GenomeNet

Database: UniProt
Entry: H2QQ14_PANTR
LinkDB: H2QQ14_PANTR
Original site: H2QQ14_PANTR 
ID   H2QQ14_PANTR            Unreviewed;       265 AA.
AC   H2QQ14; A0A2J8M2B4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE            EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03206};
DE   AltName: Full=3-keto acyl-CoA synthase ELOVL6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE   AltName: Full=ELOVL fatty acid elongase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE            Short=ELOVL FA elongase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE   AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE   AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
GN   Name=ELOVL6 {ECO:0000256|HAMAP-Rule:MF_03206,
GN   ECO:0000313|EMBL:JAA10846.1, ECO:0000313|Ensembl:ENSPTRP00000028113.2,
GN   ECO:0000313|VGNC:VGNC:596};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000028113.2, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000028113.2, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA10846.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA10846.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA41273.1}, Skin {ECO:0000313|EMBL:JAA24456.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA16059.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000028113.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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 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 to 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:0000256|HAMAP-Rule:MF_03206}.
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=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:0000256|ARBA:ARBA00001211};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC         Evidence={ECO:0000256|ARBA:ARBA00001211};
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:0000256|ARBA:ARBA00001634};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC         Evidence={ECO:0000256|ARBA:ARBA00001634};
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_03206,
CC         ECO:0000256|RuleBase:RU361115};
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:0000256|ARBA:ARBA00001237};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141;
CC         Evidence={ECO:0000256|ARBA:ARBA00001237};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_03206}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|HAMAP-Rule:MF_03206};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|HAMAP-Rule:MF_03206}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- PTM: N-Glycosylated. {ECO:0000256|HAMAP-Rule:MF_03206}.
CC   -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03206}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03206}.
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DR   EMBL; AACZ04021151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04021152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01000492; JAA10846.1; -; mRNA.
DR   EMBL; GABC01000491; JAA10847.1; -; mRNA.
DR   EMBL; GABF01006086; JAA16059.1; -; mRNA.
DR   EMBL; GABF01006085; JAA16060.1; -; mRNA.
DR   EMBL; GABD01008644; JAA24456.1; -; mRNA.
DR   EMBL; GABE01003466; JAA41273.1; -; mRNA.
DR   EMBL; GABE01003465; JAA41274.1; -; mRNA.
DR   RefSeq; XP_003950444.2; XM_003950395.3.
DR   RefSeq; XP_009446414.1; XM_009448139.2.
DR   RefSeq; XP_009446415.1; XM_009448140.2.
DR   SMR; H2QQ14; -.
DR   STRING; 9598.ENSPTRP00000028113; -.
DR   PaxDb; 9598-ENSPTRP00000028113; -.
DR   Ensembl; ENSPTRT00000030447.3; ENSPTRP00000028113.2; ENSPTRG00000016368.3.
DR   GeneID; 461436; -.
DR   KEGG; ptr:461436; -.
DR   CTD; 79071; -.
DR   VGNC; VGNC:596; ELOVL6.
DR   eggNOG; KOG3072; Eukaryota.
DR   GeneTree; ENSGT01050000244965; -.
DR   HOGENOM; CLU_048483_1_1_1; -.
DR   OMA; EWVPISL; -.
DR   OrthoDB; 2312411at2759; -.
DR   TreeFam; TF106467; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002277; Chromosome 4.
DR   Bgee; ENSPTRG00000016368; Expressed in fibroblast and 19 other cell types or tissues.
DR   GO; GO:0009923; C:fatty acid elongase complex; 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:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; 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_03206; VLCF_elongase_6; 1.
DR   InterPro; IPR030457; ELO_CS.
DR   InterPro; IPR002076; ELO_fam.
DR   InterPro; IPR033675; ELOVL6.
DR   PANTHER; PTHR11157:SF125; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 6; 1.
DR   PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01151; ELO; 1.
DR   PROSITE; PS01188; ELO; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03206,
KW   ECO:0000256|RuleBase:RU361115};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03206,
KW   ECO:0000256|RuleBase:RU361115};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03206};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_03206};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_03206}.
FT   TRANSMEM        34..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        63..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        139..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        195..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        237..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   265 AA;  31376 MW;  01234E0EEF6CE341 CRC64;
     MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
     KPLVLWSLTL AVFSIFGALR TGAYMVYILM TKGLKQSVCD QGFYNGPVSK FWAYAFVLSK
     APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
     YALRAAGFRV SRKFAMFITL SQITQMLMGC VVNYLVFCWM QHDQCHSHFQ NIFWSSLMYL
     SYLVLFCHFF FEAYIGKMRK TTKAE
//
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