ID A0A3Q2V484_HAPBU Unreviewed; 324 AA.
AC A0A3Q2V484;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Elongation of very long chain fatty acids protein 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=ELOVL fatty acid elongase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE Short=ELOVL FA elongase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
GN Name=ELOVL1 {ECO:0000256|HAMAP-Rule:MF_03201};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000005712.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000005712.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle.
CC This endoplasmic reticulum-bound enzymatic process allows the addition
CC of 2 carbons to the chain of long- and very long-chain fatty acids
CC (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward
CC saturated C18 to C26 acyl-CoA substrates, with the highest activity
CC towards C22:0 acyl-CoA. May participate to the production of both
CC saturated and monounsaturated VLCFAs of different chain lengths that
CC are involved in multiple biological processes as precursors of membrane
CC lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03201}.
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; Evidence={ECO:0000256|HAMAP-Rule:MF_03201,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_03201}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03201}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03201}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000256|HAMAP-Rule:MF_03201}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03201}.
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DR RefSeq; XP_005946579.1; XM_005946517.2.
DR AlphaFoldDB; A0A3Q2V484; -.
DR STRING; 8153.ENSHBUP00000005712; -.
DR Ensembl; ENSHBUT00000006537.1; ENSHBUP00000005712.1; ENSHBUG00000007114.1.
DR GeneID; 102312907; -.
DR CTD; 406725; -.
DR GeneTree; ENSGT01050000244838; -.
DR OMA; HAMVNSM; -.
DR OrthoDB; 168669at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0048794; P:swim bladder development; IEA:Ensembl.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03201; VLCF_elongase_1; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033681; ELOVL1.
DR PANTHER; PTHR11157:SF19; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 1; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03201};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03201,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03201,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03201};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03201}.
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 145..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 235..260
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 320..324
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201"
SQ SEQUENCE 324 AA; 37599 MW; F184DE0504B20281 CRC64;
MLQEIQEMGS HAKDIYDFLL SGLDPRITDY PLMQSPITMT TILLGYLFFV LYLGPRLMAN
RKPFQLKEPM IVYNFLLVAL SIFIVYEFLM SGWATTYTWR CDAVDASNSP QALRMVQVAW
LFWFSKIIEL MDTIFFVLRK KHGQITFLHI FHHSFMPWTW WWGVAYAPGG MGSFHAMVNS
SVHVVMYFYY GLSAAGPRFQ KFLWWKKYMT AIQLIQFVLV SLHATQYYFM SSCDYQFPVI
LHLIWIYGTF FFVLFSNFWF QAYIKGKRLP KQCQNSTAVH TNGKYCENGN GVKNGTANGV
SHGVTNGSVH HENGSSYMGK MKKA
//
