PLP8_ARATH
ID PLP8_ARATH Reviewed; 525 AA.
AC Q8H133; Q9SZQ3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Patatin-like protein 8;
DE Short=AtPLP8;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIIgamma;
DE Short=pPLAIIIg;
DE AltName: Full=Phospholipase A IVD;
DE Short=AtPLAIVD;
GN Name=PLP8; OrderedLocusNames=At4g29800; ORFNames=F27B13.40;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
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 Q8H133; Q38845: PP2AA1; NbExp=3; IntAct=EBI-16967096, EBI-1645478;
CC Q8H133; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-16967096, EBI-15192297;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H133-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H133-2; Sequence=VSP_053857;
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BX828321; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={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; AL050352; CAB43655.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79738.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85677.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85678.1; -; Genomic_DNA.
DR EMBL; BT000869; AAN41269.1; -; mRNA.
DR EMBL; BX828321; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T08541; T08541.
DR RefSeq; NP_001190866.1; NM_001203937.2. [Q8H133-2]
DR RefSeq; NP_194709.2; NM_119126.3. [Q8H133-1]
DR AlphaFoldDB; Q8H133; -.
DR SMR; Q8H133; -.
DR BioGRID; 14389; 5.
DR IntAct; Q8H133; 5.
DR STRING; 3702.AT4G29800.2; -.
DR iPTMnet; Q8H133; -.
DR PaxDb; Q8H133; -.
DR PRIDE; Q8H133; -.
DR ProteomicsDB; 234972; -. [Q8H133-1]
DR EnsemblPlants; AT4G29800.1; AT4G29800.1; AT4G29800. [Q8H133-1]
DR EnsemblPlants; AT4G29800.2; AT4G29800.2; AT4G29800. [Q8H133-2]
DR GeneID; 829102; -.
DR Gramene; AT4G29800.1; AT4G29800.1; AT4G29800. [Q8H133-1]
DR Gramene; AT4G29800.2; AT4G29800.2; AT4G29800. [Q8H133-2]
DR KEGG; ath:AT4G29800; -.
DR Araport; AT4G29800; -.
DR TAIR; locus:2123894; AT4G29800.
DR eggNOG; KOG0513; Eukaryota.
DR OMA; ADHAPRM; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; Q8H133; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:Q8H133; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H133; baseline and differential.
DR Genevisible; Q8H133; AT.
DR GO; GO:0016298; F:lipase activity; IEA:UniProt.
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 Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Plant defense; Reference proteome.
FT CHAIN 1..525
FT /note="Patatin-like protein 8"
FT /id="PRO_0000425820"
FT DOMAIN 124..338
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..133
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 26..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT VAR_SEQ 420
FT /note="I -> IQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053857"
SQ SEQUENCE 525 AA; 56961 MW; EEF3AD3A8D8B83E2 CRC64;
MNRRYEKPPP LSVSSKGKKK HFVNHTAPNT PGNYERTQTS PTLSTARSHE PDDKLNYEIF
SILESKFLFG YEDPRLLWIP QSPLRPGDSE AGPSPRSPLT PNGVVLPGTP SSSFRSPRGR
ICVLSIDGGG MRGLLAGKSL IYLEQMLKEK SGDPNARIAD YFDVAAGSGV GGVFAAMIFA
TRDGNRPIFK AEDTWKFLVE NAEGFYRSGS GSGGGGAGAA IKRVIRSGSG SGSSSVTAAT
AKLEKAMKAS FADLTLKDTL KPILISCYDL SSTAPFLFSR ADALESDSFD FRLRDICRAT
WAEPGTFDPV RTCSVDGKTR CVAVGGGLAM SNPTAAAITH VFHNKQEFPA VKGVEDLLVL
SLGTGQLFEV NYDYEQVKNW RVKEWARPMA RISGDGSAEF VDQAVAMGFG PYRSSNYVRI
QANGSRLGAC GPNVDTDPRA ENVKKLTEIA DEMLKQNNVE SVLFGSKRIG EMSNSEKIEW
FASELVIEQQ RRSVRASPTV TLKQAVSKTN RNAINATLTL ISKDR
