LCAT2_ARATH
ID LCAT2_ARATH Reviewed; 633 AA.
AC Q4VCM1; Q9ZWC1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Phospholipid--sterol O-acyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Lecithin-cholesterol acyltransferase-like 2;
GN Name=PSAT; Synonyms=LCAT2, PSAT1; OrderedLocusNames=At1g04010;
GN ORFNames=F21M11.5;
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], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16020547; DOI=10.1074/jbc.m504459200;
RA Banas A., Carlsson A.S., Huang B., Lenman M., Banas W., Lee M., Noiriel A.,
RA Benveniste P., Schaller H., Bouvier-Nave P., Stymne S.;
RT "Cellular sterol ester synthesis in plants is performed by an enzyme
RT (phospholipid:sterol acyltransferase) different from the yeast and
RT mammalian acyl-CoA:sterol acyltransferases.";
RL J. Biol. Chem. 280:34626-34634(2005).
RN [2]
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 [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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19923239; DOI=10.1104/pp.109.145672;
RA Bouvier-Nave P., Berna A., Noiriel A., Compagnon V., Carlsson A.S.,
RA Banas A., Stymne S., Schaller H.;
RT "Involvement of the phospholipid sterol acyltransferase1 in plant sterol
RT homeostasis and leaf senescence.";
RL Plant Physiol. 152:107-119(2010).
CC -!- FUNCTION: Involved in lipid catabolism. Essential for sterol esters
CC biosynthesis in leaves and seeds, but not in flowers. Plays a role in
CC controlling the free sterol content of leaves. Catalyzes the
CC transacylation of acyl groups from phospholipids to a variety of
CC different sterols. Prefers phosphatidylethanolamine over
CC phosphatidylcholine as an acyl donor. Not active toward neutral lipids.
CC Highly specific for position sn-2, which in plant lipids is essentially
CC devoid of saturated acyl groups. Broad sterol specificity (cholesterol
CC > campesterol > sitosterol > stigmasterol), but no activity with lupeol
CC or beta-amyrin. {ECO:0000269|PubMed:16020547,
CC ECO:0000269|PubMed:19923239}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:16020547};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:16020547}.
CC -!- INDUCTION: By senescence. {ECO:0000269|PubMed:19923239}.
CC -!- DISRUPTION PHENOTYPE: Early leaf senescence. Strong reduction in total
CC sterol esters content in leaves and seeds. No change in flowers.
CC {ECO:0000269|PubMed:16020547, ECO:0000269|PubMed:19923239}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10668.1; Type=Erroneous gene model prediction; 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; AY989885; AAY43920.1; -; mRNA.
DR EMBL; AC003027; AAD10668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27645.1; -; Genomic_DNA.
DR PIR; C86171; C86171.
DR RefSeq; NP_171897.2; NM_100282.4.
DR AlphaFoldDB; Q4VCM1; -.
DR SMR; Q4VCM1; -.
DR BioGRID; 24570; 1.
DR STRING; 3702.AT1G04010.1; -.
DR ESTHER; arath-LCAT2; PC-sterol_acyltransferase.
DR iPTMnet; Q4VCM1; -.
DR PaxDb; Q4VCM1; -.
DR PRIDE; Q4VCM1; -.
DR ProteomicsDB; 237158; -.
DR EnsemblPlants; AT1G04010.1; AT1G04010.1; AT1G04010.
DR GeneID; 839335; -.
DR Gramene; AT1G04010.1; AT1G04010.1; AT1G04010.
DR KEGG; ath:AT1G04010; -.
DR Araport; AT1G04010; -.
DR TAIR; locus:2024117; AT1G04010.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_024778_0_0_1; -.
DR InParanoid; Q4VCM1; -.
DR OMA; ILMRELW; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; Q4VCM1; -.
DR PRO; PR:Q4VCM1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4VCM1; baseline and differential.
DR Genevisible; Q4VCM1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:TAIR.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0080096; F:phosphatidate-sterol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080095; F:phosphatidylethanolamine-sterol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0016127; P:sterol catabolic process; IMP:TAIR.
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 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Microsome; Reference proteome; Signal-anchor; Steroid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="Phospholipid--sterol O-acyltransferase"
FT /id="PRO_0000398820"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..633
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 195
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255"
FT ACT_SITE 461
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 505
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 145
FT /note="I -> V (in Ref. 1; AAY43920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 71688 MW; D80FD668E1001015 CRC64;
MGANSKSVTA SFTVIAVFFL ICGGRTAVED ETEFHGDYSK LSGIIIPGFA STQLRAWSIL
DCPYTPLDFN PLDLVWLDTT KLLSAVNCWF KCMVLDPYNQ TDHPECKSRP DSGLSAITEL
DPGYITGPLS TVWKEWLKWC VEFGIEANAI VAVPYDWRLS PTKLEERDLY FHKLKLTFET
ALKLRGGPSI VFAHSMGNNV FRYFLEWLRL EIAPKHYLKW LDQHIHAYFA VGAPLLGSVE
AIKSTLSGVT FGLPVSEGTA RLLSNSFASS LWLMPFSKNC KGDNTFWTHF SGGAAKKDKR
VYHCDEEEYQ SKYSGWPTNI INIEIPSTSV TETALVNMTS MECGLPTLLS FTARELADGT
LFKAIEDYDP DSKRMLHQLK KLYHDDPVFN PLTPWERPPI KNVFCIYGAH LKTEVGYYFA
PSGKPYPDNW IITDIIYETE GSLVSRSGTV VDGNAGPITG DETVPYHSLS WCKNWLGPKV
NITMAPQPEH DGSDVHVELN VDHEHGSDII ANMTKAPRVK YITFYEDSES IPGKRTAVWE
LDKTNHRNIV RSPVLMRELW LQMWHDIQPG AKSKFVTKAK RGPLRDADCY WDYGKACCAW
QEYCEYRYSF GDVHLGQSCR LRNTSANMLL QYI