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Q9GZR5

- ELOV4_HUMAN

UniProt

Q9GZR5 - ELOV4_HUMAN

Protein

Elongation of very long chain fatty acids protein 4

Gene

ELOVL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. G-protein coupled photoreceptor activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. detection of visible light Source: GOC
    3. fatty acid biosynthetic process Source: UniProtKB
    4. fatty acid elongation, saturated fatty acid Source: UniProtKB
    5. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. triglyceride biosynthetic process Source: Reactome
    8. very long-chain fatty acid biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000118402-MONOMER.
    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ELOVL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14415. ELOVL4.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. integral component of endoplasmic reticulum membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Ichthyosis, Mental retardation, Stargardt disease

    Organism-specific databases

    MIMi600110. phenotype.
    614457. phenotype.
    Orphaneti352333. Congenital ichthyosis - intellectual disability - spastic quadriplegia.
    827. Stargardt disease.
    PharmGKBiPA27763.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Elongation of very long chain fatty acids protein 4PRO_0000207542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi20 – 201N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9GZR5.
    PRIDEiQ9GZR5.

    PTM databases

    PhosphoSiteiQ9GZR5.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    BgeeiQ9GZR5.
    CleanExiHS_ELOVL4.
    GenevestigatoriQ9GZR5.

    Interactioni

    Subunit structurei

    Oligomer.

    Protein-protein interaction databases

    BioGridi112661. 3 interactions.
    STRINGi9606.ENSP00000358831.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GZR5.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei42 – 6221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei165 – 18521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei188 – 20821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei247 – 26721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi310 – 3145Di-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.
    HOGENOMiHOG000038120.
    HOVERGENiHBG051468.
    InParanoidiQ9GZR5.
    KOiK10249.
    OMAiFYVRTYK.
    OrthoDBiEOG7Z3F4V.
    PhylomeDBiQ9GZR5.
    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.

    Q9GZR5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL    50
    SISTLYLLFV WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG 100
    SYNAGYSYIC QSVDYSNNVH EVRIAAALWW YFVSKGVEYL DTVFFILRKK 150
    NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ AFFGAQLNSF IHVIMYSYYG 200
    LTAFGPWIQK YLWWKRYLTM LQLIQFHVTI GHTALSLYTD CPFPKWMHWA 250
    LIAYAISFIF LFLNFYIRTY KEPKKPKAGK TAMNGISANG VSKSEKQLMI 300
    ENGKKQKNGK AKGD 314
    Length:314
    Mass (Da):36,829
    Last modified:March 1, 2001 - v1
    Checksum:iB2EBCE54D868E96E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441Q → R in AAH38506. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti267 – 2671I → T.1 Publication
    Corresponds to variant rs148594713 [ dbSNP | Ensembl ].
    VAR_017043
    Natural varianti299 – 2991M → V.2 Publications
    Corresponds to variant rs3812153 [ dbSNP | Ensembl ].
    VAR_012492

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF279654
    , 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.
    CCDSiCCDS4992.1.
    RefSeqiNP_073563.1. NM_022726.3.
    UniGeneiHs.101915.

    Genome annotation databases

    EnsembliENST00000369816; ENSP00000358831; ENSG00000118402.
    GeneIDi6785.
    KEGGihsa:6785.
    UCSCiuc003pja.4. human.

    Polymorphism databases

    DMDMi20137966.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the ELOVL4 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF279654
    , 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 .
    CCDSi CCDS4992.1.
    RefSeqi NP_073563.1. NM_022726.3.
    UniGenei Hs.101915.

    3D structure databases

    ProteinModelPortali Q9GZR5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112661. 3 interactions.
    STRINGi 9606.ENSP00000358831.

    Chemistry

    DrugBanki DB00132. Alpha-Linolenic Acid.

    PTM databases

    PhosphoSitei Q9GZR5.

    Polymorphism databases

    DMDMi 20137966.

    Proteomic databases

    PaxDbi Q9GZR5.
    PRIDEi Q9GZR5.

    Protocols and materials databases

    DNASUi 6785.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369816 ; ENSP00000358831 ; ENSG00000118402 .
    GeneIDi 6785.
    KEGGi hsa:6785.
    UCSCi uc003pja.4. human.

    Organism-specific databases

    CTDi 6785.
    GeneCardsi GC06M080624.
    HGNCi HGNC:14415. ELOVL4.
    MIMi 600110. phenotype.
    605512. gene.
    614457. phenotype.
    neXtProti NX_Q9GZR5.
    Orphaneti 352333. Congenital ichthyosis - intellectual disability - spastic quadriplegia.
    827. Stargardt disease.
    PharmGKBi PA27763.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305096.
    HOGENOMi HOG000038120.
    HOVERGENi HBG051468.
    InParanoidi Q9GZR5.
    KOi K10249.
    OMAi FYVRTYK.
    OrthoDBi EOG7Z3F4V.
    PhylomeDBi Q9GZR5.
    TreeFami TF323454.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000118402-MONOMER.
    Reactomei REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    GeneWikii ELOVL4.
    GenomeRNAii 6785.
    NextBioi 26492.
    PROi Q9GZR5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9GZR5.
    CleanExi HS_ELOVL4.
    Genevestigatori Q9GZR5.

    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

    1. 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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiELOV4_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZR5
    Secondary accession number(s): B2R6B5
    , Q5TCS2, Q86YJ1, Q9H139
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3