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Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (rELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)

 ELOV5_RAT               Reviewed;         299 AA.
Q920L7; G9BD46;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 100.
RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:22216341};
AltName: Full=3-keto acyl-CoA synthase Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=Fatty acid elongase 1;
Short=rELO1;
AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
Name=Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=12005057; DOI=10.1271/bbb.66.613;
Inagaki K., Aki T., Fukuda Y., Kawamoto S., Shigeta S., Ono K.,
Suzuki O.;
"Identification and expression of a rat fatty acid elongase involved
in the biosynthesis of C18 fatty acids.";
Biosci. Biotechnol. Biochem. 66:613-621(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=22216341; DOI=10.1371/journal.pone.0029662;
Gregory M.K., Gibson R.A., Cook-Johnson R.J., Cleland L.G.,
James M.J.;
"Elongase reactions as control points in long-chain polyunsaturated
fatty acid synthesis.";
PLoS ONE 6:E29662-E29662(2011).
-!- FUNCTION: Catalyzes the first and rate-limiting reaction of the
four that constitute the long-chain fatty acids elongation cycle.
This endoplasmic reticulum-bound enzymatic process, allows the
addition of 2 carbons to the chain of long- and very long-chain
fatty acids/VLCFAs per cycle. Condensing enzyme that acts
specifically toward polyunsaturated acyl-CoA with the higher
activity toward C18:3(n-6) acyl-CoA. May participate in the
production of monounsaturated and of polyunsaturated VLCFAs of
different chain lengths that are involved in multiple biological
processes as precursors of membrane lipids and lipid mediators.
{ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:22216341}.
-!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + malonyl-CoA = CoA
+ a very-long-chain 3-oxoacyl-CoA + CO(2). {ECO:0000255|HAMAP-
Rule:MF_03205, ECO:0000269|PubMed:22216341}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03205,
ECO:0000269|PubMed:22216341}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite
{ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the
protein localizes to the soma and proximal portion of the
dendritic tree. {ECO:0000255|HAMAP-Rule:MF_03205}.
-!- TISSUE SPECIFICITY: Highly expressed in lung and brain.
{ECO:0000269|PubMed:12005057}.
-!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03205}.
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EMBL; AB071985; BAB69887.1; -; mRNA.
EMBL; HQ404314; ADP36858.1; -; mRNA.
RefSeq; NP_599209.1; NM_134382.1.
RefSeq; XP_006243479.1; XM_006243417.2.
UniGene; Rn.212229; -.
UniGene; Rn.233746; -.
STRING; 10116.ENSRNOP00000010409; -.
SwissLipids; SLP:000000274; -.
SwissLipids; SLP:000000452; -.
PaxDb; Q920L7; -.
PRIDE; Q920L7; -.
Ensembl; ENSRNOT00000010409; ENSRNOP00000010409; ENSRNOG00000006331.
GeneID; 171400; -.
KEGG; rno:171400; -.
UCSC; RGD:620583; rat.
CTD; 60481; -.
RGD; 620583; Elovl5.
eggNOG; KOG3071; Eukaryota.
eggNOG; ENOG410XRWT; LUCA.
GeneTree; ENSGT00760000119122; -.
HOGENOM; HOG000038120; -.
HOVERGEN; HBG051468; -.
InParanoid; Q920L7; -.
KO; K10244; -.
OMA; NVKPRKQ; -.
OrthoDB; EOG091G0N2V; -.
PhylomeDB; Q920L7; -.
TreeFam; TF323454; -.
Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
UniPathway; UPA00658; -.
PRO; PR:Q920L7; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000006331; -.
Genevisible; Q920L7; RN.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0097447; C:dendritic tree; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102337; F:3-oxo-cerotoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; ISS:UniProtKB.
GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IDA:UniProtKB.
GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB.
HAMAP; MF_03205; VLCF_elongase_5; 1.
InterPro; IPR002076; ELO_fam.
InterPro; IPR033677; ELOVL5.
PANTHER; PTHR11157; PTHR11157; 1.
PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
Pfam; PF01151; ELO; 1.
1: Evidence at protein level;
Acetylation; Cell projection; Complete proteome;
Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 299 Elongation of very long chain fatty acids
protein 5.
/FTId=PRO_0000282842.
TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 64 84 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 112 132 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 139 158 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 168 187 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 205 225 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 227 247 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9NYP7}.
CONFLICT 59 59 F -> S (in Ref. 2; ADP36858).
{ECO:0000305}.
CONFLICT 64 64 I -> T (in Ref. 2; ADP36858).
{ECO:0000305}.
CONFLICT 104 104 E -> G (in Ref. 2; ADP36858).
{ECO:0000305}.
CONFLICT 130 130 F -> L (in Ref. 2; ADP36858).
{ECO:0000305}.
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


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