位置:首页 > 蛋白库 > PDAT_YEAST
PDAT_YEAST
ID   PDAT_YEAST              Reviewed;         661 AA.
AC   P40345; D6W1I3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Phospholipid:diacylglycerol acyltransferase {ECO:0000305};
DE            Short=PDAT;
DE            EC=2.3.1.158 {ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386, ECO:0000269|PubMed:30706417};
DE   AltName: Full=LCAT-related open reading frame 1 {ECO:0000303|PubMed:10747858};
DE   AltName: Full=Lecithin cholesterol acyl transferase-related open reading frame 1 {ECO:0000303|PubMed:10747858};
DE   AltName: Full=Triacylglycerol synthase;
DE            Short=TAG synthase;
GN   Name=LRO1 {ECO:0000303|PubMed:10747858}; OrderedLocusNames=YNR008W;
GN   ORFNames=N2042;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7900425; DOI=10.1002/yea.320101013;
RA   Verhasselt P., Aert R., Voet M., Volckaert G.;
RT   "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT   centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL   Yeast 10:1355-1361(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=10747858; DOI=10.1074/jbc.c000144200;
RA   Oelkers P., Tinkelenberg A., Erdeniz N., Cromley D., Billheimer J.T.,
RA   Sturley S.L.;
RT   "A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol
RT   esterification in yeast.";
RL   J. Biol. Chem. 275:15609-15612(2000).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10829075; DOI=10.1073/pnas.120067297;
RA   Dahlqvist A., Stahl U., Lenman M., Banas A., Lee M., Sandager L., Ronne H.,
RA   Stymne S.;
RT   "Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the
RT   acyl-CoA-independent formation of triacylglycerol in yeast and plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6487-6492(2000).
RN   [6]
RP   CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RX   PubMed=18037386; DOI=10.1016/j.bbalip.2007.10.007;
RA   Ghosal A., Banas A., Staahl U., Dahlqvist A., Lindqvist Y., Stymne S.;
RT   "Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase
RT   (PDAT) devoid of its membrane anchor region is a soluble and active enzyme
RT   retaining its substrate specificities.";
RL   Biochim. Biophys. Acta 1771:1457-1463(2007).
RN   [7]
RP   TOPOLOGY, AND SUBCELLULAR LOCATION.
RX   PubMed=22446555; DOI=10.4161/cib.17830;
RA   Choudhary V., Jacquier N., Schneiter R.;
RT   "The topology of the triacylglycerol synthesizing enzyme Lro1 indicates
RT   that neutral lipids can be produced within the luminal compartment of the
RT   endoplasmatic reticulum: Implications for the biogenesis of lipid
RT   droplets.";
RL   Commun. Integr. Biol. 4:781-784(2011).
RN   [8]
RP   FUNCTION.
RX   PubMed=22738231; DOI=10.1042/bj20120712;
RA   Voynova N.S., Vionnet C., Ejsing C.S., Conzelmann A.;
RT   "A novel pathway of ceramide metabolism in Saccharomyces cerevisiae.";
RL   Biochem. J. 447:103-114(2012).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22454508; DOI=10.1242/jcs.100230;
RA   Wang C.W., Lee S.C.;
RT   "The ubiquitin-like (UBX)-domain-containing protein Ubx2/Ubxd8 regulates
RT   lipid droplet homeostasis.";
RL   J. Cell Sci. 125:2930-2939(2012).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND GLYCOSYLATION AT
RP   ASN-453; ASN-461; ASN-469 AND ASN-594.
RX   PubMed=30706417; DOI=10.1007/s12010-019-02954-x;
RA   Feng Y., Zhang Y., Ding W., Wu P., Cao X., Xue S.;
RT   "Expanding of phospholipid:diacylglycerol acyltransferase (PDAT) from
RT   Saccharomyces cerevisiae as multifunctional biocatalyst with broad acyl
RT   donor/acceptor selectivity.";
RL   Appl. Biochem. Biotechnol. 188:824-835(2019).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-324.
RX   PubMed=31422915; DOI=10.1016/j.devcel.2019.07.009;
RA   Barbosa A.D., Lim K., Mari M., Edgar J.R., Gal L., Sterk P., Jenkins B.J.,
RA   Koulman A., Savage D.B., Schuldiner M., Reggiori F., Wigge P.A.,
RA   Siniossoglou S.;
RT   "Compartmentalized synthesis of triacylglycerol at the inner nuclear
RT   membrane regulates nuclear organization.";
RL   Dev. Cell 50:755-766.e6(2019).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-618.
RX   PubMed=32349126; DOI=10.1083/jcb.201910177;
RA   Choudhary V., El Atab O., Mizzon G., Prinz W.A., Schneiter R.;
RT   "Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid
RT   droplet biogenesis.";
RL   J. Cell Biol. 219:0-0(2020).
CC   -!- FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA
CC       independent pathway. The enzyme specifically transfers acyl groups from
CC       the sn-2 position of a phospholipid to diacylglycerol (DAG), thus
CC       forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075,
CC       PubMed:32349126). The preferred acyl donors are
CC       phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also
CC       capable of using broad acyl donors such as phosphatidic acid (PA),
CC       phosphatidylserine (PS), phosphatidylglycerol (PG) and
CC       phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol
CC       (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more
CC       likely to use unsaturated acyl donors. As acyl acceptors, it prefers
CC       1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification
CC       activity that can utilize methanol as acyl acceptor to generate fatty
CC       acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide
CC       instead of DAG, acylating the ceramides by attaching a fatty acid to
CC       the hydroxy group on the first carbon atom of the long-chain base to
CC       produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle
CC       synthesis from the endoplasmic reticulum, promoting localized TAG
CC       production at discrete ER subdomains (PubMed:32349126). Relocates from
CC       the endoplasmic reticulum to a subdomain of the inner nuclear membrane
CC       upon nutrient starvation, where it provides a site of TAG synthesis,
CC       which is coupled with nuclear membrane remodeling (PubMed:31422915).
CC       {ECO:0000269|PubMed:10747858, ECO:0000269|PubMed:10829075,
CC       ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:30706417,
CC       ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a
CC         monoacylglycerophospholipid + a triacyl-sn-glycerol;
CC         Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615,
CC         ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158;
CC         Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386,
CC         ECO:0000269|PubMed:30706417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-
CC         glycerol = a 1,2-diacyl-sn-glycerol + a 1-acyl-sn-glycero-3-
CC         phosphocholine; Xref=Rhea:RHEA:32859, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:64683;
CC         Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32860;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC         1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-
CC         glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:44232, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753,
CC         ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC         Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44233;
CC         Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1,2-di-
CC         (9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol
CC         + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:44236, ChEBI:CHEBI:28610, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:53753, ChEBI:CHEBI:74669;
CC         Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44237;
CC         Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-
CC         octadecenoyl)-sn-glycerol = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphocholine + di-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:44240,
CC         ChEBI:CHEBI:28610, ChEBI:CHEBI:74669, ChEBI:CHEBI:75757,
CC         ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44241;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-(9Z-
CC         octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:44244,
CC         ChEBI:CHEBI:28610, ChEBI:CHEBI:52323, ChEBI:CHEBI:73990,
CC         ChEBI:CHEBI:74669; Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44245;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-
CC         hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-
CC         octadecenoyl-3-hexadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-
CC         glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44248,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:75583,
CC         ChEBI:CHEBI:78813; Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44249;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-
CC         octadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-
CC         octadecenoyl-3-octadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-
CC         glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44252,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:77686,
CC         ChEBI:CHEBI:84234; Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44253;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z)-octadecenoyl-2-
CC         (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-
CC         (9Z)-octadecenoyl-3-(9Z,12Z)-octadecadienoyl-sn-glycerol + 1-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44256,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:74977,
CC         ChEBI:CHEBI:77683; Evidence={ECO:0000269|PubMed:18037386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44257;
CC         Evidence={ECO:0000305|PubMed:18037386};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22446555, ECO:0000269|PubMed:22454508,
CC       ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}; Single-pass
CC       type II membrane protein {ECO:0000269|PubMed:22446555}. Nucleus inner
CC       membrane {ECO:0000269|PubMed:31422915}; Single-pass type II membrane
CC       protein {ECO:0000255}. Note=Localizes to sites of lipid droplet
CC       biogenesis in the endoplasmic reticulum (PubMed:22454508,
CC       PubMed:32349126). Relocates from the endoplasmic reticulum to a
CC       subdomain of the inner nuclear membrane that associates with the
CC       nucleolus upon nutrient starvation (PubMed:31422915).
CC       {ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915,
CC       ECO:0000269|PubMed:32349126}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {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; X77395; CAA54576.1; -; Genomic_DNA.
DR   EMBL; Z71623; CAA96285.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10549.1; -; Genomic_DNA.
DR   PIR; S45131; S45131.
DR   RefSeq; NP_014405.1; NM_001183185.1.
DR   AlphaFoldDB; P40345; -.
DR   BioGRID; 35833; 138.
DR   DIP; DIP-6403N; -.
DR   IntAct; P40345; 2.
DR   STRING; 4932.YNR008W; -.
DR   SwissLipids; SLP:000000059; -.
DR   ESTHER; yeast-pdat; PC-sterol_acyltransferase.
DR   iPTMnet; P40345; -.
DR   MaxQB; P40345; -.
DR   PaxDb; P40345; -.
DR   PRIDE; P40345; -.
DR   EnsemblFungi; YNR008W_mRNA; YNR008W; YNR008W.
DR   GeneID; 855742; -.
DR   KEGG; sce:YNR008W; -.
DR   SGD; S000005291; LRO1.
DR   VEuPathDB; FungiDB:YNR008W; -.
DR   eggNOG; KOG2369; Eukaryota.
DR   HOGENOM; CLU_016065_1_0_1; -.
DR   InParanoid; P40345; -.
DR   OMA; WGNSTWA; -.
DR   BioCyc; YEAST:YNR008W-MON; -.
DR   BRENDA; 2.3.1.158; 984.
DR   PRO; PR:P40345; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P40345; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0003824; F:catalytic activity; IMP:SGD.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase activity; IDA:SGD.
DR   GO; GO:0006672; P:ceramide metabolic process; IDA:SGD.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0019915; P:lipid storage; IDA:SGD.
DR   GO; GO:0055091; P:phospholipid homeostasis; IDA:SGD.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IDA:SGD.
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   Acyltransferase; Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..661
FT                   /note="Phospholipid:diacylglycerol acyltransferase"
FT                   /id="PRO_0000058268"
FT   TOPO_DOM        1..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:22446555"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..661
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:22446555"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..50
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           64..71
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           322..326
FT                   /note="GHSXG lipase motif"
FT                   /evidence="ECO:0000305|PubMed:31422915"
FT   COMPBIAS        11..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        324
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT   ACT_SITE        567
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT   ACT_SITE        618
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCC3,
FT                   ECO:0000305|PubMed:32349126"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30706417"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30706417"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30706417"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30706417"
FT   MUTAGEN         324
FT                   /note="S->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:31422915"
FT   MUTAGEN         618
FT                   /note="H->A: Abolishes catalytic activity. Fails to
FT                   localize to lipid droplet biogenesis sites on the ER."
FT                   /evidence="ECO:0000269|PubMed:32349126"
SQ   SEQUENCE   661 AA;  75393 MW;  01C043319A836F44 CRC64;
     MGTLFRRNVQ NQKSDSDENN KGGSVHNKRE SRNHIHHQQG LGHKRRRGIS GSAKRNERGK
     DFDRKRDGNG RKRWRDSRRL IFILGAFLGV LLPFSFGAYH VHNSDSDLFD NFVNFDSLKV
     YLDDWKDVLP QGISSFIDDI QAGNYSTSSL DDLSENFAVG KQLLRDYNIE AKHPVVMVPG
     VISTGIESWG VIGDDECDSS AHFRKRLWGS FYMLRTMVMD KVCWLKHVML DPETGLDPPN
     FTLRAAQGFE STDYFIAGYW IWNKVFQNLG VIGYEPNKMT SAAYDWRLAY LDLERRDRYF
     TKLKEQIELF HQLSGEKVCL IGHSMGSQII FYFMKWVEAE GPLYGNGGRG WVNEHIDSFI
     NAAGTLLGAP KAVPALISGE MKDTIQLNTL AMYGLEKFFS RIERVKMLQT WGGIPSMLPK
     GEEVIWGDMK SSSEDALNNN TDTYGNFIRF ERNTSDAFNK NLTMKDAINM TLSISPEWLQ
     RRVHEQYSFG YSKNEEELRK NELHHKHWSN PMEVPLPEAP HMKIYCIYGV NNPTERAYVY
     KEEDDSSALN LTIDYESKQP VFLTEGDGTV PLVAHSMCHK WAQGASPYNP AGINVTIVEM
     KHQPDRFDIR GGAKSAEHVD ILGSAELNDY ILKIASGNGD LVEPRQLSNL SQWVSQMPFP
     M
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024