ELO1_CAEEL
ID ELO1_CAEEL Reviewed; 288 AA.
AC G5EEE5; K8ES54;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Elongation of long chain fatty acids protein 1;
DE Short=ELO-1;
DE EC=2.3.1.- {ECO:0000269|PubMed:10829069, ECO:0000269|PubMed:11972048};
DE AltName: Full=Long-chain 3-oxoacyl-CoA synthase 1;
DE Short=CEELO1;
GN Name=elo-1 {ECO:0000312|EMBL:CAA92958.1, ECO:0000312|WormBase:F56H11.4a};
GN ORFNames=F56H11.4 {ECO:0000312|WormBase:F56H11.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Das T., Parker-Barnes J.M., Thurmond J.M., Bobik E., Leonard A.E.,
RA Chuang L., Huang Y.-S., Mukerji P.;
RT "Identification and characterization of novel polyunsaturated fatty acid
RT elongating enzymes from Mortierella alpina and Caenorhabditis elegans.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10829069; DOI=10.1073/pnas.110140197;
RA Beaudoin F., Michaelson L.V., Hey S.J., Lewis M.J., Shewry P.R.,
RA Sayanova O., Napier J.A.;
RT "Heterologous reconstitution in yeast of the polyunsaturated fatty acid
RT biosynthetic pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6421-6426(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11972048; DOI=10.1073/pnas.092064799;
RA Watts J.L., Browse J.;
RT "Genetic dissection of polyunsaturated fatty acid synthesis in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5854-5859(2002).
RN [5]
RP FUNCTION.
RX PubMed=32961767; DOI=10.3390/cells9092127;
RA Guha S., Calarco S., Gachet M.S., Gertsch J.;
RT "Juniperonic Acid Biosynthesis is Essential in Caenorhabditis Elegans
RT Lacking Delta6 Desaturase (fat-3) and Generates New omega-3
RT Endocannabinoids.";
RL Cells 9:0-0(2020).
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle.
CC Uses malonyl-CoA to add 2 carbons per cycle to the chain of long-chain
CC fatty acids. Condensing enzyme that catalyzes the elongation of
CC monounsaturated (MUFA) and polyunsaturated (PUFA) fatty acids that are
CC involved in multiple biological processes as precursors of membrane
CC lipids and lipid mediators. {ECO:0000269|PubMed:10829069,
CC ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:32961767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71481; Evidence={ECO:0000269|PubMed:10829069,
CC ECO:0000269|PubMed:11972048};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000269|PubMed:10829069, ECO:0000269|PubMed:11972048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489,
CC ChEBI:CHEBI:71491; Evidence={ECO:0000269|PubMed:10829069,
CC ECO:0000269|PubMed:11972048};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC Evidence={ECO:0000269|PubMed:10829069, ECO:0000269|PubMed:11972048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC Evidence={ECO:0000269|PubMed:10829069};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000269|PubMed:10829069};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:10829069, ECO:0000269|PubMed:11972048}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=a;
CC IsoId=G5EEE5-1; Sequence=Displayed;
CC Name=b;
CC IsoId=G5EEE5-2; Sequence=VSP_061024;
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; AF244356; AAF70462.1; -; mRNA.
DR EMBL; BX284604; CAA92958.1; -; Genomic_DNA.
DR EMBL; BX284604; CCO25597.1; -; Genomic_DNA.
DR PIR; T22789; T22789.
DR RefSeq; NP_001263767.1; NM_001276838.1. [G5EEE5-2]
DR RefSeq; NP_501689.1; NM_069288.7. [G5EEE5-1]
DR AlphaFoldDB; G5EEE5; -.
DR SMR; G5EEE5; -.
DR STRING; 6239.F56H11.4a; -.
DR SwissLipids; SLP:000000572; -.
DR EPD; G5EEE5; -.
DR PaxDb; G5EEE5; -.
DR PeptideAtlas; G5EEE5; -.
DR EnsemblMetazoa; F56H11.4a.1; F56H11.4a.1; WBGene00001239. [G5EEE5-1]
DR EnsemblMetazoa; F56H11.4b.1; F56H11.4b.1; WBGene00001239. [G5EEE5-2]
DR GeneID; 177787; -.
DR KEGG; cel:CELE_F56H11.4; -.
DR CTD; 177787; -.
DR WormBase; F56H11.4a; CE05979; WBGene00001239; elo-1.
DR WormBase; F56H11.4b; CE47981; WBGene00001239; elo-1.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_0_1; -.
DR InParanoid; G5EEE5; -.
DR OMA; RPLMFLH; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; G5EEE5; -.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001239; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; G5EEE5; baseline and differential.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:WormBase.
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 Alternative initiation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Elongation of long chain fatty acids protein 1"
FT /id="PRO_0000452610"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform b)"
FT /id="VSP_061024"
SQ SEQUENCE 288 AA; 33562 MW; 8BA5CD4892012B0E CRC64;
MAQHPLVQRL LDVKFDTKRF VAIATHGPKN FPDAEGRKFF ADHFDVTIQA SILYMVVVFG
TKWFMRNRQP FQLTIPLNIW NFILAAFSIA GAVKMTPEFF GTIANKGIVA SYCKVFDFTK
GENGYWVWLF MASKLFELVD TIFLVLRKRP LMFLHWYHHI LTMIYAWYSH PLTPGFNRYG
IYLNFVVHAF MYSYYFLRSM KIRVPGFIAQ AITSLQIVQF IISCAVLAHL GYLMHFTNAN
CDFEPSVFKL AVFMDTTYLA LFVNFFLQSY VLRGGKDKYK AVPKKKNN
