ELOV5_RAT
ID ELOV5_RAT Reviewed; 299 AA.
AC Q920L7; G9BD46;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268};
DE AltName: Full=3-keto acyl-CoA synthase Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Fatty acid elongase 1;
DE Short=rELO1;
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
GN Name=Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12005057; DOI=10.1271/bbb.66.613;
RA Inagaki K., Aki T., Fukuda Y., Kawamoto S., Shigeta S., Ono K., Suzuki O.;
RT "Identification and expression of a rat fatty acid elongase involved in the
RT biosynthesis of C18 fatty acids.";
RL Biosci. Biotechnol. Biochem. 66:613-621(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22216341; DOI=10.1371/journal.pone.0029662;
RA Gregory M.K., Gibson R.A., Cook-Johnson R.J., Cleland L.G., James M.J.;
RT "Elongase reactions as control points in long-chain polyunsaturated fatty
RT acid synthesis.";
RL PLoS ONE 6:E29662-E29662(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF SER-218; CYS-219;
RP GLY-220; TRP-231 AND TYR-233.
RX PubMed=23873268; DOI=10.1194/jlr.m041368;
RA Gregory M.K., Cleland L.G., James M.J.;
RT "Molecular basis for differential elongation of omega-3 docosapentaenoic
RT acid by the rat Elovl5 and Elovl2.";
RL J. Lipid Res. 54:2851-2857(2013).
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 in 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 (By similarity) (PubMed:22216341, PubMed:23873268). In
CC conditions where the essential linoleic and alpha linoleic fatty acids
CC are lacking it is also involved in the synthesis of Mead acid from
CC oleic acid (By similarity). {ECO:0000250|UniProtKB:Q8BHI7,
CC ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:22216341,
CC ECO:0000269|PubMed:23873268}.
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:0000255|HAMAP-Rule:MF_03205,
CC ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:22216341};
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:0000269|PubMed:22216341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC Evidence={ECO:0000305|PubMed:22216341};
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:0000269|PubMed:22216341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000305|PubMed:22216341};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA
CC = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862,
CC ChEBI:CHEBI:73863; Evidence={ECO:0000269|PubMed:22216341,
CC ECO:0000269|PubMed:23873268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC Evidence={ECO:0000305|PubMed:22216341};
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:0000269|PubMed:22216341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:22216341};
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:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
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:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
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:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
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:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
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:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:22216341,
CC ECO:0000269|PubMed:23873268}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite
CC {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein
CC localizes to the soma and proximal portion of the dendritic tree.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and brain.
CC {ECO:0000269|PubMed:12005057}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
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DR EMBL; AB071985; BAB69887.1; -; mRNA.
DR EMBL; HQ404314; ADP36858.1; -; mRNA.
DR RefSeq; NP_599209.1; NM_134382.1.
DR RefSeq; XP_006243479.1; XM_006243417.2.
DR AlphaFoldDB; Q920L7; -.
DR SMR; Q920L7; -.
DR STRING; 10116.ENSRNOP00000010409; -.
DR SwissLipids; SLP:000000274; -.
DR SwissLipids; SLP:000000452; -.
DR PhosphoSitePlus; Q920L7; -.
DR PaxDb; Q920L7; -.
DR Ensembl; ENSRNOT00000010409; ENSRNOP00000010409; ENSRNOG00000006331.
DR GeneID; 171400; -.
DR KEGG; rno:171400; -.
DR UCSC; RGD:620583; rat.
DR CTD; 60481; -.
DR RGD; 620583; Elovl5.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; Q920L7; -.
DR OMA; WVVIDIN; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q920L7; -.
DR TreeFam; TF323454; -.
DR Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q920L7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000006331; Expressed in liver and 19 other tissues.
DR Genevisible; Q920L7; RN.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0097447; C:dendritic tree; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; ISS:UniProtKB.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IDA:UniProtKB.
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:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
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; IDA:UniProtKB.
DR HAMAP; MF_03205; VLCF_elongase_5; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033677; ELOVL5.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
DR Pfam; PF01151; ELO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..299
FT /note="Elongation of very long chain fatty acids protein 5"
FT /id="PRO_0000282842"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYP7"
FT MUTAGEN 218
FT /note="S->L: No effect on fatty acid elongase activity."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 219
FT /note="C->S: No effect on fatty acid elongase activity."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 220
FT /note="G->A: No effect on fatty acid elongase activity."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 231
FT /note="W->C: Changed substrate specificity. Can elongate
FT (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA into
FT (9Z,12Z,15Z,18Z,21Z)-3-oxotetracosapentaenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 233
FT /note="Y->I: No effect on fatty acid elongase activity."
FT /evidence="ECO:0000269|PubMed:23873268"
FT CONFLICT 59
FT /note="F -> S (in Ref. 2; ADP36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="I -> T (in Ref. 2; ADP36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> G (in Ref. 2; ADP36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="F -> L (in Ref. 2; ADP36858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 35235 MW; 661CFAD9E168D7A8 CRC64;
MEHFDASLST YFRALLGPRD TRVKGWFLLD NYIPTFVCSA IYLLIVWLGP KYMKNRQPFS
CRGILVVYNL GLTLLSLYMF YELVTGVWEG KYNFFCQGTR SAGESDMKVI RVLWWYYFSK
LIEFMDTFFF ILRKNNHQIT VLHVYHHATM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
YSYYGLSSVP SMRPYLWWKK YITQGQLVQF VLTIIQTSCG VIWPCSFPLG WLYFQIGYMI
SLIALFTNFY IQTYNKKGAS RRKEHLKGHQ NGSMTAVNGH TNNFASLENS VTSRKQRKD
