ID A0A3Q2EFU3_CYPVA Unreviewed; 320 AA.
AC A0A3Q2EFU3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
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};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000031388.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000031388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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. {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 -!- SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03204}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03204}.
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DR RefSeq; XP_015238013.1; XM_015382527.1.
DR AlphaFoldDB; A0A3Q2EFU3; -.
DR Ensembl; ENSCVAT00000026304.1; ENSCVAP00000031388.1; ENSCVAG00000020620.1.
DR GeneID; 107089631; -.
DR KEGG; cvg:107089631; -.
DR CTD; 393769; -.
DR GeneTree; ENSGT01050000244838; -.
DR OMA; WTYFTST; -.
DR OrthoDB; 168669at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000265020; 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: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:SF137; 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|HAMAP-Rule:MF_03204,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03204,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03204};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
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 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03204,
FT ECO:0000256|RuleBase:RU361115"
FT REGION 266..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 37838 MW; 03F9593998258B6A CRC64;
MEIVTHLIND TIEFYKWTLT IADKRVEKWP LMDNPLPTLA ISTSYLLFLW LGPKYMKNRE
PFQLRKTLIV YNFSMVFLNF FIFKELFMAA RAAQYSYICQ PVDYSDDPNE VRVAGALWWY
FISKGIEYLD TVFFILRKKF NQVTFLHVYH HCTMFTLWWI GIKWVAGGQS FFGAHMNALI
HVLMYLYYGL ASCGPRIQKY LWWKKYLTII QMVQFHVTIG HTALSLYVNC DFPHWMHYSL
ICYAITFIVL FGNFYYQTYR RQQPTRRDAS SSTKAGKHVY NGNLNGLSRA ANGTPLVTSK
EEKPQENSGR RKRKGRAKRD
//