ELO1_YEAST
ID ELO1_YEAST Reviewed; 310 AA.
AC P39540; D6VVZ6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Elongation of fatty acids protein 1 {ECO:0000303|PubMed:8702485};
DE EC=2.3.1.199 {ECO:0000269|PubMed:9546663};
DE AltName: Full=3-keto acyl-CoA synthase ELO1 {ECO:0000305};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 1 {ECO:0000305};
GN Name=ELO1 {ECO:0000303|PubMed:8702485};
GN OrderedLocusNames=YJL196C {ECO:0000312|SGD:S000003732}; ORFNames=J0343;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8702485; DOI=10.1074/jbc.271.31.18413;
RA Toke D.A., Martin C.E.;
RT "Isolation and characterization of a gene affecting fatty acid elongation
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:18413-18422(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9546663; DOI=10.1046/j.1432-1327.1998.2520477.x;
RA Dittrich F., Zajonc D., Huhne K., Hoja U., Ekici A., Greiner E., Klein H.,
RA Hofmann J., Bessoule J.J., Sperling P., Schweizer E.;
RT "Fatty acid elongation in yeast--biochemical characteristics of the enzyme
RT system and isolation of elongation-defective mutants.";
RL Eur. J. Biochem. 252:477-485(1998).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10850979; DOI=10.1128/jb.182.13.3655-3660.2000;
RA Schneiter R., Tatzer V., Gogg G., Leitner E., Kohlwein S.D.;
RT "Elo1p-dependent carboxy-terminal elongation of C14:1Delta(9) to
RT C16:1Delta(11) fatty acids in Saccharomyces cerevisiae.";
RL J. Bacteriol. 182:3655-3660(2000).
RN [7]
RP FUNCTION.
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 [8]
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 [9]
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 [10]
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).
CC -!- FUNCTION: Component of a microsomal membrane bound medium-chain fatty
CC acid elongation system, which extends medium-chain-length fatty acids
CC to long-chain fatty acids. Component of elongase I, which extends 12-
CC 16-carbon fatty acyl-CoAs such as lauroyl-CoA to 14-18-carbon fatty
CC acids by incorporation of malonyl-CoA. {ECO:0000269|PubMed:10850979,
CC ECO:0000269|PubMed:12684876, ECO:0000269|PubMed:8702485,
CC ECO:0000269|PubMed:9546663}.
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:9546663};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:8702485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000269|PubMed:8702485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC hexadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:42356,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:65060, ChEBI:CHEBI:79021;
CC Evidence={ECO:0000269|PubMed:10850979};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42357;
CC Evidence={ECO:0000269|PubMed:10850979};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for octanoyl-CoA {ECO:0000269|PubMed:9546663};
CC KM=0.83 mM for decanoyl-CoA {ECO:0000269|PubMed:9546663};
CC KM=0.05 mM for lauroyl-CoA {ECO:0000269|PubMed:9546663};
CC KM=0.4 mM for myristoyl-CoA {ECO:0000269|PubMed:9546663};
CC KM=0.13 mM for palmitoyl-CoA {ECO:0000269|PubMed:9546663};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced in wild-type cells supplemented with 14:0 fatty
CC acids and repressed when cells are supplied with 16- and 18-carbon
CC fatty acids.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000303|PubMed:8702485}.
CC -!- DOMAIN: The HxxHH motif is essential for ELOp function in vivo and 3-
CC keto acyl-CoA synthase activity in vitro.
CC {ECO:0000250|UniProtKB:P40319}.
CC -!- MISCELLANEOUS: Present with 937 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; X77688; CAA54764.1; -; Genomic_DNA.
DR EMBL; Z49471; CAA89491.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08612.1; -; Genomic_DNA.
DR PIR; S46638; S46638.
DR RefSeq; NP_012339.1; NM_001181629.1.
DR AlphaFoldDB; P39540; -.
DR SMR; P39540; -.
DR BioGRID; 33568; 105.
DR DIP; DIP-8755N; -.
DR IntAct; P39540; 6.
DR MINT; P39540; -.
DR STRING; 4932.YJL196C; -.
DR SwissLipids; SLP:000000576; -.
DR SwissLipids; SLP:000000876; -.
DR MaxQB; P39540; -.
DR PaxDb; P39540; -.
DR PRIDE; P39540; -.
DR EnsemblFungi; YJL196C_mRNA; YJL196C; YJL196C.
DR GeneID; 853243; -.
DR KEGG; sce:YJL196C; -.
DR SGD; S000003732; ELO1.
DR VEuPathDB; FungiDB:YJL196C; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_6_1_1; -.
DR InParanoid; P39540; -.
DR OMA; MQANWSK; -.
DR BioCyc; YEAST:G3O-31627-MON; -.
DR SABIO-RK; P39540; -.
DR PRO; PR:P39540; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39540; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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: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:0019368; P:fatty acid elongation, unsaturated fatty acid; IMP:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
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 Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Elongation of fatty acids protein 1"
FT /id="PRO_0000207548"
FT TOPO_DOM 1..63
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 64..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 101..121
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..141
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 142..163
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 175..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..201
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 202..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 235..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..271
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MOTIF 172..176
FT /note="HxxHH motif"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT MOTIF 304..307
FT /note="Di-lysine motif"
FT /evidence="ECO:0000303|PubMed:8702485"
SQ SEQUENCE 310 AA; 36234 MW; 051D5369976BF48F CRC64;
MVSDWKNFCL EKASRFRPTI DRPFFNIYLW DYFNRAVGWA TAGRFQPKDF EFTVGKQPLS
EPRPVLLFIA MYYVVIFGGR SLVKSCKPLK LRFISQVHNL MLTSVSFLWL ILMVEQMLPI
VYRHGLYFAV CNVESWTQPM ETLYYLNYMT KFVEFADTVL MVLKHRKLTF LHTYHHGATA
LLCYNQLVGY TAVTWVPVTL NLAVHVLMYW YYFLSASGIR VWWKAWVTRL QIVQFMLDLI
VVYYVLYQKI VAAYFKNACT PQCEDCLGSM TAIAAGAAIL TSYLFLFISF YIEVYKRGSA
SGKKKINKNN
