ID G3R6X9_GORGO Unreviewed; 299 AA.
AC G3R6X9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
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};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000011103.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000011103.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000011103.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000011103.3}
RP IDENTIFICATION.
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}.
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DR EMBL; CABD030045109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030045110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004044261.1; XM_004044213.2.
DR RefSeq; XP_018885064.1; XM_019029519.1.
DR AlphaFoldDB; G3R6X9; -.
DR SMR; G3R6X9; -.
DR Ensembl; ENSGGOT00000011430.3; ENSGGOP00000011103.3; ENSGGOG00000011386.3.
DR GeneID; 101124844; -.
DR KEGG; ggo:101124844; -.
DR CTD; 60481; -.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000011386; Expressed in testis and 6 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: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: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:UP000001519};
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..80
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 167..186
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 274..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 35293 MW; AE5150AA3432E984 CRC64;
MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP KYMRNKQPFS
CRGILVVYNL GLTLLSLYMF CELVTGVWEG KYNFFCQGTR TAGESDMKII RVLWWYYFSK
LIEFMDTFFF ILRKNNHQIT VLHVYHHASM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
YSYYGLSSVP SMRPYLWWKK YITQGQLLQF VLTIIQTSCG VIWPCTFPLG WLYFQIGYMI
SLIALFTNFY IQTYNKKGAS RRKDHLKDHQ NGSMAAVNGH TNSFSPLENN VKPRKLRKD
//
