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Q9GZR5 (ELOV4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation of very long chain fatty acids protein 4

EC=2.3.1.199
Alternative name(s):
3-keto acyl-CoA synthase ELOVL4
ELOVL fatty acid elongase 4
Short name=ELOVL FA elongase 4
Very-long-chain 3-oxoacyl-CoA synthase 4
Gene names
Name:ELOVL4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Condensing enzyme that elongates saturated and monounsaturated very long chain fatty acids (VLCFAs). Elongates C24:0 and C26:0 acyl-CoAs. Seems to represent a photoreceptor-specific component of the fatty acid elongation system residing on the endoplasmic reticulum. May be implicated in docosahexaenoic acid (DHA) biosynthesis, which requires dietary consumption of the essential alpha-linolenic acid and a subsequent series of three elongation steps. May play a critical role in early brain and skin development. Ref.8 Ref.9

Catalytic activity

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

Subunit structure

Oligomer. Ref.7

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7 Ref.8.

Tissue specificity

Expressed in the retina and at much lower level in the brain. Ubiquitous, highest expression in thymus, followed by testis, small intestine, ovary, and prostate. Little or no expression in heart, lung, liver, or leukocates. Ref.8

Domain

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

Involvement in disease

Stargardt disease 3 (STGD3) [MIM:600110]: A common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Ichthyosis, spastic quadriplegia, and mental retardation (ISQMR) [MIM:614457]: A severe autosomal recessive disorder characterized by ichthyosis apparent from birth, profound psychomotor retardation with essentially no development, spastic quadriplegia, and seizures.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9

Sequence similarities

Belongs to the ELO family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseIchthyosis
Mental retardation
Stargardt disease
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

detection of visible light

Non-traceable author statement Ref.1. Source: GOC

fatty acid biosynthetic process

Non-traceable author statement Ref.1. Source: UniProtKB

fatty acid elongation, saturated fatty acid

Inferred from direct assay Ref.8. Source: UniProtKB

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

very long-chain fatty acid biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.8. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionG-protein coupled photoreceptor activity

Non-traceable author statement Ref.1. Source: UniProtKB

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Elongation of very long chain fatty acids protein 4
PRO_0000207542

Regions

Transmembrane42 – 6221Helical; Potential
Transmembrane78 – 9821Helical; Potential
Transmembrane165 – 18521Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane247 – 26721Helical; Potential
Motif310 – 3145Di-lysine motif Potential

Amino acid modifications

Glycosylation201N-linked (GlcNAc...) Ref.7

Natural variations

Natural variant2671I → T. Ref.10
Corresponds to variant rs148594713 [ dbSNP | Ensembl ].
VAR_017043
Natural variant2991M → V. Ref.1 Ref.10
Corresponds to variant rs3812153 [ dbSNP | Ensembl ].
VAR_012492

Experimental info

Sequence conflict441Q → R in AAH38506. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9GZR5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B2EBCE54D868E96E

FASTA31436,829
        10         20         30         40         50         60 
MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL SISTLYLLFV 

        70         80         90        100        110        120 
WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG SYNAGYSYIC QSVDYSNNVH 

       130        140        150        160        170        180 
EVRIAAALWW YFVSKGVEYL DTVFFILRKK NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ 

       190        200        210        220        230        240 
AFFGAQLNSF IHVIMYSYYG LTAFGPWIQK YLWWKRYLTM LQLIQFHVTI GHTALSLYTD 

       250        260        270        280        290        300 
CPFPKWMHWA LIAYAISFIF LFLNFYIRTY KEPKKPKAGK TAMNGISANG VSKSEKQLMI 

       310 
ENGKKQKNGK AKGD 

« Hide

References

« Hide 'large scale' references
[1]"A 5-bp deletion in ELOVL4 is associated with two related forms of autosomal dominant macular dystrophy."
Zhang K., Kniazeva M., Han M., Li W., Yu Z., Yang Z., Li Y., Metzker M.L., Allikmets R., Zack D.J., Kakuk L.E., Lagali P.S., Wong P.W., McDonald I.M., Sieving P.A., Figueroa D.J., Austin C.P., Gould R.J., Ayyagari R., Petrukhin K.
Nat. Genet. 27:89-93(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT VAL-299, DISEASE.
Tissue: Retina.
[2]"A novel gene for autosomal dominant Stargardt-like macular dystrophy with homology to the SUR4 protein family."
Edwards A.O., Donoso L.A., Ritter R. III
Invest. Ophthalmol. Vis. Sci. 42:2652-2663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Thalamus.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Brain.
[7]"Dominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4."
Grayson C., Molday R.S.
J. Biol. Chem. 280:32521-32530(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, OLIGOMERIZATION, GLYCOSYLATION AT ASN-20.
[8]"ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis."
Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y., Sassa T., Kihara A.
Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Recessive mutations in ELOVL4 cause ichthyosis, intellectual disability, and spastic quadriplegia."
Aldahmesh M.A., Mohamed J.Y., Alkuraya H.S., Verma I.C., Puri R.D., Alaiya A.A., Rizzo W.B., Alkuraya F.S.
Am. J. Hum. Genet. 89:745-750(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE ROLE IN BRAIN AND SKIN DEVELOPMENT, INVOLVEMENT IN ISQMR.
[10]"Evaluation of the ELOVL4 gene in patients with autosomal recessive retinitis pigmentosa and Leber congenital amaurosis."
Rivolta C., Ayyagari R., Sieving P.A., Berson E.L., Dryja T.P.
Mol. Vis. 9:49-51(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-267 AND VAL-299.
+Additional computationally mapped references.

Web resources

Mutations of the ELOVL4 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF279654 expand/collapse EMBL AC list , AF279649, AF279650, AF279651, AF279652, AF279653 Genomic DNA. Translation: AAG47669.1.
AF277094 mRNA. Translation: AAG47668.1.
AY037298 mRNA. Translation: AAK68639.1.
AK055277 mRNA. Translation: BAB70895.1.
AK312511 mRNA. Translation: BAG35412.1.
AL133475, AL132875 Genomic DNA. Translation: CAI20320.1.
AL132875, AL133475 Genomic DNA. Translation: CAI23374.1.
CH471051 Genomic DNA. Translation: EAW48701.1.
BC038506 mRNA. Translation: AAH38506.1.
RefSeqNP_073563.1. NM_022726.3.
UniGeneHs.101915.

3D structure databases

ProteinModelPortalQ9GZR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112661. 3 interactions.
STRING9606.ENSP00000358831.

Chemistry

DrugBankDB00132. Alpha-Linolenic Acid.

PTM databases

PhosphoSiteQ9GZR5.

Polymorphism databases

DMDM20137966.

Proteomic databases

PaxDbQ9GZR5.
PRIDEQ9GZR5.

Protocols and materials databases

DNASU6785.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369816; ENSP00000358831; ENSG00000118402.
GeneID6785.
KEGGhsa:6785.
UCSCuc003pja.4. human.

Organism-specific databases

CTD6785.
GeneCardsGC06M080624.
HGNCHGNC:14415. ELOVL4.
MIM600110. phenotype.
605512. gene.
614457. phenotype.
neXtProtNX_Q9GZR5.
Orphanet352333. Congenital ichthyosis - intellectual deficit - spastic quadriplegia.
827. Stargardt disease.
PharmGKBPA27763.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305096.
HOGENOMHOG000038120.
HOVERGENHBG051468.
InParanoidQ9GZR5.
KOK10249.
OMAFYVRTYK.
OrthoDBEOG7Z3F4V.
PhylomeDBQ9GZR5.
TreeFamTF323454.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000118402-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ9GZR5.
CleanExHS_ELOVL4.
GenevestigatorQ9GZR5.

Family and domain databases

InterProIPR002076. GNS1_SUR4.
[Graphical view]
PANTHERPTHR11157. PTHR11157. 1 hit.
PfamPF01151. ELO. 1 hit.
[Graphical view]
PROSITEPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiELOVL4.
GenomeRNAi6785.
NextBio26492.
PROQ9GZR5.
SOURCESearch...

Entry information

Entry nameELOV4_HUMAN
AccessionPrimary (citable) accession number: Q9GZR5
Secondary accession number(s): B2R6B5 expand/collapse secondary AC list , Q5TCS2, Q86YJ1, Q9H139
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM