ELOV1_MOUSE
ID ELOV1_MOUSE Reviewed; 279 AA.
AC Q9JLJ5; Q9D1B2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
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:20937905, ECO:0000269|PubMed:23689133};
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:0000255|HAMAP-Rule:MF_03201}; Synonyms=Ssc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10791983; DOI=10.1083/jcb.149.3.707;
RA Tvrdik P., Westerberg R., Silve S., Asadi A., Jakobsson A., Cannon B.,
RA Loison G., Jacobsson A.;
RT "Role of a new mammalian gene family in the biosynthesis of very long chain
RT fatty acids and sphingolipids.";
RL J. Cell Biol. 149:707-718(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-279.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [6]
RP FUNCTION.
RX PubMed=23407971; DOI=10.1523/jneurosci.2428-12.2013;
RA Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G., Miner J.H.,
RA Jin M.;
RT "Fatty acid transport protein 4 (FATP4) prevents light-induced degeneration
RT of cone and rod photoreceptors by inhibiting RPE65 isomerase.";
RL J. Neurosci. 33:3178-3189(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND CAUTION.
RX PubMed=23689133; DOI=10.1128/mcb.00192-13;
RA Sassa T., Ohno Y., Suzuki S., Nomura T., Nishioka C., Kashiwagi T.,
RA Hirayama T., Akiyama M., Taguchi R., Shimizu H., Itohara S., Kihara A.;
RT "Impaired epidermal permeability barrier in mice lacking elovl1, the gene
RT responsible for very-long-chain fatty acid production.";
RL Mol. Cell. Biol. 33:2787-2796(2013).
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 exhibits activity toward
CC saturated and monounsaturated acyl-CoA substrates, with the highest
CC activity towards C22:0 acyl-CoA. May participate in the production of
CC both saturated and monounsaturated VLCFAs of different chain lengths
CC that are involved in multiple biological processes as precursors of
CC membrane lipids and lipid mediators. Important for saturated C24:0 and
CC monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65
CC via production of VLCFAs. {ECO:0000255|HAMAP-Rule:MF_03201,
CC ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:23407971, ECO:0000269|PubMed:23689133}.
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:20937905, ECO:0000269|PubMed:23689133};
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:20937905, ECO:0000269|PubMed:23689133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000269|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:20937905, ECO:0000269|PubMed:23689133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36508;
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:23689133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36516;
CC Evidence={ECO:0000305|PubMed:23689133};
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:0000250|UniProtKB:Q9BW60};
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:0000250|UniProtKB:Q9BW60};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03201, ECO:0000269|PubMed:20937905}.
CC -!- SUBUNIT: Interacts with LASS2, TECR and HSD17B12. {ECO:0000255|HAMAP-
CC Rule:MF_03201}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03201}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- TISSUE SPECIFICITY: Expressed in a broad variety of tissues. Highly
CC expressed in stomach, lung, kidney, skin and intestine. Moderately
CC expressed in white adipose tissue, liver, spleen, brain, brown adipose
CC tissue, heart and muscle. Weakly expressed in testis.
CC {ECO:0000269|PubMed:10791983}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice die within one day after
CC birth (PubMed:23689133). Death is caused by a skin barrier deficiency
CC and excessive water loss that are associated with impaired formation of
CC lipid lamellae in the stratum corneum (PubMed:23689133). In the
CC epidermis, the levels of ceramides with fatty acid chains containing
CC more than 26 carbons are decreased, while the levels of ceramides with
CC less than 24 carbons are increased (PubMed:23689133).
CC {ECO:0000269|PubMed:23689133}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03201}.
CC -!- CAUTION: The substrate specificity could be slightly different compared
CC to human ELOVL1, AC Q9BW60. No activity toward octadecanoyl-CoA, for
CC instance, is observed in vivo (PubMed:23689133).
CC {ECO:0000269|PubMed:23689133, ECO:0000305|PubMed:23689133}.
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DR EMBL; AF170907; AAF72572.1; -; mRNA.
DR EMBL; BC006735; AAH06735.1; -; mRNA.
DR EMBL; AK003743; BAB22975.1; -; mRNA.
DR CCDS; CCDS18549.1; -.
DR RefSeq; NP_001034264.1; NM_001039175.2.
DR RefSeq; NP_001034265.1; NM_001039176.2.
DR RefSeq; NP_062295.1; NM_019422.3.
DR RefSeq; XP_006503296.1; XM_006503233.2.
DR AlphaFoldDB; Q9JLJ5; -.
DR SMR; Q9JLJ5; -.
DR BioGRID; 207611; 1.
DR IntAct; Q9JLJ5; 1.
DR STRING; 10090.ENSMUSP00000006557; -.
DR SwissLipids; SLP:000000257; -.
DR PhosphoSitePlus; Q9JLJ5; -.
DR SwissPalm; Q9JLJ5; -.
DR EPD; Q9JLJ5; -.
DR jPOST; Q9JLJ5; -.
DR MaxQB; Q9JLJ5; -.
DR PaxDb; Q9JLJ5; -.
DR PRIDE; Q9JLJ5; -.
DR ProteomicsDB; 277821; -.
DR Antibodypedia; 32316; 224 antibodies from 26 providers.
DR Ensembl; ENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390.
DR Ensembl; ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390.
DR Ensembl; ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390.
DR GeneID; 54325; -.
DR KEGG; mmu:54325; -.
DR UCSC; uc008ujz.2; mouse.
DR CTD; 64834; -.
DR MGI; MGI:1858959; Elovl1.
DR VEuPathDB; HostDB:ENSMUSG00000006390; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_0_1; -.
DR InParanoid; Q9JLJ5; -.
DR OMA; KVAPGGM; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9JLJ5; -.
DR TreeFam; TF323454; -.
DR Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 54325; 10 hits in 77 CRISPR screens.
DR ChiTaRS; Elovl1; mouse.
DR PRO; PR:Q9JLJ5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JLJ5; protein.
DR Bgee; ENSMUSG00000006390; Expressed in condyle and 243 other tissues.
DR ExpressionAtlas; Q9JLJ5; baseline and differential.
DR Genevisible; Q9JLJ5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; ISS: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; 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; 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; ISS: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; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..279
FT /note="Elongation of very long chain fatty acids protein 1"
FT /id="PRO_0000207537"
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 203..223
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:0000250|UniProtKB:Q9BW60"
FT CONFLICT 78..79
FT /note="YE -> MR (in Ref. 3; BAB22975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 32678 MW; CA5A1CF55FDB2F76 CRC64;
MEAVVNLYHE LMKHADPRIQ SYPLMGSPLL ITSILLTYVY FILSLGPRIM ANRKPFQLRG
FMIVYNFSLV ILSLYIVYEF LMSGWLSTYT WRCDPIDFSN SPEALRMVRV AWLFMLSKVI
ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW SWWWGIKIAP GGMGSFHAMI NSSVHVVMYL
YYGLSALGPV AQPYLWWKKH MTAIQLIQFV LVSLHISQYY FMPSCNYQYP IIIHLIWMYG
TIFFILFSNF WYHSYTKGKR LPRAVQQNGA PATTKVKAN
