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Protein

Elongation of very long chain fatty acids protein 1

Gene

Elovl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs.2 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.By similarity

Pathwayi

GO - Molecular functioni

  1. fatty acid elongase activity Source: MGI

GO - Biological processi

  1. fatty acid elongation, monounsaturated fatty acid Source: UniProtKB
  2. fatty acid elongation, saturated fatty acid Source: UniProtKB
  3. sphingolipid biosynthetic process Source: UniProtKB
  4. very long-chain fatty acid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_292148. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 1Curated (EC:2.3.1.199By similarity)
Alternative name(s):
3-keto acyl-CoA synthase Elovl1
ELOVL fatty acid elongase 1
Short name:
ELOVL FA elongase 1
Very-long-chain 3-oxoacyl-CoA synthase 1
Gene namesi
Name:Elovl1
Synonyms:Ssc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1858959. Elovl1.

Subcellular locationi

  1. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321HelicalSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence AnalysisAdd
BLAST
Transmembranei203 – 22321HelicalSequence AnalysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Elongation of very long chain fatty acids protein 1PRO_0000207537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JLJ5.
PaxDbiQ9JLJ5.
PRIDEiQ9JLJ5.

PTM databases

PhosphoSiteiQ9JLJ5.

Expressioni

Tissue specificityi

Expressed in a broad variety of tissues. Highly expressed in stomach, lung, kidney, skin and intestine. Moderately expressed in white adipose tissue, liver, spleen, brain, brown adipose tissue, heart and muscle. Weakly expressed in testis.1 Publication

Gene expression databases

BgeeiQ9JLJ5.
ExpressionAtlasiQ9JLJ5. baseline and differential.
GenevestigatoriQ9JLJ5.

Interactioni

Subunit structurei

Interacts with LASS2, TECR and HSD17B12.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064816.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi275 – 2795Di-lysine motifSequence Analysis

Domaini

The di-lysine motif may confer endoplasmic reticulum localization.By similarity

Sequence similaritiesi

Belongs to the ELO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9JLJ5.
KOiK10247.
OMAiWGVKIAP.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9JLJ5.
TreeFamiTF323454.

Family and domain databases

InterProiIPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JLJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVVNLYHE LMKHADPRIQ SYPLMGSPLL ITSILLTYVY FILSLGPRIM
60 70 80 90 100
ANRKPFQLRG FMIVYNFSLV ILSLYIVYEF LMSGWLSTYT WRCDPIDFSN
110 120 130 140 150
SPEALRMVRV AWLFMLSKVI ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW
160 170 180 190 200
SWWWGIKIAP GGMGSFHAMI NSSVHVVMYL YYGLSALGPV AQPYLWWKKH
210 220 230 240 250
MTAIQLIQFV LVSLHISQYY FMPSCNYQYP IIIHLIWMYG TIFFILFSNF
260 270
WYHSYTKGKR LPRAVQQNGA PATTKVKAN
Length:279
Mass (Da):32,678
Last modified:October 1, 2000 - v1
Checksum:iCA5A1CF55FDB2F76
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792YE → MR in BAB22975 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170907 mRNA. Translation: AAF72572.1.
BC006735 mRNA. Translation: AAH06735.1.
AK003743 mRNA. Translation: BAB22975.1.
CCDSiCCDS18549.1.
RefSeqiNP_001034264.1. NM_001039175.2.
NP_001034265.1. NM_001039176.2.
NP_062295.1. NM_019422.3.
XP_006503296.1. XM_006503233.1.
UniGeneiMm.282096.

Genome annotation databases

EnsembliENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390.
ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390.
ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390.
GeneIDi54325.
KEGGimmu:54325.
UCSCiuc008ujz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170907 mRNA. Translation: AAF72572.1.
BC006735 mRNA. Translation: AAH06735.1.
AK003743 mRNA. Translation: BAB22975.1.
CCDSiCCDS18549.1.
RefSeqiNP_001034264.1. NM_001039175.2.
NP_001034265.1. NM_001039176.2.
NP_062295.1. NM_019422.3.
XP_006503296.1. XM_006503233.1.
UniGeneiMm.282096.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064816.

PTM databases

PhosphoSiteiQ9JLJ5.

Proteomic databases

MaxQBiQ9JLJ5.
PaxDbiQ9JLJ5.
PRIDEiQ9JLJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390.
ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390.
ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390.
GeneIDi54325.
KEGGimmu:54325.
UCSCiuc008ujz.1. mouse.

Organism-specific databases

CTDi64834.
MGIiMGI:1858959. Elovl1.

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9JLJ5.
KOiK10247.
OMAiWGVKIAP.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9JLJ5.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiREACT_292148. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi311104.
PROiQ9JLJ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLJ5.
ExpressionAtlasiQ9JLJ5. baseline and differential.
GenevestigatoriQ9JLJ5.

Family and domain databases

InterProiIPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Role of a new mammalian gene family in the biosynthesis of very long chain fatty acids and sphingolipids."
    Tvrdik P., Westerberg R., Silve S., Asadi A., Jakobsson A., Cannon B., Loison G., Jacobsson A.
    J. Cell Biol. 149:707-718(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-279.
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Fatty acid transport protein 4 (FATP4) prevents light-induced degeneration of cone and rod photoreceptors by inhibiting RPE65 isomerase."
    Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G., Miner J.H., Jin M.
    J. Neurosci. 33:3178-3189(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiELOV1_MOUSE
AccessioniPrimary (citable) accession number: Q9JLJ5
Secondary accession number(s): Q9D1B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.