ELO6_CAEEL
ID ELO6_CAEEL Reviewed; 274 AA.
AC Q20303;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Elongation of long chain fatty acids protein 6;
DE Short=ELO-6 {ECO:0000303|PubMed:15340492};
DE EC=2.3.1.- {ECO:0000269|PubMed:15340492};
DE AltName: Full=3-keto acyl-CoA synthase elo-6;
DE AltName: Full=Long-chain 3-oxoacyl-CoA synthase 6;
DE Short=CEELO6;
DE AltName: Full=Monomethyl branched-chain fatty acid elongase 6;
DE Short=mmBCFA elongase 6;
GN Name=elo-6; ORFNames=F41H10.8;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=15340492; DOI=10.1371/journal.pbio.0020257;
RA Kniazeva M., Crawford Q.T., Seiber M., Wang C.Y., Han M.;
RT "Monomethyl branched-chain fatty acids play an essential role in
RT Caenorhabditis elegans development.";
RL PLoS Biol. 2:E257-E257(2004).
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 required for the formation of
CC isoheptadecanoate (C17iso), which plays critical roles in animal
CC development and growth. {ECO:0000269|PubMed:15340492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + isopentadecanoyl-CoA + malonyl-CoA = 3-
CC oxoisoheptadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35335,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:70827, ChEBI:CHEBI:71445;
CC Evidence={ECO:0000269|PubMed:15340492};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35336;
CC Evidence={ECO:0000269|PubMed:15340492};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:15340492}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the gut, neurons, pharynx and muscles
CC of the vulva. {ECO:0000269|PubMed:15340492}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; FO081367; CCD71101.1; -; Genomic_DNA.
DR PIR; H88690; H88690.
DR RefSeq; NP_500797.1; NM_068396.4.
DR AlphaFoldDB; Q20303; -.
DR SMR; Q20303; -.
DR BioGRID; 42444; 12.
DR DIP; DIP-24907N; -.
DR STRING; 6239.F41H10.8; -.
DR SwissLipids; SLP:000000029; -.
DR SwissLipids; SLP:000000189; -.
DR EPD; Q20303; -.
DR PaxDb; Q20303; -.
DR PeptideAtlas; Q20303; -.
DR EnsemblMetazoa; F41H10.8.1; F41H10.8.1; WBGene00001244.
DR GeneID; 177321; -.
DR KEGG; cel:CELE_F41H10.8; -.
DR UCSC; F41H10.8.1; c. elegans.
DR CTD; 177321; -.
DR WormBase; F41H10.8; CE10286; WBGene00001244; elo-6.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_0_1; -.
DR InParanoid; Q20303; -.
DR OMA; ILQFVIT; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q20303; -.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q20303; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q20303; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001244; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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: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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..274
FT /note="Elongation of long chain fatty acids protein 6"
FT /id="PRO_0000421277"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 274 AA; 31671 MW; DDF0840C1454A4CD CRC64;
MPQGEVSFFE VLTTAPFSHE LSKKHIAQTQ YAAFWISMAY VVVIFGLKAV MTNRKPFDLT
GPLNLWNAGL AIFSTLGSLA TTFGLLHEFF SRGFFESYIH IGDFYNGLSG MFTWLFVLSK
VAEFGDTLFI ILRKKPLMFL HWYHHVLTMN YAFMSFEANL GFNTWITWMN FSVHSIMYGY
YMLRSFGVKV PAWIAKNITT MQILQFVITH FILFHVGYLA VTGQSVDSTP GYYWFCLLME
ISYVVLFGNF YYQSYIKGGG KKFNAEKKTE KKIE
