ELO5_CAEEL
ID ELO5_CAEEL Reviewed; 274 AA.
AC Q20300; V6CLH1;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Elongation of long chain fatty acids protein 5;
DE Short=ELO-5 {ECO:0000303|PubMed:15340492};
DE EC=2.3.1.- {ECO:0000269|PubMed:15340492};
DE AltName: Full=3-keto acyl-CoA synthase elo-5;
DE AltName: Full=Long-chain 3-oxoacyl-CoA synthase 5;
DE Short=CEELO5;
DE AltName: Full=Monomethyl branched-chain fatty acid elongase 5;
DE Short=mmBCFA elongase 5;
GN Name=elo-5 {ECO:0000312|WormBase:F41H10.7};
GN ORFNames=F41H10.7 {ECO:0000312|WormBase:F41H10.7};
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, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 isopentadecanoate (C15iso) and isoheptadecanoate (C17iso), both play
CC critical roles in animal development and growth.
CC {ECO:0000269|PubMed:15340492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-methyldodecanoyl-CoA + H(+) + malonyl-CoA = 3-
CC oxoisopentadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35291,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71427, ChEBI:CHEBI:71430;
CC Evidence={ECO:0000269|PubMed:15340492};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35292;
CC Evidence={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 and unidentified head cells.
CC {ECO:0000269|PubMed:15340492}.
CC -!- DISRUPTION PHENOTYPE: Loss of function induces an egg-laying defect
CC from the second day of adulthood with progeny arrested at the larval
CC stage L1. The small larvae maintain morphological integrity and survive
CC for up to 3 to 4 days. Animals had reduced levels of isoheptadecanoate
CC (C17iso) and isopentadecanoate (C15iso). The phenotype could be fully
CC suppressed by feeding with C17iso and partially suppressed by feeding
CC with C15iso. {ECO:0000269|PubMed:15340492}.
CC -!- SIMILARITY: Belongs to the ELO family. {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; BX284604; CDK13459.1; -; Genomic_DNA.
DR PIR; E88690; E88690.
DR RefSeq; NP_001293757.1; NM_001306828.1.
DR AlphaFoldDB; Q20300; -.
DR SMR; Q20300; -.
DR STRING; 6239.F41H10.7; -.
DR SwissLipids; SLP:000000028; -.
DR SwissLipids; SLP:000000188; -.
DR EPD; Q20300; -.
DR PaxDb; Q20300; -.
DR PeptideAtlas; Q20300; -.
DR EnsemblMetazoa; F41H10.7.1; F41H10.7.1; WBGene00001243.
DR UCSC; F41H10.7; c. elegans.
DR WormBase; F41H10.7; CE49372; WBGene00001243; elo-5.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_0_1; -.
DR InParanoid; Q20300; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q20300; -.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q20300; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001243; Expressed in larva and 3 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; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; 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 5"
FT /id="PRO_0000421276"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..156
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..227
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 31720 MW; D31E2846EAFE0AD9 CRC64;
MMDQILGTNF TYEGAKEVAR GLEGFSAKLA VGYIATIFGL KYYMKDRKAF DLSTPLNIWN
GILSTFSLLG FLFTFPTLLS VIRKDGFSHT YSHVSELYTD STSGYWIFLW VISKIPELLD
TVFIVLRKRP LIFMHWYHHA LTGYYALVCY HEDAVHMVWV VWMNYIIHAF MYGYYLLKSL
KVPIPPSVAQ AITTSQMVQF AVAIFAQVHV SYKHYVEGVE GLAYSFRGTA IGFFMLTTYF
YLWIQFYKEH YLKNGGKKYN LAKDQAKTQT KKAN
