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Protein

Elongation of very long chain fatty acids protein 6

Gene

Elovl6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.UniRule annotation2 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000454.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 6UniRule annotationCurated (EC:2.3.1.199UniRule annotation1 Publication)
Alternative name(s):
3-keto acyl-CoA synthase Elovl6UniRule annotation
ELOVL fatty acid elongase 6UniRule annotation
Short name:
ELOVL FA elongase 6UniRule annotation
Fatty acyl-CoA elongase
Long chain fatty acid elongase
Myelin-associated SUR4 protein
Very long chain 3-ketoacyl-CoA synthase 6UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 6UniRule annotation
Gene namesi
Name:Elovl6UniRule annotation
Synonyms:Face, Lce, Masr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2156528. Elovl6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5118HelicalUniRule annotationAdd
BLAST
Transmembranei70 – 9021HelicalUniRule annotationAdd
BLAST
Transmembranei111 – 13121HelicalUniRule annotationAdd
BLAST
Transmembranei136 – 15621HelicalUniRule annotationAdd
BLAST
Transmembranei159 – 17921HelicalUniRule annotationAdd
BLAST
Transmembranei197 – 21721HelicalUniRule annotationAdd
BLAST
Transmembranei234 – 25421HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5726.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Elongation of very long chain fatty acids protein 6PRO_0000282846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi2 – 21N-linked (GlcNAc...)UniRule annotation

Post-translational modificationi

N-Glycosylated.UniRule annotation

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ920L5.
PaxDbiQ920L5.
PRIDEiQ920L5.

PTM databases

PhosphoSiteiQ920L5.

Expressioni

Tissue specificityi

Highly expressed in adrenal gland, liver, white adipose tissue (WAT), adult and fetal brain, cerebellum, spinal cord, testis, skin and peripheral nerve; where lipogenesis and steroidogenesis are active. Weakly expressed in kidney, heart, skeletal muscle, lung, and spleen.3 Publications

Inductioni

By SREBF1.2 Publications

Gene expression databases

BgeeiQ920L5.
ExpressionAtlasiQ920L5. baseline and differential.
GenevisibleiQ920L5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071351.

Chemistry

BindingDBiQ920L5.

Structurei

3D structure databases

ProteinModelPortaliQ920L5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELO family. ELOVL6 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3072. Eukaryota.
ENOG410Z3FZ. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038943.
HOVERGENiHBG099423.
InParanoidiQ920L5.
KOiK10203.
OMAiCITILCY.
OrthoDBiEOG7MKW6F.
PhylomeDBiQ920L5.
TreeFamiTF106467.

Family and domain databases

HAMAPiMF_03206. VLCF_elongase_6.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q920L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL
60 70 80 90 100
MNKRAKFELR KPLVLWSLTL AVFSIFGALR TGAYMLYILM TKGLKQSVCD
110 120 130 140 150
QSFYNGPVSK FWAYAFVLSK APELGDTIFI ILRKQKLIFL HWYHHITVLL
160 170 180 190 200
YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY YALRAAGFRV SRKFAMFITL
210 220 230 240 250
SQITQMLMGC VINYLVFNWM QHDNDQCYSH FQNIFWSSLM YLSYLVLFCH
260
FFFEAYIGKV KKATKAE
Length:267
Mass (Da):31,610
Last modified:December 1, 2001 - v1
Checksum:i4026C9CB33FDDD23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441H → Q in BAC26252 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY053453 mRNA. Translation: AAL14239.1.
AB072039 mRNA. Translation: BAB68544.1.
AF480860 mRNA. Translation: AAM13450.1.
AK029029 mRNA. Translation: BAC26252.1.
AK167373 mRNA. Translation: BAE39469.1.
BC051041 mRNA. Translation: AAH51041.1.
BC098492 mRNA. Translation: AAH98492.1.
BC100576 mRNA. Translation: AAI00577.1.
CCDSiCCDS38632.1.
RefSeqiNP_569717.1. NM_130450.2.
UniGeneiMm.314113.

Genome annotation databases

EnsembliENSMUST00000071402; ENSMUSP00000071351; ENSMUSG00000041220.
ENSMUST00000199910; ENSMUSP00000142832; ENSMUSG00000041220.
GeneIDi170439.
KEGGimmu:170439.
UCSCiuc008rid.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY053453 mRNA. Translation: AAL14239.1.
AB072039 mRNA. Translation: BAB68544.1.
AF480860 mRNA. Translation: AAM13450.1.
AK029029 mRNA. Translation: BAC26252.1.
AK167373 mRNA. Translation: BAE39469.1.
BC051041 mRNA. Translation: AAH51041.1.
BC098492 mRNA. Translation: AAH98492.1.
BC100576 mRNA. Translation: AAI00577.1.
CCDSiCCDS38632.1.
RefSeqiNP_569717.1. NM_130450.2.
UniGeneiMm.314113.

3D structure databases

ProteinModelPortaliQ920L5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071351.

Chemistry

BindingDBiQ920L5.
ChEMBLiCHEMBL5726.
SwissLipidsiSLP:000000454.

PTM databases

PhosphoSiteiQ920L5.

Proteomic databases

MaxQBiQ920L5.
PaxDbiQ920L5.
PRIDEiQ920L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071402; ENSMUSP00000071351; ENSMUSG00000041220.
ENSMUST00000199910; ENSMUSP00000142832; ENSMUSG00000041220.
GeneIDi170439.
KEGGimmu:170439.
UCSCiuc008rid.1. mouse.

Organism-specific databases

CTDi79071.
MGIiMGI:2156528. Elovl6.

Phylogenomic databases

eggNOGiKOG3072. Eukaryota.
ENOG410Z3FZ. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038943.
HOVERGENiHBG099423.
InParanoidiQ920L5.
KOiK10203.
OMAiCITILCY.
OrthoDBiEOG7MKW6F.
PhylomeDBiQ920L5.
TreeFamiTF106467.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiElovl6. mouse.
PROiQ920L5.
SOURCEiSearch...

Gene expression databases

BgeeiQ920L5.
ExpressionAtlasiQ920L5. baseline and differential.
GenevisibleiQ920L5. MM.

Family and domain databases

HAMAPiMF_03206. VLCF_elongase_6.
InterProiIPR030457. ELO_CS.
IPR002076. 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. "Identification of a mammalian long chain fatty acyl elongase regulated by sterol regulatory element-binding proteins."
    Moon Y.-A., Shah N.A., Mohapatra S., Warrington J.A., Horton J.D.
    J. Biol. Chem. 276:45358-45366(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INDUCTION BY SREBF1, TISSUE SPECIFICITY.
  2. "Cloning and characterization of a mammalian fatty acyl-CoA elongase as a lipogenic enzyme regulated by SREBPs."
    Matsuzaka T., Shimano H., Yahagi N., Yoshikawa T., Amemiya-Kudo M., Hasty A.H., Okazaki H., Tamura Y., Iizuka Y., Ohashi K., Osuga J., Takahashi A., Yato S., Sone H., Ishibashi S., Yamada N.
    J. Lipid Res. 43:911-920(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SREBF1.
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "Deciphering peripheral nerve myelination by using Schwann cell expression profiling."
    Nagarajan R., Le N., Mahoney H., Araki T., Milbrandt J.
    Proc. Natl. Acad. Sci. U.S.A. 99:8998-9003(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Amnion and Skin.
  5. "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].
    Strain: CD-1 and Czech II.
    Tissue: Mammary tumor and Neural stem cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue.

Entry informationi

Entry nameiELOV6_MOUSE
AccessioniPrimary (citable) accession number: Q920L5
Secondary accession number(s): Q8CE45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 104 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

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 one 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.