNE AASWREKLDQ LYKSSSQSFR
VVIHGSKHSA NEFERLLKEM CADEDGDLLI ESAVKNVPKV FVVSTLVSVM PAQPFIFRNY
QYPVGTPEMS YAFSDHSGGS TLTSSTASDQ AGYYKQSAFM GSCKHQVWQA IRASSAAPYY
LDDFSVDSYR WQDGAIVANN PTIFAIREAQ LLWPDTKIDC LVSIGSGSVP TRVRKGGWRY
LDTGQVLIES ACSVERVEEA LSTLLPMLPE IQYFRFNPVD DRCGMELDET DPAIWLKLEA
AIEEFIQSNP QVFKNVCERL TLPFLNDEKW CDNLKPRFMN GKLPNSRVES SPSLGWRRNV
LLMEAQHSPD SGRVKYHARA LESFCSNNGI KLSSLHTTAT PGCQKPSPGT AFPTPFTSPL
ITGSLPPSPL LFTPELGPQK FNRIDMVPPL SLDGGHVGKT VMSPPSSPPR QRQLYLPLRQ
MHEKLQNLPQ VGILHLSLQN DSNGSILSWQ NDVFVVAEPG DLADKFLQSV KVSILSVMQS
NRRKAASVLS NICSISDLVR SKKCFQVGNI IHRYIGRQTL VMEDDQEIAS FMFRRTVPSA
HLTPDDIRWM VGAWRDRIIV FSGTFGPTQA VVKAFLDSGA KAVIGPSNEP QETPLITSQG
SSEYNIGDQN GKFEIGEEED EDEEVNEETE REEMEPPTPT SDWEDSDHEK TNRDGKYCGL
WEDDEEEVSE FVCQLYDQLF RENSRVDVAL QKALASHRKL RYTCHLPNV
