ID G3TK02_LOXAF Unreviewed; 300 AA.
AC G3TK02;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000256|HAMAP-Rule:MF_03205};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03205};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL5 {ECO:0000256|HAMAP-Rule:MF_03205};
DE AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000256|HAMAP-Rule:MF_03205};
DE Short=ELOVL FA elongase 5 {ECO:0000256|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000256|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000256|HAMAP-Rule:MF_03205};
GN Name=ELOVL5 {ECO:0000256|HAMAP-Rule:MF_03205,
GN ECO:0000313|Ensembl:ENSLAFP00000015107.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015107.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015107.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015107.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000015107.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015107.2};
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 acts specifically toward
CC polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6)
CC acyl-CoA. May participate to the production of monounsaturated and of
CC polyunsaturated 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_03205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-
CC eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:75121, ChEBI:CHEBI:76559;
CC Evidence={ECO:0000256|ARBA:ARBA00001296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680;
CC Evidence={ECO:0000256|ARBA:ARBA00001296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:73852; Evidence={ECO:0000256|ARBA:ARBA00000904};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000256|ARBA:ARBA00000904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71481; Evidence={ECO:0000256|ARBA:ARBA00000735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000256|ARBA:ARBA00000735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489,
CC ChEBI:CHEBI:71491; Evidence={ECO:0000256|ARBA:ARBA00000337};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC Evidence={ECO:0000256|ARBA:ARBA00000337};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC Evidence={ECO:0000256|ARBA:ARBA00001297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000256|ARBA:ARBA00001297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC Evidence={ECO:0000256|ARBA:ARBA00001347};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000256|ARBA:ARBA00001347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC 3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC Evidence={ECO:0000256|ARBA:ARBA00000592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000256|ARBA:ARBA00000592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:74054; Evidence={ECO:0000256|ARBA:ARBA00001158};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000256|ARBA:ARBA00001158};
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_03205,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03205}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite
CC {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein
CC localizes to the soma and proximal portion of the dendritic tree.
CC {ECO:0000256|HAMAP-Rule:MF_03205}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03205}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G3TK02; -.
DR STRING; 9785.ENSLAFP00000015107; -.
DR Ensembl; ENSLAFT00000018022.2; ENSLAFP00000015107.2; ENSLAFG00000018020.2.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; G3TK02; -.
DR OMA; PISWVPI; -.
DR TreeFam; TF323454; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:InterPro.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; 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_03205; VLCF_elongase_5; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033677; ELOVL5.
DR PANTHER; PTHR11157:SF18; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 5; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273, ECO:0000256|HAMAP-
KW Rule:MF_03205}; Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03205};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03205};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03205};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03205,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03205,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03205};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03205};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03205};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03205}.
FT TRANSMEM 33..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 115..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 145..162
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 208..225
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT REGION 272..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 35473 MW; 8545580CF9FE2C9D CRC64;
MEHFDASLST YFKALLGPRA DTRVKGWFLL DNYIPTFICS ILYLLIVWLG PKYMRNRQPF
SCRGILVVYN LGLTLLSLYM FCELVTGVWE GKYNFFCQGT RSAGESDMKI IRVLWWYYFS
KLIEFMDTFF FILRKNNHQI TVLHVYHHVS MLNIWWFVMN WVPCGHCYFG ATLNSFIHVL
MYSYYGLSSV PSMRPYLWWK KYITQGQLLQ FVLTIIQTSL GVIWPCSFPL GWLYFQIGYM
ISLIALFTNF YIQTYNKKGA SRRKDHLKDH QNGSLATVNG HTNSFSSLEN HVKPRKQRKD
//
