ELO2_CAEEL
ID ELO2_CAEEL Reviewed; 274 AA.
AC Q9XVQ9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Elongation of long chain fatty acids protein 2;
DE Short=ELO-2 {ECO:0000303|PubMed:12586704};
DE EC=2.3.1.- {ECO:0000269|PubMed:12586704};
DE AltName: Full=F11E6.5/ELO-2 {ECO:0000303|PubMed:12586704};
DE AltName: Full=Long-chain 3-oxoacyl-CoA synthase 2;
DE Short=CEELO2;
GN Name=elo-2 {ECO:0000303|PubMed:12586704, ECO:0000312|WormBase:F11E6.5};
GN ORFNames=F11E6.5 {ECO:0000312|WormBase:F11E6.5};
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=12586704; DOI=10.1093/genetics/163.1.159;
RA Kniazeva M., Sieber M., McCauley S., Zhang K., Watts J.L., Han M.;
RT "Suppression of the ELO-2 FA elongation activity results in alterations of
RT the fatty acid composition and multiple physiological defects, including
RT abnormal ultradian rhythms, in Caenorhabditis elegans.";
RL Genetics 163:159-169(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 responsible for the elongation of
CC palmitate (hexadecanoate, 16:0), also involved in polyunsaturated fatty
CC acid (PUFA) biosynthesis. {ECO:0000269|PubMed:12586704,
CC ECO:0000269|PubMed:32961767}.
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:12586704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000269|PubMed:12586704};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:12586704}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in various tissues and parts of the body,
CC including the ventral cord, pharyngeal muscles, uterus, and the tail,
CC and most strongly in intestinal cells. {ECO:0000269|PubMed:12586704}.
CC -!- DISRUPTION PHENOTYPE: Suppression of ELO-2 causes an accumulation of
CC palmitate and an associated decrease in the PUFA fraction in
CC triacylglycerides and phospholipid classes. This imbalance in the fatty
CC acid composition results in multiple phenotypic defects such as slow
CC growth, small body size, reproductive defects, and changes in rhythmic
CC behavior (PubMed:12586704). Suppression of ELO-2 decreases growth rate
CC and reduces brood size (PubMed:32961767). {ECO:0000269|PubMed:12586704,
CC ECO:0000269|PubMed:32961767}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; BX284604; CAB02921.1; -; Genomic_DNA.
DR PIR; T20786; T20786.
DR RefSeq; NP_503114.1; NM_070713.5.
DR AlphaFoldDB; Q9XVQ9; -.
DR SMR; Q9XVQ9; -.
DR DIP; DIP-26940N; -.
DR STRING; 6239.F11E6.5; -.
DR SwissLipids; SLP:000000573; -.
DR EPD; Q9XVQ9; -.
DR PaxDb; Q9XVQ9; -.
DR PeptideAtlas; Q9XVQ9; -.
DR EnsemblMetazoa; F11E6.5.1; F11E6.5.1; WBGene00001240.
DR GeneID; 178532; -.
DR KEGG; cel:CELE_F11E6.5; -.
DR UCSC; F11E6.5.1; c. elegans.
DR CTD; 178532; -.
DR WormBase; F11E6.5; CE19785; WBGene00001240; elo-2.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_0_1; -.
DR InParanoid; Q9XVQ9; -.
DR OMA; HQAWARW; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9XVQ9; -.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001240; 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:0008340; P:determination of adult lifespan; IMP:WormBase.
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:0006629; P:lipid metabolic process; IMP:WormBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
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 2"
FT /id="PRO_0000452611"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 274 AA; 31361 MW; 2CBB7DA5F418D714 CRC64;
MAAAQTSPAA TLVDVLTKPW SLDQTDSYMS TFVPLSYKIM IGYLVTIYFG QKLMAHRKPF
DLQNTLALWN FGFSLFSGIA AYKLIPELFG VFMKDGFVAS YCQNENYYTD ASTGFWGWAF
VMSKAPELGD TMFLVLRKKP VIFMHWYHHA LTFVYAVVTY SEHQAWARWS LALNLAVHTV
MYFYFAVRAL NIQTPRPVAK FITTIQIVQF VISCYIFGHL VFIKSADSVP GCAVSWNVLS
IGGLMYISYL FLFAKFFYKA YIQKRSPTKT SKQE
