ID A0A2Y9ELU1_PHYMC Unreviewed; 314 AA.
AC A0A2Y9ELU1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Elongation of very long chain fatty acids protein 4 {ECO:0000256|HAMAP-Rule:MF_03204};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03204};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL4 {ECO:0000256|HAMAP-Rule:MF_03204};
DE AltName: Full=ELOVL fatty acid elongase 4 {ECO:0000256|HAMAP-Rule:MF_03204};
DE Short=ELOVL FA elongase 4 {ECO:0000256|HAMAP-Rule:MF_03204};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 4 {ECO:0000256|HAMAP-Rule:MF_03204};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 4 {ECO:0000256|HAMAP-Rule:MF_03204};
GN Name=ELOVL4 {ECO:0000256|HAMAP-Rule:MF_03204,
GN ECO:0000313|RefSeq:XP_007104948.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007104948.1};
RN [1] {ECO:0000313|RefSeq:XP_007104948.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007104948.1};
RG RefSeq;
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 specifically elongates C24:0
CC and C26:0 acyl-CoAs. May participate to the production of saturated and
CC monounsaturated VLCFAs of different chain lengths that are involved in
CC multiple biological processes as precursors of membrane lipids and
CC lipid mediators. May play a critical role in early brain and skin
CC development. {ECO:0000256|HAMAP-Rule:MF_03204}.
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_03204,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_03204}.
CC -!- SUBUNIT: Oligomer. {ECO:0000256|HAMAP-Rule:MF_03204}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03204}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03204}. 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_03204}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03204}.
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DR RefSeq; XP_007104948.1; XM_007104886.4.
DR AlphaFoldDB; A0A2Y9ELU1; -.
DR STRING; 9755.ENSPCTP00005002902; -.
DR Ensembl; ENSPCTT00005003183; ENSPCTP00005002902; ENSPCTG00005002097.
DR GeneID; 102992831; -.
DR KEGG; pcad:102992831; -.
DR CTD; 6785; -.
DR InParanoid; A0A2Y9ELU1; -.
DR OrthoDB; 168669at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000248484; Chromosome 11.
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:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
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_03204; VLCF_elongase_4; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033678; ELOVL4.
DR PANTHER; PTHR11157:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 4; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03204};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03204};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03204};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03204}.
FT TRANSMEM 45..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT REGION 276..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..314
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 36709 MW; 16CA7E948B5CF9A4 CRC64;
MGLLDSEPGS VLNVVSTALN DTVEFYRWTL SITDKRVENW PMMQSPLPTL CISTLYLLFV
WLGPKWMKDR EPFQMRLALI IYNFGMVLLN LFIFRELFMG SYNAGYSYIC QSVDYSDNVH
EVRIAAALWW YFISKGIEYL DTVFFILRKK NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ
AFFGAQMNSF IHVIMYSYYG LTAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD
CPFPKWMHWA LIAYAVSFIC LFLNFYVRTY KEPKKAKPGK TAANGISANG VNQSENHLVV
ENGKKQKNGK AKRE
//
