LCAT3_ARATH
ID LCAT3_ARATH Reviewed; 447 AA.
AC Q93V61; Q9SRN5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phospholipase A(1) LCAT3;
DE EC=3.1.1.32;
DE AltName: Full=Lecithin-cholesterol acyltransferase-like 3;
GN Name=LCAT3; OrderedLocusNames=At3g03310; ORFNames=T21P5.27;
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 [MRNA], MUTAGENESIS OF SER-177; TYR-346; THR-352;
RP ASP-384 AND HIS-409, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND FUNCTION.
RX PubMed=15355352; DOI=10.1111/j.1432-1033.2004.04317.x;
RA Noiriel A., Benveniste P., Banas A., Stymne S., Bouvier-Nave P.;
RT "Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis
RT thaliana.";
RL Eur. J. Biochem. 271:3752-3764(2004).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: Hydrolyzes the sn-1 acylester bond of phospholipids.
CC Phosphatidylcholine, phosphatidylethanolamine and phosphatidic acid can
CC be used as substrates. Weak activity with lysophosphatidylcholine and
CC no activity with tripalmitoylglycerol and cholesteryl oleate. Seems to
CC have a preference for unsaturated fatty acids at the sn-1 position.
CC {ECO:0000269|PubMed:15355352}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:15355352};
CC Temperature dependence:
CC Optimum temperature is 60 to 65 degrees Celsius.
CC {ECO:0000269|PubMed:15355352};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:15355352};
CC Peripheral membrane protein {ECO:0000269|PubMed:15355352}.
CC -!- MISCELLANEOUS: Unaffected by calcium.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01599.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF421148; AAQ04051.1; -; mRNA.
DR EMBL; AC009895; AAF01599.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73928.1; -; Genomic_DNA.
DR EMBL; AY054239; AAL06898.1; -; mRNA.
DR EMBL; AY056414; AAL08270.1; -; mRNA.
DR EMBL; AY113174; AAM47477.1; -; mRNA.
DR RefSeq; NP_566201.1; NM_111202.4.
DR AlphaFoldDB; Q93V61; -.
DR SMR; Q93V61; -.
DR STRING; 3702.AT3G03310.1; -.
DR ESTHER; arath-LCAT3; PC-sterol_acyltransferase.
DR PaxDb; Q93V61; -.
DR PRIDE; Q93V61; -.
DR ProteomicsDB; 237128; -.
DR EnsemblPlants; AT3G03310.1; AT3G03310.1; AT3G03310.
DR GeneID; 821286; -.
DR Gramene; AT3G03310.1; AT3G03310.1; AT3G03310.
DR KEGG; ath:AT3G03310; -.
DR Araport; AT3G03310; -.
DR TAIR; locus:2099609; AT3G03310.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_035096_0_0_1; -.
DR InParanoid; Q93V61; -.
DR OMA; VPQDDYG; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; Q93V61; -.
DR BioCyc; ARA:AT3G03310-MON; -.
DR BioCyc; MetaCyc:AT3G03301-MON; -.
DR BRENDA; 3.1.1.32; 399.
DR PRO; PR:Q93V61; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93V61; baseline and differential.
DR Genevisible; Q93V61; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Microsome; Reference proteome.
FT CHAIN 1..447
FT /note="Phospholipase A(1) LCAT3"
FT /id="PRO_0000398821"
FT ACT_SITE 177
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT MUTAGEN 177
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15355352"
FT MUTAGEN 346
FT /note="Y->F: Decreased activity."
FT /evidence="ECO:0000269|PubMed:15355352"
FT MUTAGEN 352
FT /note="T->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:15355352"
FT MUTAGEN 384
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15355352"
FT MUTAGEN 409
FT /note="H->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15355352"
SQ SEQUENCE 447 AA; 50349 MW; F24D3903BB60D22A CRC64;
MGWIPCPCWG TNDDENAGEV ADRDPVLLVS GIGGSILHSK KKNSKSEIRV WVRIFLANLA
FKQSLWSLYN PKTGYTEPLD DNIEVLVPDD DHGLYAIDIL DPSWFVKLCH LTEVYHFHDM
IEMLVGCGYK KGTTLFGYGY DFRQSNRIDL LILGLKKKLE TAYKRSGGRK VTIISHSMGG
LMVSCFMYLH PEAFSKYVNK WITIATPFQG APGCINDSIL TGVQFVEGLE SFFFVSRWTM
HQLLVECPSI YEMMANPDFK WKKQPEIRVW RKKSENDVDT SVELESFGLI ESIDLFNDAL
KNNELSYGGN KIALPFNFAI LDWAAKTREI LNKAQLPDGV SFYNIYGVSL NTPFDVCYGT
ETSPIDDLSE ICQTMPEYTY VDGDGTVPAE SAAAAQFKAV ASVGVSGSHR GLLRDERVFE
LIQQWLGVEP KKAKRKHLRT HKVVDSG
