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Phospholipid--sterol O-acyltransferase (EC 2.3.1.-) (Lecithin-cholesterol acyltransferase-like 2)

 LCAT2_ARATH             Reviewed;         633 AA.
Q4VCM1; Q9ZWC1;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
07-JUN-2017, entry version 71.
RecName: Full=Phospholipid--sterol O-acyltransferase;
EC=2.3.1.-;
AltName: Full=Lecithin-cholesterol acyltransferase-like 2;
Name=PSAT; Synonyms=LCAT2, PSAT1; OrderedLocusNames=At1g04010;
ORFNames=F21M11.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=16020547; DOI=10.1074/jbc.M504459200;
Banas A., Carlsson A.S., Huang B., Lenman M., Banas W., Lee M.,
Noiriel A., Benveniste P., Schaller H., Bouvier-Nave P., Stymne S.;
"Cellular sterol ester synthesis in plants is performed by an enzyme
(phospholipid:sterol acyltransferase) different from the yeast and
mammalian acyl-CoA:sterol acyltransferases.";
J. Biol. Chem. 280:34626-34634(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=19923239; DOI=10.1104/pp.109.145672;
Bouvier-Nave P., Berna A., Noiriel A., Compagnon V., Carlsson A.S.,
Banas A., Stymne S., Schaller H.;
"Involvement of the phospholipid sterol acyltransferase1 in plant
sterol homeostasis and leaf senescence.";
Plant Physiol. 152:107-119(2010).
-!- FUNCTION: Involved in lipid catabolism. Essential for sterol
esters biosynthesis in leaves and seeds, but not in flowers. Plays
a role in controlling the free sterol content of leaves. Catalyzes
the transacylation of acyl groups from phospholipids to a variety
of different sterols. Prefers phosphatidylethanolamine over
phosphatidylcholine as an acyl donor. Not active toward neutral
lipids. Highly specific for position sn-2, which in plant lipids
is essentially devoid of saturated acyl groups. Broad sterol
specificity (cholesterol > campesterol > sitosterol >
stigmasterol), but no activity with lupeol or beta-amyrin.
{ECO:0000269|PubMed:16020547, ECO:0000269|PubMed:19923239}.
-!- SUBCELLULAR LOCATION: Microsome membrane
{ECO:0000269|PubMed:16020547}; Single-pass type II membrane
protein {ECO:0000269|PubMed:16020547}.
-!- INDUCTION: By senescence. {ECO:0000269|PubMed:19923239}.
-!- DISRUPTION PHENOTYPE: Early leaf senescence. Strong reduction in
total sterol esters content in leaves and seeds. No change in
flowers. {ECO:0000269|PubMed:16020547,
ECO:0000269|PubMed:19923239}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD10668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY989885; AAY43920.1; -; mRNA.
EMBL; AC003027; AAD10668.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE27645.1; -; Genomic_DNA.
PIR; C86171; C86171.
RefSeq; NP_171897.2; NM_100282.4.
UniGene; At.42498; -.
ProteinModelPortal; Q4VCM1; -.
BioGrid; 24570; 1.
STRING; 3702.AT1G04010.1; -.
ESTHER; arath-LCAT2; PC-sterol_acyltransferase.
iPTMnet; Q4VCM1; -.
PaxDb; Q4VCM1; -.
EnsemblPlants; AT1G04010.1; AT1G04010.1; AT1G04010.
GeneID; 839335; -.
Gramene; AT1G04010.1; AT1G04010.1; AT1G04010.
KEGG; ath:AT1G04010; -.
Araport; AT1G04010; -.
TAIR; locus:2024117; AT1G04010.
eggNOG; KOG2369; Eukaryota.
eggNOG; ENOG410Y9CF; LUCA.
HOGENOM; HOG000239610; -.
InParanoid; Q4VCM1; -.
OMA; PEHCEYR; -.
OrthoDB; EOG093604GZ; -.
PhylomeDB; Q4VCM1; -.
BioCyc; ARA:GQT-401-MONOMER; -.
PRO; PR:Q4VCM1; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q4VCM1; baseline and differential.
Genevisible; Q4VCM1; AT.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0080096; F:phosphatidate-sterol O-acyltransferase activity; IDA:TAIR.
GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:TAIR.
GO; GO:0080095; F:phosphatidylethanolamine-sterol O-acyltransferase activity; IDA:TAIR.
GO; GO:0010150; P:leaf senescence; IMP:TAIR.
GO; GO:0016127; P:sterol catabolic process; IMP:TAIR.
GO; GO:0034434; P:sterol esterification; IDA:TAIR.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR003386; LACT/PDAT_acylTrfase.
Pfam; PF02450; LCAT; 1.
SUPFAM; SSF53474; SSF53474; 2.
2: Evidence at transcript level;
Acyltransferase; Complete proteome; Endoplasmic reticulum;
Lipid metabolism; Membrane; Microsome; Reference proteome;
Signal-anchor; Steroid metabolism; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 633 Phospholipid--sterol O-acyltransferase.
/FTId=PRO_0000398820.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 633 Lumenal. {ECO:0000255}.
ACT_SITE 195 195 Acyl-ester intermediate. {ECO:0000255}.
ACT_SITE 461 461 Charge relay system. {ECO:0000250}.
ACT_SITE 505 505 Charge relay system. {ECO:0000250}.
CONFLICT 145 145 I -> V (in Ref. 1; AAY43920).
{ECO:0000305}.
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


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