ELOV6_CHICK
ID ELOV6_CHICK Reviewed; 265 AA.
AC Q5ZJR8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000250|UniProtKB:Q9H5J4, ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=ELOVL fatty acid elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE Short=ELOVL FA elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
GN Name=ELOVL6 {ECO:0000255|HAMAP-Rule:MF_03206}; ORFNames=RCJMB04_16d24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 elongates fatty acids with
CC 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs.
CC Catalyzes the synthesis of unsaturated C16 long chain fatty acids and,
CC to a lesser extent, C18:0 and those with low desaturation degree. May
CC participate in the production of saturated and monounsaturated VLCFAs
CC of different chain lengths that are involved in multiple biological
CC processes as precursors of membrane lipids and lipid mediators.
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
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_03206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:Q920L5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetradecanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:60140, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:62543;
CC Evidence={ECO:0000250|UniProtKB:Q920L5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141;
CC Evidence={ECO:0000250|UniProtKB:Q920L5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- ACTIVITY REGULATION: The reaction is stimulated by the presence of
CC HSD17B12, the enzyme catalyzing the second step of the elongation
CC cycle. {ECO:0000250|UniProtKB:Q9H5J4}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03206}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03206}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
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DR EMBL; AJ720366; CAG32025.1; -; mRNA.
DR RefSeq; NP_001026710.1; NM_001031539.1.
DR AlphaFoldDB; Q5ZJR8; -.
DR SMR; Q5ZJR8; -.
DR PaxDb; Q5ZJR8; -.
DR GeneID; 428772; -.
DR KEGG; gga:428772; -.
DR CTD; 79071; -.
DR VEuPathDB; HostDB:geneid_428772; -.
DR HOGENOM; CLU_048483_1_3_1; -.
DR InParanoid; Q5ZJR8; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q5ZJR8; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q5ZJR8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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; 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; ISS:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
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_03206; VLCF_elongase_6; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033675; ELOVL6.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF125; PTHR11157:SF125; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..265
FT /note="Elongation of very long chain fatty acids protein 6"
FT /id="PRO_0000282849"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
SQ SEQUENCE 265 AA; 31268 MW; 15991AFE36ECE305 CRC64;
MNMSVLTLQE YEFEKQFNEH EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
KPLVLWSLSL AVFSIFGAVR TAPYMLYILM TKGLKQSVCD QSFYIGPVSK FWAYAFVLSK
APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
YALRAAGFRV SRKFAMFITL SQITQMLVGC VINYLVFSWM QHGQCHSHVQ NIIWSSLMYL
SYFVLFCHFF FEAYIGKTTK ARKVD
