GenomeNet

Database: UniProt
Entry: F7DY13_MONDO
LinkDB: F7DY13_MONDO
Original site: F7DY13_MONDO 
ID   F7DY13_MONDO            Unreviewed;       265 AA.
AC   F7DY13;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 69.
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|Ensembl:ENSMODP00000016038.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000016038.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000016038.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000016038.3}
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|HAMAP-Rule:MF_03206}; Multi-pass membrane protein
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   RefSeq; XP_007481089.1; XM_007481027.2.
DR   AlphaFoldDB; F7DY13; -.
DR   STRING; 13616.ENSMODP00000016038; -.
DR   Ensembl; ENSMODT00000016335.3; ENSMODP00000016038.3; ENSMODG00000012821.3.
DR   GeneID; 100020799; -.
DR   KEGG; mdo:100020799; -.
DR   eggNOG; KOG3072; Eukaryota.
DR   GeneTree; ENSGT01050000244965; -.
DR   HOGENOM; CLU_048483_1_1_1; -.
DR   InParanoid; F7DY13; -.
DR   OMA; EWVPISL; -.
DR   OrthoDB; 2312411at2759; -.
DR   TreeFam; TF106467; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002280; Chromosome 2.
DR   Bgee; ENSMODG00000012821; Expressed in skeleton of lower jaw and 17 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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   3: Inferred from homology;
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:UP000002280};
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..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        232..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT                   ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   265 AA;  31445 MW;  55FB4C354EA66767 CRC64;
     MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
     KPLVLWSLSL AVFSIFGALR TGAYMVYILM TKGLKQSVCD QSFYIGPVSK FWAYAFVLSK
     APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
     YALRAAGFRV SRKFAMFITL SQITQMLMGL VVNYLVFYWM QQDQCHSHVQ NIIWSSLMYV
     SYFVLFCHFF FEAYIGKMRK TRKAE
//
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