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Q9JLJ5

- ELOV1_MOUSE

UniProt

Q9JLJ5 - ELOV1_MOUSE

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Protein

Elongation of very long chain fatty acids protein 1

Gene
Elovl1, Ssc1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Condensing enzyme that catalyzes the synthesis of both saturated and monounsaturated very long chain fatty acids (VLCFAs). Exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. 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.

GO - Molecular functioni

  1. fatty acid elongase activity Source: Ensembl

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

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 1 (EC:2.3.1.199)
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: Chromosome 4

Organism-specific databases

MGIiMGI:1858959. Elovl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321Helical; Reviewed predictionAdd
BLAST
Transmembranei61 – 8121Helical; Reviewed predictionAdd
BLAST
Transmembranei176 – 19621Helical; Reviewed predictionAdd
BLAST
Transmembranei203 – 22321Helical; Reviewed predictionAdd
BLAST
Transmembranei231 – 25121Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
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-acetylmethionine By 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

ArrayExpressiQ9JLJ5.
BgeeiQ9JLJ5.
GenevestigatoriQ9JLJ5.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064816.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi275 – 2795Di-lysine motif Reviewed prediction

Domaini

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

Sequence similaritiesi

Belongs to the ELO family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00740000115027.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9JLJ5.
KOiK10247.
OMAiWGVKIAP.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9JLJ5.
TreeFamiTF323454.

Family and domain databases

InterProiIPR002076. GNS1_SUR4.
[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

MEAVVNLYHE LMKHADPRIQ SYPLMGSPLL ITSILLTYVY FILSLGPRIM    50
ANRKPFQLRG FMIVYNFSLV ILSLYIVYEF LMSGWLSTYT WRCDPIDFSN 100
SPEALRMVRV AWLFMLSKVI ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW 150
SWWWGIKIAP GGMGSFHAMI NSSVHVVMYL YYGLSALGPV AQPYLWWKKH 200
MTAIQLIQFV LVSLHISQYY FMPSCNYQYP IIIHLIWMYG TIFFILFSNF 250
WYHSYTKGKR LPRAVQQNGA PATTKVKAN 279
Length:279
Mass (Da):32,678
Last modified:October 1, 2000 - v1
Checksum:iCA5A1CF55FDB2F76
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792YE → MR in BAB22975. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF170907 mRNA. Translation: AAF72572.1 .
BC006735 mRNA. Translation: AAH06735.1 .
AK003743 mRNA. Translation: BAB22975.1 .
CCDSi CCDS18549.1.
RefSeqi NP_001034264.1. NM_001039175.2.
NP_001034265.1. NM_001039176.2.
NP_062295.1. NM_019422.3.
XP_006503296.1. XM_006503233.1.
UniGenei Mm.282096.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000064816.

PTM databases

PhosphoSitei Q9JLJ5.

Proteomic databases

MaxQBi Q9JLJ5.
PaxDbi Q9JLJ5.
PRIDEi Q9JLJ5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006557 ; ENSMUSP00000006557 ; ENSMUSG00000006390 .
ENSMUST00000067896 ; ENSMUSP00000064816 ; ENSMUSG00000006390 .
ENSMUST00000167636 ; ENSMUSP00000126685 ; ENSMUSG00000006390 .
GeneIDi 54325.
KEGGi mmu:54325.
UCSCi uc008ujz.1. mouse.

Organism-specific databases

CTDi 64834.
MGIi MGI:1858959. Elovl1.

Phylogenomic databases

eggNOGi NOG305096.
GeneTreei ENSGT00740000115027.
HOGENOMi HOG000038120.
HOVERGENi HBG051468.
InParanoidi Q9JLJ5.
KOi K10247.
OMAi WGVKIAP.
OrthoDBi EOG7Z3F4V.
PhylomeDBi Q9JLJ5.
TreeFami TF323454.

Miscellaneous databases

NextBioi 311104.
PROi Q9JLJ5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9JLJ5.
Bgeei Q9JLJ5.
Genevestigatori Q9JLJ5.

Family and domain databases

InterProi IPR002076. GNS1_SUR4.
[Graphical view ]
PANTHERi PTHR11157. PTHR11157. 1 hit.
Pfami PF01151. ELO. 1 hit.
[Graphical view ]
PROSITEi PS01188. ELO. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 102 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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