ID F6R8E9_ORNAN Unreviewed; 294 AA.
AC F6R8E9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 82.
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:ENSOANP00000018699.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000018699.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000018699.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018699.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000018699.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018699.3};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03205}.
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DR RefSeq; XP_007658623.1; XM_007660433.2.
DR AlphaFoldDB; F6R8E9; -.
DR STRING; 9258.ENSOANP00000018699; -.
DR Ensembl; ENSOANT00000018702.4; ENSOANP00000018699.3; ENSOANG00000011799.4.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; F6R8E9; -.
DR OMA; PISWVPI; -.
DR OrthoDB; 168669at2759; -.
DR TreeFam; TF323454; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000002279; Chromosome 1.
DR Bgee; ENSOANG00000011799; Expressed in adult mammalian kidney and 7 other cell types or tissues.
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; 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:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
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_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:UP000002279};
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 32..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 144..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 207..224
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03205,
FT ECO:0000256|RuleBase:RU361115"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 34807 MW; 7AD2506E9AAC4018 CRC64;
MEFLDATINS YSEILLGPRD PRVKGWLLLD NYMPTFIFSV LYLLIVWMGP KYMQNKQPYS
CRGILVVYNL GLTLLSFYMF YELVTGVWEG GYNFYCQDTH SGGDADMKII RVLWWYYFSK
LIEFMDTFFF ILRKNNHQIT VLHVYHHASM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
YSYYGLSAIP AMRPYLWWKK YITQGQLVQF VLTIVQTSCG VVWPCSFPMG WLYFQICYMI
SLITLFTNFY IQTYNKASAR RKDYQNGSAL VVNGHTNSFS SHENNVKPRK QRKD
//
