ID Q3T120_BOVIN Unreviewed; 279 AA.
AC Q3T120;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
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,
GN ECO:0000313|EMBL:AAI02159.1,
GN ECO:0000313|Ensembl:ENSBTAP00000072145.1};
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:AAI02159.1};
RN [1] {ECO:0000313|EMBL:AAI02159.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Crossbred x Angus {ECO:0000313|EMBL:AAI02159.1};
RC TISSUE=Ileum {ECO:0000313|EMBL:AAI02159.1};
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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000072145.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072145.1,
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:ENSBTAP00000072145.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072145.1};
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. Important for saturated C24:0 and
CC monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65
CC via production of VLCFAs. {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 -!- SUBUNIT: Interacts with LASS2, TECR and HSD17B12. {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 EMBL; BC102158; AAI02159.1; -; mRNA.
DR RefSeq; NP_001029875.1; NM_001034703.2.
DR RefSeq; XP_005204882.1; XM_005204825.2.
DR RefSeq; XP_005204883.1; XM_005204826.1.
DR RefSeq; XP_005204884.1; XM_005204827.3.
DR PaxDb; 9913-ENSBTAP00000012940; -.
DR Ensembl; ENSBTAT00000086981.1; ENSBTAP00000072145.1; ENSBTAG00000016899.6.
DR GeneID; 540348; -.
DR KEGG; bta:540348; -.
DR CTD; 64834; -.
DR VEuPathDB; HostDB:ENSBTAG00000016899; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT00390000011838; -.
DR HOGENOM; CLU_048483_0_0_1; -.
DR TreeFam; TF323454; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000016899; Expressed in zone of skin and 103 other cell types or tissues.
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: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_03201; VLCF_elongase_1; 1.
DR InterPro; IPR030457; ELO_CS.
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.
DR PROSITE; PS01188; ELO; 1.
PE 2: Evidence at transcript level;
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:UP000009136};
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 29..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 137..156
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 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 227..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 275..279
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201"
SQ SEQUENCE 279 AA; 32683 MW; 645F3E991CAB128C CRC64;
MEAIVNLYQE MMKHADPRVQ GYPLMESPLL MTSILLTYVY FVLSLGPRIM ANRKPFQLRG
FMVVYNFSLV ALSLYIVYEF LMSGWLSSYT WRCDPVDFSN NPEALRMVRV AWLFLFSKFI
ELIDTLIFVL RKKDGQVTFL HVFHHSVLPW SWWWGVKIAP GGMGSFHAMI NSSVHVVMYL
YYGLSALGPV AQPYLWWKKH MTAIQLIQFV LVSLHISQYY FLPSCNYQYP VIIHLIWMYG
TIFFVLFSNF WYQSYTKGKR LPRVSQQNGV PGTTKVKAN
//
