ELOV1_HUMAN
ID ELOV1_HUMAN Reviewed; 279 AA.
AC Q9BW60; B4DP24; Q53HT2; Q5JUY3; Q8WXU3; Q9NVD9; Q9Y396;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Elongation of very long chain fatty acids protein 1 {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20166112, ECO:0000269|PubMed:20937905};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL1 {ECO:0000255|HAMAP-Rule:MF_03201};
DE AltName: Full=ELOVL fatty acid elongase 1 {ECO:0000255|HAMAP-Rule:MF_03201};
DE Short=ELOVL FA elongase 1 {ECO:0000255|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 1 {ECO:0000255|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 1 {ECO:0000255|HAMAP-Rule:MF_03201};
GN Name=ELOVL1 {ECO:0000312|HGNC:HGNC:14418}; Synonyms=SSC1; ORFNames=CGI-88;
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).
RA Asadi A., Jacobsson A.;
RT "Description of the human SSC1/ELOVL1 gene. Relocation of the CDC20 gene to
RT human chromosome 1 support a bi-directional transcription of the human
RT SSC1/ELOVL1 and CDC20 genes.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [6]
RP REVIEW.
RX PubMed=16564093; DOI=10.1016/j.plipres.2006.01.004;
RA Jakobsson A., Westerberg R., Jacobsson A.;
RT "Fatty acid elongases in mammals: their regulation and roles in
RT metabolism.";
RL Prog. Lipid Res. 45:237-249(2006).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20166112; DOI=10.1002/emmm.201000061;
RA Ofman R., Dijkstra I.M.E., van Roermund C.W.T., Burger N., Turkenburg M.,
RA van Cruchten A., van Engen C.E., Wanders R.J.A., Kemp S.;
RT "The role of ELOVL1 in very long-chain fatty acid homeostasis and X-linked
RT adrenoleukodystrophy.";
RL EMBO Mol. Med. 2:90-97(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH LASS2; HSD17B12 AND TECR.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
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).
RN [12]
RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, INVOLVEMENT IN IKSHD, VARIANT IKSHD
RP PHE-165, AND CHARACTERIZATION OF VARIANT IKSHD PHE-165.
RX PubMed=29496980; DOI=10.1136/jmedgenet-2017-105172;
RA Kutkowska-Kazmierczak A., Rydzanicz M., Chlebowski A.,
RA Klosowska-Kosicka K., Mika A., Gruchota J., Jurkiewicz E., Kowalewski C.,
RA Pollak A., Stradomska T.J., Kmiec T., Jakubowski R., Gasperowicz P.,
RA Walczak A., Sladowski D., Jankowska-Steifer E., Korniszewski L.,
RA Kosinska J., Obersztyn E., Nowak W., Sledzinski T., Dziembowski A.,
RA Ploski R.;
RT "Dominant ELOVL1 mutation causes neurological disorder with ichthyotic
RT keratoderma, spasticity, hypomyelination and dysmorphic features.";
RL J. Med. Genet. 55:408-414(2018).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP PATHWAY, INVOLVEMENT IN IKSHD, VARIANT IKSHD PHE-165, AND CHARACTERIZATION
RP OF VARIANT IKSHD PHE-165.
RX PubMed=30487246; DOI=10.1136/jmedgenet-2018-105711;
RA Mueller N., Sassa T., Morales-Gonzalez S., Schneider J., Salchow D.J.,
RA Seelow D., Knierim E., Stenzel W., Kihara A., Schuelke M.;
RT "De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans,
RT hypomyelination, spastic paraplegia, high frequency deafness and optic
RT atrophy.";
RL J. Med. Genet. 56:164-175(2019).
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle
CC (PubMed:29496980, PubMed:30487246). This endoplasmic reticulum-bound
CC enzymatic process allows the addition of 2 carbons to the chain of
CC long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing
CC enzyme that exhibits activity toward saturated and monounsaturated
CC acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA.
CC May participate in the production of both saturated and monounsaturated
CC VLCFAs of different chain lengths that are involved in multiple
CC biological processes as precursors of membrane lipids and lipid
CC mediators. Important for saturated C24:0 and monounsaturated C24:1
CC sphingolipid synthesis (PubMed:20937905). Indirectly inhibits RPE65 via
CC production of VLCFAs. {ECO:0000255|HAMAP-Rule:MF_03201,
CC ECO:0000269|PubMed:20166112, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:29496980, ECO:0000269|PubMed:30487246}.
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_03201,
CC ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20166112,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:29496980,
CC ECO:0000269|PubMed:30487246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71451;
CC Evidence={ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-eicosenoyl-CoA + H(+) + malonyl-CoA = (13Z)-3-
CC oxodocosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36527,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:74069, ChEBI:CHEBI:74070;
CC Evidence={ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36528;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetracosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:36507, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:73977;
CC Evidence={ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36508;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13Z)-docosenoyl-CoA + H(+) + malonyl-CoA = (15Z)-3-
CC oxotetracosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36531,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:74068, ChEBI:CHEBI:74071;
CC Evidence={ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36532;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetracosanoyl-CoA = 3-oxohexacosanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:36515, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:73980;
CC Evidence={ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36516;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexacosanoyl-CoA + malonyl-CoA = 3-oxooctacosanyol-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:36519, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:64868, ChEBI:CHEBI:73976;
CC Evidence={ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36520;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65115;
CC Evidence={ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC Evidence={ECO:0000269|PubMed:20937905};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03201, ECO:0000269|PubMed:20166112,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:29496980}.
CC -!- SUBUNIT: Interacts with LASS2, TECR and HSD17B12. {ECO:0000255|HAMAP-
CC Rule:MF_03201, ECO:0000269|PubMed:20937905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:30487246}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BW60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BW60-2; Sequence=VSP_045436;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:30487246}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- DISEASE: Ichthyotic keratoderma, spasticity, hypomyelination, and
CC dysmorphic facies (IKSHD) [MIM:618527]: An autosomal dominant disease
CC characterized by ichthyosis due to epidermal hyperproliferation and
CC increased keratinisation, hypomyelination of the central white matter,
CC spastic paraplegia, central nystagmus, optic atrophy, reduction of
CC peripheral vision and visual acuity, and dysmorphic facial features.
CC {ECO:0000269|PubMed:29496980, ECO:0000269|PubMed:30487246}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34083.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF336793; AAL71993.1; -; mRNA.
DR EMBL; AF151846; AAD34083.1; ALT_FRAME; mRNA.
DR EMBL; AK001653; BAA91813.1; -; mRNA.
DR EMBL; AK222498; BAD96218.1; -; mRNA.
DR EMBL; AK298163; BAG60436.1; -; mRNA.
DR EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000618; AAH00618.1; -; mRNA.
DR CCDS; CCDS485.1; -. [Q9BW60-1]
DR CCDS; CCDS57987.1; -. [Q9BW60-2]
DR RefSeq; NP_001243328.1; NM_001256399.1. [Q9BW60-1]
DR RefSeq; NP_001243330.1; NM_001256401.1. [Q9BW60-2]
DR RefSeq; NP_001243331.1; NM_001256402.1.
DR RefSeq; NP_073732.1; NM_022821.3. [Q9BW60-1]
DR AlphaFoldDB; Q9BW60; -.
DR SMR; Q9BW60; -.
DR BioGRID; 122312; 39.
DR IntAct; Q9BW60; 9.
DR MINT; Q9BW60; -.
DR STRING; 9606.ENSP00000477602; -.
DR BindingDB; Q9BW60; -.
DR ChEMBL; CHEMBL6001; -.
DR SwissLipids; SLP:000000249; -.
DR GlyGen; Q9BW60; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BW60; -.
DR MetOSite; Q9BW60; -.
DR PhosphoSitePlus; Q9BW60; -.
DR SwissPalm; Q9BW60; -.
DR BioMuta; ELOVL1; -.
DR DMDM; 20137931; -.
DR EPD; Q9BW60; -.
DR jPOST; Q9BW60; -.
DR MassIVE; Q9BW60; -.
DR MaxQB; Q9BW60; -.
DR PaxDb; Q9BW60; -.
DR PeptideAtlas; Q9BW60; -.
DR PRIDE; Q9BW60; -.
DR ProteomicsDB; 4745; -.
DR ProteomicsDB; 79254; -. [Q9BW60-1]
DR TopDownProteomics; Q9BW60-1; -. [Q9BW60-1]
DR Antibodypedia; 32316; 224 antibodies from 26 providers.
DR DNASU; 64834; -.
DR Ensembl; ENST00000372458.8; ENSP00000361536.3; ENSG00000066322.15. [Q9BW60-1]
DR Ensembl; ENST00000413844.3; ENSP00000416024.2; ENSG00000066322.15. [Q9BW60-2]
DR Ensembl; ENST00000621943.4; ENSP00000477602.1; ENSG00000066322.15. [Q9BW60-1]
DR GeneID; 64834; -.
DR KEGG; hsa:64834; -.
DR MANE-Select; ENST00000372458.8; ENSP00000361536.3; NM_022821.4; NP_073732.1.
DR UCSC; uc001cjb.5; human. [Q9BW60-1]
DR CTD; 64834; -.
DR DisGeNET; 64834; -.
DR GeneCards; ELOVL1; -.
DR HGNC; HGNC:14418; ELOVL1.
DR HPA; ENSG00000066322; Low tissue specificity.
DR MalaCards; ELOVL1; -.
DR MIM; 611813; gene.
DR MIM; 618527; phenotype.
DR neXtProt; NX_Q9BW60; -.
DR OpenTargets; ENSG00000066322; -.
DR PharmGKB; PA27760; -.
DR VEuPathDB; HostDB:ENSG00000066322; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_0_1; -.
DR InParanoid; Q9BW60; -.
DR OMA; KVAPGGM; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9BW60; -.
DR TreeFam; TF323454; -.
DR PathwayCommons; Q9BW60; -.
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; Q9BW60; -.
DR SIGNOR; Q9BW60; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 64834; 98 hits in 1077 CRISPR screens.
DR ChiTaRS; ELOVL1; human.
DR GenomeRNAi; 64834; -.
DR Pharos; Q9BW60; Tbio.
DR PRO; PR:Q9BW60; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BW60; protein.
DR Bgee; ENSG00000066322; Expressed in C1 segment of cervical spinal cord and 95 other tissues.
DR Genevisible; Q9BW60; HS.
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:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0102337; F:3-oxo-cerotoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:RHEA.
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:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IDA:UniProtKB.
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; IDA:UniProtKB.
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:0030148; P:sphingolipid biosynthetic process; IMP:UniProtKB.
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_03201; VLCF_elongase_1; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033681; ELOVL1.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Ichthyosis;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..279
FT /note="Elongation of very long chain fatty acids protein 1"
FT /id="PRO_0000207536"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT MOTIF 275..279
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03201"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT VAR_SEQ 80..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045436"
FT VARIANT 165
FT /note="S -> F (in IKSHD; loss of fatty acid elongase
FT activity)"
FT /evidence="ECO:0000269|PubMed:29496980,
FT ECO:0000269|PubMed:30487246"
FT /id="VAR_083193"
FT CONFLICT 68
FT /note="S -> P (in Ref. 3; BAA91813)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="Y -> H (in Ref. 1; AAL71993)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="M -> T (in Ref. 3; BAD96218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 32663 MW; B168EE4C7EAF92A6 CRC64;
MEAVVNLYQE VMKHADPRIQ GYPLMGSPLL MTSILLTYVY FVLSLGPRIM ANRKPFQLRG
FMIVYNFSLV ALSLYIVYEF LMSGWLSTYT WRCDPVDYSN SPEALRMVRV AWLFLFSKFI
ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW SWWWGVKIAP GGMGSFHAMI NSSVHVIMYL
YYGLSAFGPV AQPYLWWKKH MTAIQLIQFV LVSLHISQYY FMSSCNYQYP VIIHLIWMYG
TIFFMLFSNF WYHSYTKGKR LPRALQQNGA PGIAKVKAN
