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Protein

Elongation of very long chain fatty acids protein 4

Gene

Elovl4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 specifically elongates C24:0 and C26:0 acyl-CoAs. 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. May play a critical role in early brain and skin development.UniRule annotation

Catalytic activityi

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

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
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-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000264.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 4UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
Alternative name(s):
3-keto acyl-CoA synthase Elovl4UniRule annotation
ELOVL fatty acid elongase 4UniRule annotation
Short name:
ELOVL FA elongase 4UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 4UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 4UniRule annotation
Gene namesi
Name:Elovl4UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1933331. Elovl4.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei42 – 6221HelicalUniRule annotationAdd
BLAST
Transmembranei78 – 9821HelicalUniRule annotationAdd
BLAST
Transmembranei127 – 14721HelicalUniRule annotationAdd
BLAST
Transmembranei165 – 18521HelicalUniRule annotationAdd
BLAST
Transmembranei188 – 20821HelicalUniRule annotationAdd
BLAST
Transmembranei217 – 23721HelicalUniRule annotationAdd
BLAST
Transmembranei246 – 26621HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Elongation of very long chain fatty acids protein 4PRO_0000207545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi20 – 201N-linked (GlcNAc...)UniRule annotation
Glycosylationi292 – 2921N-linked (GlcNAc...)UniRule annotation

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9EQC4.
PaxDbiQ9EQC4.
PRIDEiQ9EQC4.

PTM databases

PhosphoSiteiQ9EQC4.

Expressioni

Tissue specificityi

Expressed in the retina, exclusively in photoreceptor cells and in the brain, skin, testis and lens.1 Publication

Developmental stagei

Expressed in the ocular tissues of the retina at 10.5 dpc and becomes restricted predominantly to the photoreceptor layer in the mature retina (at protein level). Expressed in the embryo at 7 dpc.1 Publication

Gene expression databases

BgeeiQ9EQC4.
ExpressionAtlasiQ9EQC4. baseline and differential.
GenevisibleiQ9EQC4. MM.

Interactioni

Subunit structurei

Oligomer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034796.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi308 – 3125Di-lysine motifUniRule annotation

Domaini

The C-terminal di-lysine motif may confer endoplasmic reticulum localization.UniRule annotation

Sequence similaritiesi

Belongs to the ELO family. ELOVL4 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9EQC4.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG7Z3F4V.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03204. VLCF_elongase_4.
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.

Q9EQC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLDSEPGS VLNAMSTAFN DTVEFYRWTW TIADKRVADW PLMQSPWPTI
60 70 80 90 100
SISTLYLLFV WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG
110 120 130 140 150
SYNAGYSYIC QSVDYSNDVN EVRIAGALWW YFVSKGVEYL DTVFFILRKK
160 170 180 190 200
NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ AFFGAQMNSF IHVIMYSYYG
210 220 230 240 250
LTAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD CPFPKWMHWA
260 270 280 290 300
LIAYAISFIF LFLNFYTRTY NEPKQSKTGK TATNGISSNG VNKSEKALEN
310
GKPQKNGKPK GE
Length:312
Mass (Da):36,506
Last modified:July 27, 2011 - v2
Checksum:iB049772627D28294
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261G → A in AAG47667 (PubMed:11138005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277093 mRNA. Translation: AAG47667.1.
AJ550628
, AJ550629, AJ550630, AJ550631, AJ550632, AJ550633 Genomic DNA. Translation: CAD80158.4.
AK029065 mRNA. Translation: BAC26274.1.
CH466522 Genomic DNA. Translation: EDL26470.1.
BC037030 mRNA. Translation: AAH37030.1.
CCDSiCCDS23376.1.
RefSeqiNP_683743.2. NM_148941.2.
UniGeneiMm.83949.

Genome annotation databases

EnsembliENSMUST00000034796; ENSMUSP00000034796; ENSMUSG00000032262.
GeneIDi83603.
KEGGimmu:83603.
UCSCiuc012gxk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277093 mRNA. Translation: AAG47667.1.
AJ550628
, AJ550629, AJ550630, AJ550631, AJ550632, AJ550633 Genomic DNA. Translation: CAD80158.4.
AK029065 mRNA. Translation: BAC26274.1.
CH466522 Genomic DNA. Translation: EDL26470.1.
BC037030 mRNA. Translation: AAH37030.1.
CCDSiCCDS23376.1.
RefSeqiNP_683743.2. NM_148941.2.
UniGeneiMm.83949.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034796.

Chemistry

SwissLipidsiSLP:000000264.

PTM databases

PhosphoSiteiQ9EQC4.

Proteomic databases

MaxQBiQ9EQC4.
PaxDbiQ9EQC4.
PRIDEiQ9EQC4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034796; ENSMUSP00000034796; ENSMUSG00000032262.
GeneIDi83603.
KEGGimmu:83603.
UCSCiuc012gxk.1. mouse.

Organism-specific databases

CTDi6785.
MGIiMGI:1933331. Elovl4.

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9EQC4.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG7Z3F4V.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiQ9EQC4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQC4.
ExpressionAtlasiQ9EQC4. baseline and differential.
GenevisibleiQ9EQC4. MM.

Family and domain databases

HAMAPiMF_03204. VLCF_elongase_4.
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "Characterization of mouse orthologue of ELOVL4: genomic organization and spatial and temporal expression."
    Mandal M.N., Ambasudhan R., Wong P.W., Gage P.J., Sieving P.A., Ayyagari R.
    Genomics 83:626-635(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
    Tissue: Brain.
  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].
    Strain: C57BL/6J.
    Tissue: Skin.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Eye.

Entry informationi

Entry nameiELOV4_MOUSE
AccessioniPrimary (citable) accession number: Q9EQC4
Secondary accession number(s): Q8JZV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 102 of the entry and version 2 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.