ID A5PKE6_BOVIN Unreviewed; 314 AA.
AC A5PKE6;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
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|EMBL:AAI42460.1, ECO:0000313|Ensembl:ENSBTAP00000020598.5,
GN ECO:0000313|VGNC:VGNC:28450};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI42460.1};
RN [1] {ECO:0000313|EMBL:AAI42460.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI42460.1};
RC TISSUE=Thymus {ECO:0000313|EMBL:AAI42460.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000020598.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020598.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000020598.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020598.5};
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 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 EMBL; BC142459; AAI42460.1; -; mRNA.
DR RefSeq; NP_001092520.1; NM_001099050.1.
DR STRING; 9913.ENSBTAP00000020598; -.
DR PaxDb; 9913-ENSBTAP00000020598; -.
DR Ensembl; ENSBTAT00000020598.6; ENSBTAP00000020598.5; ENSBTAG00000015498.6.
DR GeneID; 532015; -.
DR KEGG; bta:532015; -.
DR CTD; 6785; -.
DR VEuPathDB; HostDB:ENSBTAG00000015498; -.
DR VGNC; VGNC:28450; ELOVL4.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR OMA; WTYFTST; -.
DR OrthoDB; 168669at2759; -.
DR TreeFam; TF323454; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009136; Chromosome 9.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
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:UP000009136};
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 275..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 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 36626 MW; EFF1DAD700FAEB7F CRC64;
MGLLDSEPGS VLNAVSTALN DTVEFYRWTL SITDKRVENW PLMQSPLPTL CISTLYLLFV
WLGPKWMKDR EPFQMRLVLI LYNFGMVLLN LFIFRELLMG SYNAGYSYIC QTVDYSDNVH
EVRIAAALWW YFISKGIEYL DTVFFILRKK NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ
AFFGAQINSF IHVIMYSYYG LAAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD
CPFPKWMHWA LIVYAVSFIF LFLNFYVRTY KEPKKAKPGK TATNGISANG VNKSENHLVV
ENGKKQKNGK AKGE
//
