ELO3_CAEEL
ID ELO3_CAEEL Reviewed; 320 AA.
AC P49191;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative fatty acid elongation protein 3;
DE EC=2.3.1.199;
DE AltName: Full=3-keto acyl-CoA synthase elo-3;
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 3;
GN Name=elo-3; ORFNames=D2024.3;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Could be implicated in synthesis of very long chain fatty
CC acids (By similarity). May be required for normally rapid growth.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; FO080386; CCD63356.1; -; Genomic_DNA.
DR PIR; T34200; T34200.
DR RefSeq; NP_001255291.1; NM_001268362.1.
DR AlphaFoldDB; P49191; -.
DR SMR; P49191; -.
DR BioGRID; 48753; 1.
DR iPTMnet; P49191; -.
DR EPD; P49191; -.
DR PeptideAtlas; P49191; -.
DR EnsemblMetazoa; D2024.3.1; D2024.3.1; WBGene00001241.
DR UCSC; D2024.3; c. elegans.
DR WormBase; D2024.3; CE34783; WBGene00001241; elo-3.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_2_1; -.
DR InParanoid; P49191; -.
DR OMA; PISWVPI; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; P49191; -.
DR Reactome; R-CEL-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-CEL-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:P49191; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001241; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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: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; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="Putative fatty acid elongation protein 3"
FT /id="PRO_0000207546"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 320 AA; 37857 MW; B5808D92B7B51EFE CRC64;
MAKYDYNPKY GLENYSIFLP FETSFDAFRS TTWMQNHWYQ SITASVVYVA VIFTGKKIME
KYKPFQLDTP LFVWNSFLAI FSILGFLRMT PEFVWSWSAE GNSFKYSICH SSYAQGVTGF
WTEQFAMSKL FELIDTIFIV LRKRPLIFLH WYHHVTVMIY TWHAYKDHTA SGRWFIWMNY
GVHALMYSYY ALRSLKFRLP KQMAMVVTTL QLAQMVMGVI IGVTVYRIKS SGEYCQQTWD
NLGLCFGVYF TYFLLFANFF YHAYVKKNNR YTEVKKDKKE KEEPVDFEIL EPKEDINANI
AEPSITTRSA AARRKVQKAD
