ELOV5_HUMAN
ID ELOV5_HUMAN Reviewed; 299 AA.
AC Q9NYP7; B4DZJ2; F6SH78; Q59EL3; Q5TGH5; Q6NXE7; Q7L2S5; Q8NCG4; Q9UI22;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:10970790, ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Fatty acid elongase 1;
DE Short=hELO1;
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
GN Name=ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205}; Synonyms=ELOVL2;
GN ORFNames=PRO0530;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10970790; DOI=10.1042/bj3500765;
RA Leonard A.E., Bobik E.G., Dorado J., Kroeger P.E., Chuang L.-T.,
RA Thurmond J.M., Parker-Barnes J.M., Das T., Huang Y.-S., Mukerji P.;
RT "Cloning of a human cDNA encoding a novel enzyme involved in the elongation
RT of long-chain polyunsaturated fatty acids.";
RL Biochem. J. 350:765-770(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Suzuki T., Nitta A., Morita R., Sugimoto Y., Yamakawa K.;
RT "Homo sapiens mRNA for elongation of very long chain fatty acids
RT (FEN1/Elo2, SUR4/Elo3, yeast)-like 2 (ELOVL2).";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye, Leiomyosarcoma, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-299 (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-299 (ISOFORM 1).
RC TISSUE=Liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhang Y.,
RA Liu M., He F.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP CATALYTIC ACTIVITY.
RX PubMed=19575253; DOI=10.1007/s11745-009-3320-8;
RA Kitazawa H., Miyamoto Y., Shimamura K., Nagumo A., Tokita S.;
RT "Development of a high-density assay for long-chain fatty acyl-CoA
RT elongases.";
RL Lipids 44:765-773(2009).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20937905; DOI=10.1073/pnas.1005572107;
RA Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
RA Sassa T., Kihara A.;
RT "ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN SCA38, AND
RP VARIANTS SCA38 VAL-72 AND VAL-230.
RX PubMed=25065913; DOI=10.1016/j.ajhg.2014.07.001;
RA Di Gregorio E., Borroni B., Giorgio E., Lacerenza D., Ferrero M.,
RA Lo Buono N., Ragusa N., Mancini C., Gaussen M., Calcia A., Mitro N.,
RA Hoxha E., Mura I., Coviello D.A., Moon Y.A., Tesson C., Vaula G.,
RA Couarch P., Orsi L., Duregon E., Papotti M.G., Deleuze J.F., Imbert J.,
RA Costanzi C., Padovani A., Giunti P., Maillet-Vioud M., Durr A., Brice A.,
RA Tempia F., Funaro A., Boccone L., Caruso D., Stevanin G., Brusco A.;
RT "ELOVL5 mutations cause spinocerebellar ataxia 38.";
RL Am. J. Hum. Genet. 95:209-217(2014).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 in 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 (By similarity) (PubMed:10970790, PubMed:20937905). In
CC conditions where the essential linoleic and alpha linoleic fatty acids
CC are lacking it is also involved in the synthesis of Mead acid from
CC oleic acid (By similarity). {ECO:0000250|UniProtKB:Q8BHI7,
CC ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:10970790,
CC ECO:0000269|PubMed:20937905}.
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_03205,
CC ECO:0000269|PubMed:10970790, ECO:0000269|PubMed:19575253,
CC ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790,
CC ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790,
CC ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:10970790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC Evidence={ECO:0000305|PubMed:10970790};
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:0000269|PubMed:10970790,
CC ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:10970790};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA
CC = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862,
CC ChEBI:CHEBI:73863; Evidence={ECO:0000269|PubMed:10970790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC Evidence={ECO:0000305|PubMed:10970790};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:20937905}.
CC -!- INTERACTION:
CC Q9NYP7; O14523: C2CD2L; NbExp=3; IntAct=EBI-11037623, EBI-12822627;
CC Q9NYP7; O14653: GOSR2; NbExp=3; IntAct=EBI-11037623, EBI-4401517;
CC Q9NYP7; P09601: HMOX1; NbExp=3; IntAct=EBI-11037623, EBI-2806151;
CC Q9NYP7; P30519: HMOX2; NbExp=3; IntAct=EBI-11037623, EBI-712096;
CC Q9NYP7; P24593: IGFBP5; NbExp=3; IntAct=EBI-11037623, EBI-720480;
CC Q9NYP7; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11037623, EBI-10317425;
CC Q9NYP7; Q04941: PLP2; NbExp=3; IntAct=EBI-11037623, EBI-608347;
CC Q9NYP7; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-11037623, EBI-2823239;
CC Q9NYP7; O15400: STX7; NbExp=3; IntAct=EBI-11037623, EBI-3221827;
CC Q9NYP7; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-11037623, EBI-1049004;
CC Q9NYP7; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-11037623, EBI-13075176;
CC Q9NYP7; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-11037623, EBI-310962;
CC Q9NYP7; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-11037623, EBI-12887458;
CC Q9NYP7; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-11037623, EBI-12003468;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:20937905}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}. Cell
CC projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205,
CC ECO:0000269|PubMed:25065913}. Note=In Purkinje cells, the protein
CC localizes to the soma and proximal portion of the dendritic tree.
CC {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:25065913}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NYP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYP7-2; Sequence=VSP_045918;
CC Name=3;
CC IsoId=Q9NYP7-3; Sequence=VSP_045917, VSP_045919;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the adrenal gland
CC and testis. Weakly expressed in prostate, lung and brain. Expressed in
CC the cerebellum. {ECO:0000269|PubMed:10970790,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25065913}.
CC -!- DISEASE: Spinocerebellar ataxia 38 (SCA38) [MIM:615957]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA38 is an autosomal dominant form
CC characterized by adult-onset of slowly progressive gait ataxia
CC accompanied by nystagmus. Brain MRI shows cerebellar atrophy.
CC {ECO:0000269|PubMed:25065913}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16688.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11178.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF231981; AAF70631.1; -; mRNA.
DR EMBL; AF338241; AAM00193.1; -; mRNA.
DR EMBL; AL136939; CAB66873.1; -; mRNA.
DR EMBL; AK074889; BAC11270.1; -; mRNA.
DR EMBL; AK302948; BAG64104.1; -; mRNA.
DR EMBL; AB209798; BAD93035.1; -; mRNA.
DR EMBL; AL034374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04419.1; -; Genomic_DNA.
DR EMBL; BC017270; AAH17270.2; -; mRNA.
DR EMBL; BC067123; AAH67123.2; -; mRNA.
DR EMBL; BC074503; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074748; BAC11178.1; ALT_INIT; mRNA.
DR EMBL; AF111849; AAF16688.1; ALT_INIT; mRNA.
DR CCDS; CCDS4951.1; -. [Q9NYP7-1]
DR CCDS; CCDS56433.1; -. [Q9NYP7-2]
DR CCDS; CCDS56434.1; -. [Q9NYP7-3]
DR RefSeq; NP_001229757.1; NM_001242828.1. [Q9NYP7-2]
DR RefSeq; NP_001229759.1; NM_001242830.1.
DR RefSeq; NP_001229760.1; NM_001242831.1. [Q9NYP7-3]
DR RefSeq; NP_001288785.1; NM_001301856.1. [Q9NYP7-1]
DR RefSeq; NP_068586.1; NM_021814.4. [Q9NYP7-1]
DR AlphaFoldDB; Q9NYP7; -.
DR SMR; Q9NYP7; -.
DR BioGRID; 121914; 361.
DR IntAct; Q9NYP7; 27.
DR MINT; Q9NYP7; -.
DR STRING; 9606.ENSP00000359956; -.
DR BindingDB; Q9NYP7; -.
DR ChEMBL; CHEMBL5937; -.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB11358; Evening primrose oil.
DR SwissLipids; SLP:000000253; -.
DR GlyGen; Q9NYP7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYP7; -.
DR PhosphoSitePlus; Q9NYP7; -.
DR SwissPalm; Q9NYP7; -.
DR BioMuta; ELOVL5; -.
DR DMDM; 74753072; -.
DR EPD; Q9NYP7; -.
DR jPOST; Q9NYP7; -.
DR MassIVE; Q9NYP7; -.
DR MaxQB; Q9NYP7; -.
DR PeptideAtlas; Q9NYP7; -.
DR PRIDE; Q9NYP7; -.
DR ProteomicsDB; 27928; -.
DR ProteomicsDB; 65118; -.
DR ProteomicsDB; 83259; -. [Q9NYP7-1]
DR Antibodypedia; 4471; 361 antibodies from 28 providers.
DR DNASU; 60481; -.
DR Ensembl; ENST00000304434.11; ENSP00000306640.6; ENSG00000012660.14. [Q9NYP7-1]
DR Ensembl; ENST00000370913.5; ENSP00000359951.5; ENSG00000012660.14. [Q9NYP7-3]
DR Ensembl; ENST00000370918.8; ENSP00000359956.5; ENSG00000012660.14. [Q9NYP7-2]
DR GeneID; 60481; -.
DR KEGG; hsa:60481; -.
DR MANE-Select; ENST00000304434.11; ENSP00000306640.6; NM_021814.5; NP_068586.1.
DR UCSC; uc003pbr.3; human. [Q9NYP7-1]
DR CTD; 60481; -.
DR DisGeNET; 60481; -.
DR GeneCards; ELOVL5; -.
DR GeneReviews; ELOVL5; -.
DR HGNC; HGNC:21308; ELOVL5.
DR HPA; ENSG00000012660; Low tissue specificity.
DR MalaCards; ELOVL5; -.
DR MIM; 611805; gene.
DR MIM; 615957; phenotype.
DR neXtProt; NX_Q9NYP7; -.
DR OpenTargets; ENSG00000012660; -.
DR Orphanet; 423296; Spinocerebellar ataxia type 38.
DR PharmGKB; PA128394703; -.
DR VEuPathDB; HostDB:ENSG00000012660; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; Q9NYP7; -.
DR OMA; WVVIDIN; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9NYP7; -.
DR TreeFam; TF323454; -.
DR BioCyc; MetaCyc:ENSG00000012660-MON; -.
DR PathwayCommons; Q9NYP7; -.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q9NYP7; -.
DR SIGNOR; Q9NYP7; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 60481; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; ELOVL5; human.
DR GeneWiki; ELOVL5; -.
DR GenomeRNAi; 60481; -.
DR Pharos; Q9NYP7; Tbio.
DR PRO; PR:Q9NYP7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NYP7; protein.
DR Bgee; ENSG00000012660; Expressed in seminal vesicle and 207 other tissues.
DR ExpressionAtlas; Q9NYP7; baseline and differential.
DR Genevisible; Q9NYP7; HS.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0097447; C:dendritic tree; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IDA:UniProtKB.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IDA:UniProtKB.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
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; IDA:UniProtKB.
DR HAMAP; MF_03205; VLCF_elongase_5; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033677; ELOVL5.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
DR Pfam; PF01151; ELO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Disease variant;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Spinocerebellar ataxia; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Elongation of very long chain fatty acids protein 5"
FT /id="PRO_0000282838"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 20..88
FT /note="DTRVKGWFLLDNYIPTFICSVIYLLIVWLGPKYMRNKQPFSCRGILVVYNLG
FT LTLLSLYMFCELVTGVW -> GISSSVLRMGPPLHTVVGWLQQLQAAHSEEEEKMFHLC
FT GFKHKEVVSQSSLPAVIPQNSLATIASHAPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045917"
FT VAR_SEQ 82
FT /note="E -> ESKREQPRRSACASRTDPSTQQQLPENR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045918"
FT VAR_SEQ 89..299
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045919"
FT VARIANT 72
FT /note="L -> V (in SCA38; dbSNP:rs587777671)"
FT /evidence="ECO:0000269|PubMed:25065913"
FT /id="VAR_072361"
FT VARIANT 230
FT /note="G -> V (in SCA38; dbSNP:rs587777670)"
FT /evidence="ECO:0000269|PubMed:25065913"
FT /id="VAR_072362"
FT CONFLICT 59
FT /note="F -> L (in Ref. 4; BAG64104)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..262
FT /note="YFGATLNSFIHVLMYSYYGLSSVPSMRPYLWWKKYITQGQLLQFVLTIIQTS
FT CGVIWPCTFPLGWLYFQIGYMISLIALFTNFYIQTYNKKGASRR -> SVCADNHPDQL
FT RGHLAVHIPSWLVVFPDWIHDFPDCSLHKLLHSDLQQERGLPKERPPEGPPEWVHGCCE
FT WTHQQLFTPGKQCEAKEAAEGLKSKN (in Ref. 4; BAD93035)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..206
FT /note="QGQ -> EFH (in Ref. 9; BAC11178)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="F -> S (in Ref. 9; BAC11178)"
FT /evidence="ECO:0000305"
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
