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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};
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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
 
 
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