ELO2_YEAST
ID ELO2_YEAST Reviewed; 347 AA.
AC P25358; D6VR44;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Elongation of fatty acids protein 2 {ECO:0000303|PubMed:9211877};
DE EC=2.3.1.199 {ECO:0000269|PubMed:12684876};
DE AltName: Full=3-keto acyl-CoA synthase ELO2 {ECO:0000305};
DE AltName: Full=Fenpropimorph resistance protein 1 {ECO:0000303|PubMed:8246690};
DE AltName: Full=Glucan synthesis protein 1 {ECO:0000303|PubMed:7768822};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 2 {ECO:0000305};
DE AltName: Full=v-SNARE bypass mutant gene 2 protein {ECO:0000303|PubMed:9832547};
GN Name=ELO2 {ECO:0000303|PubMed:9211877};
GN Synonyms=FEN1 {ECO:0000303|PubMed:8246690},
GN GNS1 {ECO:0000303|PubMed:7768822}, VBM2 {ECO:0000303|PubMed:9832547};
GN OrderedLocusNames=YCR034W {ECO:0000312|SGD:S000000630};
GN ORFNames=YCR34W, YCR521;
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], AND FUNCTION.
RX PubMed=7768822; DOI=10.1128/jb.177.11.3227-3234.1995;
RA El-Sherbeini M., Clemas J.A.;
RT "Cloning and characterization of GNS1: a Saccharomyces cerevisiae gene
RT involved in synthesis of 1,3-beta-glucan in vitro.";
RL J. Bacteriol. 177:3227-3234(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=9832547; DOI=10.1083/jcb.143.5.1167;
RA David D., Sundarababu S., Gerst J.E.;
RT "Involvement of long chain fatty acid elongation in the trafficking of
RT secretory vesicles in yeast.";
RL J. Cell Biol. 143:1167-1182(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=1964349; DOI=10.1002/yea.320060609;
RA Thierry A., Fairhead C., Dujon B.;
RT "The complete sequence of the 8.2 kb segment left of MAT on chromosome III
RT reveals five ORFs, including a gene for a yeast ribokinase.";
RL Yeast 6:521-534(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1776366; DOI=10.1002/yea.320070711;
RA Wicksteed B.L., Roberts A.B., Sagliocco F.A., Brown A.J.P.;
RT "The complete sequence of a 7.5 kb region of chromosome III from
RT Saccharomyces cerevisiae that lies between CRY1 and MAT.";
RL Yeast 7:761-772(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [6]
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 [7]
RP IDENTIFICATION.
RX PubMed=8246690; DOI=10.1007/bf02537499;
RA Ladeveze V., Marcireau C., Delourme D., Karst F.;
RT "General resistance to sterol biosynthesis inhibitors in Saccharomyces
RT cerevisiae.";
RL Lipids 28:907-912(1993).
RN [8]
RP FUNCTION.
RX PubMed=9211877; DOI=10.1074/jbc.272.28.17376;
RA Oh C.-S., Toke D.A., Mandala S., Martin C.E.;
RT "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene,
RT function in fatty acid elongation and are required for sphingolipid
RT formation.";
RL J. Biol. Chem. 272:17376-17384(1997).
RN [9]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12087109; DOI=10.1074/jbc.m205620200;
RA Han G., Gable K., Kohlwein S.D., Beaudoin F., Napier J.A., Dunn T.M.;
RT "The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of
RT the microsomal fatty acid elongase.";
RL J. Biol. Chem. 277:35440-35449(2002).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12684876; DOI=10.1007/s00438-003-0836-0;
RA Roessler H., Rieck C., Delong T., Hoja U., Schweizer E.;
RT "Functional differentiation and selective inactivation of multiple
RT Saccharomyces cerevisiae genes involved in very-long-chain fatty acid
RT synthesis.";
RL Mol. Genet. Genomics 269:290-298(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17719544; DOI=10.1016/j.cell.2007.06.031;
RA Denic V., Weissman J.S.;
RT "A molecular caliper mechanism for determining very long-chain fatty acid
RT length.";
RL Cell 130:663-677(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP FUNCTION.
RX PubMed=29458843; DOI=10.1016/j.micres.2017.11.001;
RA Wang Q., Du X., Ma K., Shi P., Liu W., Sun J., Peng M., Huang Z.;
RT "A critical role for very long-chain fatty acid elongases in oleic acid-
RT mediated Saccharomyces cerevisiae cytotoxicity.";
RL Microbiol. Res. 207:1-7(2018).
CC -!- FUNCTION: Component of a microsomal membrane-bound long-chain fatty
CC acid elongation system, which produces the 20-26-carbon very long-chain
CC fatty acids (VLCFA) from long-chain fatty acid precursors and is
CC involved ceramide and inositol sphingolipid biosynthesis. Component of
CC elongase II, which elongates 16-18 carbon fatty acyl-CoAs such as
CC palmitoyl-CoA and stearoyl-CoA to 20-22-carbon fatty acids by
CC incorporation of malonyl-CoA (PubMed:9211877, PubMed:12684876).
CC Involved in the synthesis of 1,3-beta-glucan (PubMed:7768822). The
CC enzymes active site faces the cytosol, whereas VLCFA length is
CC determined by a lysine near the luminal end of transmembrane helix 6
CC (PubMed:17719544). Plays an important role in lipotoxic cell death
CC induced by oleic acid through maintaining a balanced fatty acid
CC composition in thr plasma membrane (PubMed:29458843).
CC {ECO:0000269|PubMed:12684876, ECO:0000269|PubMed:17719544,
CC ECO:0000269|PubMed:29458843, ECO:0000269|PubMed:7768822,
CC ECO:0000269|PubMed:9211877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000269|PubMed:12684876};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65115;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC Evidence={ECO:0000269|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71451;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000269|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetracosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:36507, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:73977;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36508;
CC Evidence={ECO:0000269|PubMed:17719544};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9832547}; Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The C-terminal di-lysine-like motif may confer endoplasmic
CC reticulum localization. {ECO:0000303|PubMed:9832547}.
CC -!- DOMAIN: The HxxHH motif is essential for ELOp function in vivo and 3-
CC keto acyl-CoA synthase activity in vitro.
CC {ECO:0000269|PubMed:17719544}.
CC -!- MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; S78624; AAB21260.1; -; Genomic_DNA.
DR EMBL; X56909; CAA40226.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42301.1; -; Genomic_DNA.
DR EMBL; AF012655; AAB87766.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07513.1; -; Genomic_DNA.
DR PIR; S12916; S12916.
DR RefSeq; NP_009963.1; NM_001178748.1.
DR AlphaFoldDB; P25358; -.
DR SMR; P25358; -.
DR BioGRID; 31017; 546.
DR DIP; DIP-4176N; -.
DR IntAct; P25358; 22.
DR MINT; P25358; -.
DR STRING; 4932.YCR034W; -.
DR SwissLipids; SLP:000000493; -.
DR iPTMnet; P25358; -.
DR MaxQB; P25358; -.
DR PaxDb; P25358; -.
DR PRIDE; P25358; -.
DR EnsemblFungi; YCR034W_mRNA; YCR034W; YCR034W.
DR GeneID; 850400; -.
DR KEGG; sce:YCR034W; -.
DR SGD; S000000630; ELO2.
DR VEuPathDB; FungiDB:YCR034W; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_6_1_1; -.
DR InParanoid; P25358; -.
DR OMA; PISWVPI; -.
DR BioCyc; MetaCyc:YCR034W-MON; -.
DR BioCyc; YEAST:YCR034W-MON; -.
DR PRO; PR:P25358; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25358; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0009922; F:fatty acid elongase activity; IMP:SGD.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IMP:SGD.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..347
FT /note="Elongation of fatty acids protein 2"
FT /id="PRO_0000207549"
FT TOPO_DOM 1..62
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 63..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 97..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..122
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 123..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 147..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..200
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 232..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..275
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 276..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MOTIF 178..182
FT /note="HxxHH motif"
FT /evidence="ECO:0000305|PubMed:17719544"
FT MOTIF 344..347
FT /note="Di-lysine-like motif"
FT /evidence="ECO:0000303|PubMed:9832547"
FT SITE 255
FT /note="Determines the chain length of the elongated VLCFA"
FT /evidence="ECO:0000305|PubMed:17719544"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 347 AA; 40002 MW; 24225E49A43A1003 CRC64;
MNSLVTQYAA PLFERYPQLH DYLPTLERPF FNISLWEHFD DVVTRVTNGR FVPSEFQFIA
GELPLSTLPP VLYAITAYYV IIFGGRFLLS KSKPFKLNGL FQLHNLVLTS LSLTLLLLMV
EQLVPIIVQH GLYFAICNIG AWTQPLVTLY YMNYIVKFIE FIDTFFLVLK HKKLTFLHTY
HHGATALLCY TQLMGTTSIS WVPISLNLGV HVVMYWYYFL AARGIRVWWK EWVTRFQIIQ
FVLDIGFIYF AVYQKAVHLY FPILPHCGDC VGSTTATFAG CAIISSYLVL FISFYINVYK
RKGTKTSRVV KRAHGGVAAK VNEYVNVDLK NVPTPSPSPK PQHRRKR
