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Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)

 ELOV4_HUMAN             Reviewed;         314 AA.
Q9GZR5; B2R6B5; Q5TCS2; Q86YJ1; Q9H139;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 157.
RecName: Full=Elongation of very long chain fatty acids protein 4 {ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000305};
EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:20937905};
AltName: Full=3-keto acyl-CoA synthase ELOVL4 {ECO:0000255|HAMAP-Rule:MF_03204};
AltName: Full=ELOVL fatty acid elongase 4 {ECO:0000255|HAMAP-Rule:MF_03204};
Short=ELOVL FA elongase 4 {ECO:0000255|HAMAP-Rule:MF_03204};
AltName: Full=Very long chain 3-ketoacyl-CoA synthase 4 {ECO:0000255|HAMAP-Rule:MF_03204};
AltName: Full=Very long chain 3-oxoacyl-CoA synthase 4 {ECO:0000255|HAMAP-Rule:MF_03204};
Name=ELOVL4 {ECO:0000255|HAMAP-Rule:MF_03204};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT VAL-299, AND
DISEASE.
TISSUE=Retina;
PubMed=11138005; DOI=10.1038/83817;
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.;
"A 5-bp deletion in ELOVL4 is associated with two related forms of
autosomal dominant macular dystrophy.";
Nat. Genet. 27:89-93(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN STGD3.
PubMed=11581213;
Edwards A.O., Donoso L.A., Ritter R. III;
"A novel gene for autosomal dominant Stargardt-like macular dystrophy
with homology to the SUR4 protein family.";
Invest. Ophthalmol. Vis. Sci. 42:2652-2663(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION, OLIGOMERIZATION, AND GLYCOSYLATION AT ASN-20.
PubMed=16036915; DOI=10.1074/jbc.M503411200;
Grayson C., Molday R.S.;
"Dominant negative mechanism underlies autosomal dominant Stargardt-
like macular dystrophy linked to mutations in ELOVL4.";
J. Biol. Chem. 280:32521-32530(2005).
[8]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=20937905; DOI=10.1073/pnas.1005572107;
Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
Sassa T., Kihara A.;
"ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
[9]
PROBABLE ROLE IN BRAIN AND SKIN DEVELOPMENT, AND INVOLVEMENT IN ISQMR.
PubMed=22100072; DOI=10.1016/j.ajhg.2011.10.011;
Aldahmesh M.A., Mohamed J.Y., Alkuraya H.S., Verma I.C., Puri R.D.,
Alaiya A.A., Rizzo W.B., Alkuraya F.S.;
"Recessive mutations in ELOVL4 cause ichthyosis, intellectual
disability, and spastic quadriplegia.";
Am. J. Hum. Genet. 89:745-750(2011).
[10]
VARIANTS THR-267 AND VAL-299.
PubMed=12592226;
Rivolta C., Ayyagari R., Sieving P.A., Berson E.L., Dryja T.P.;
"Evaluation of the ELOVL4 gene in patients with autosomal recessive
retinitis pigmentosa and Leber congenital amaurosis.";
Mol. Vis. 9:49-51(2003).
[11]
INVOLVEMENT IN SCA34, AND VARIANT SCA34 PHE-168.
PubMed=24566826; DOI=10.1001/jamaneurol.2013.6337;
Cadieux-Dion M., Turcotte-Gauthier M., Noreau A., Martin C.,
Meloche C., Gravel M., Drouin C.A., Rouleau G.A., Nguyen D.K.,
Cossette P.;
"Expanding the clinical phenotype associated with ELOVL4 mutation:
study of a large French-Canadian family with autosomal dominant
spinocerebellar ataxia and erythrokeratodermia.";
JAMA Neurol. 71:470-475(2014).
-!- FUNCTION: 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 in 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.
{ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:20937905}.
-!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + malonyl-CoA = CoA
+ a very-long-chain 3-oxoacyl-CoA + CO(2). {ECO:0000255|HAMAP-
Rule:MF_03204, ECO:0000269|PubMed:20937905}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:20937905}.
-!- SUBUNIT: Oligomer. {ECO:0000255|HAMAP-Rule:MF_03204,
ECO:0000269|PubMed:16036915}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:16036915,
ECO:0000269|PubMed:20937905}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03204}.
-!- 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.
{ECO:0000269|PubMed:20937905}.
-!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic
reticulum localization. {ECO:0000255|HAMAP-Rule:MF_03204}.
-!- 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. {ECO:0000269|PubMed:11138005,
ECO:0000269|PubMed:11581213}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:22100072}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Spinocerebellar ataxia 34 (SCA34) [MIM:133190]: A form of
spinocerebellar ataxia, a clinically and genetically heterogeneous
group of cerebellar disorders. Patients show progressive
incoordination of gait and often poor coordination of hands,
speech and eye movements, due to degeneration of the cerebellum
with variable involvement of the brainstem and spinal cord. SCA34
is an autosomal dominant form characterized by the association of
progressive cerebellar ataxia with erythrokeratodermia variabilis.
{ECO:0000269|PubMed:24566826}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03204}.
-!- WEB RESOURCE: Name=Mutations of the ELOVL4 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/elovlmut.htm";
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EMBL; AF279654; AAG47669.1; -; Genomic_DNA.
EMBL; AF279649; AAG47669.1; JOINED; Genomic_DNA.
EMBL; AF279650; AAG47669.1; JOINED; Genomic_DNA.
EMBL; AF279651; AAG47669.1; JOINED; Genomic_DNA.
EMBL; AF279652; AAG47669.1; JOINED; Genomic_DNA.
EMBL; AF279653; AAG47669.1; JOINED; Genomic_DNA.
EMBL; AF277094; AAG47668.1; -; mRNA.
EMBL; AY037298; AAK68639.1; -; mRNA.
EMBL; AK055277; BAB70895.1; -; mRNA.
EMBL; AK312511; BAG35412.1; -; mRNA.
EMBL; AL133475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL132875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48701.1; -; Genomic_DNA.
EMBL; BC038506; AAH38506.1; -; mRNA.
CCDS; CCDS4992.1; -.
RefSeq; NP_073563.1; NM_022726.3.
UniGene; Hs.101915; -.
ProteinModelPortal; Q9GZR5; -.
SMR; Q9GZR5; -.
BioGrid; 112661; 9.
IntAct; Q9GZR5; 78.
STRING; 9606.ENSP00000358831; -.
DrugBank; DB00132; Alpha-Linolenic Acid.
SwissLipids; SLP:000000255; -.
iPTMnet; Q9GZR5; -.
PhosphoSitePlus; Q9GZR5; -.
SwissPalm; Q9GZR5; -.
BioMuta; ELOVL4; -.
DMDM; 20137966; -.
EPD; Q9GZR5; -.
PaxDb; Q9GZR5; -.
PeptideAtlas; Q9GZR5; -.
PRIDE; Q9GZR5; -.
ProteomicsDB; 80120; -.
DNASU; 6785; -.
Ensembl; ENST00000369816; ENSP00000358831; ENSG00000118402.
GeneID; 6785; -.
KEGG; hsa:6785; -.
UCSC; uc003pja.5; human.
CTD; 6785; -.
DisGeNET; 6785; -.
EuPathDB; HostDB:ENSG00000118402.5; -.
GeneCards; ELOVL4; -.
HGNC; HGNC:14415; ELOVL4.
MalaCards; ELOVL4; -.
MIM; 133190; phenotype.
MIM; 600110; phenotype.
MIM; 605512; gene.
MIM; 614457; phenotype.
neXtProt; NX_Q9GZR5; -.
OpenTargets; ENSG00000118402; -.
Orphanet; 352333; Congenital ichthyosis - intellectual disability - spastic quadriplegia.
Orphanet; 1955; Spinocerebellar ataxia type 34.
Orphanet; 827; Stargardt disease.
PharmGKB; PA27763; -.
eggNOG; KOG3071; Eukaryota.
eggNOG; ENOG410XRWT; LUCA.
GeneTree; ENSGT00760000119122; -.
HOGENOM; HOG000038120; -.
HOVERGEN; HBG051468; -.
InParanoid; Q9GZR5; -.
KO; K10249; -.
OMA; FLWLGPK; -.
OrthoDB; EOG091G0N2V; -.
PhylomeDB; Q9GZR5; -.
TreeFam; TF323454; -.
BioCyc; MetaCyc:ENSG00000118402-MONOMER; -.
Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
UniPathway; UPA00094; -.
GeneWiki; ELOVL4; -.
GenomeRNAi; 6785; -.
PRO; PR:Q9GZR5; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118402; Expressed in 176 organ(s), highest expression level in mammalian vulva.
CleanEx; HS_ELOVL4; -.
Genevisible; Q9GZR5; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102337; F:3-oxo-cerotoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
GO; GO:0008020; F:G-protein coupled photoreceptor activity; NAS:UniProtKB.
GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0006633; P:fatty acid biosynthetic process; NAS:UniProtKB.
GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:UniProtKB.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB.
HAMAP; MF_03204; VLCF_elongase_4; 1.
InterPro; IPR030457; ELO_CS.
InterPro; IPR002076; ELO_fam.
InterPro; IPR033678; ELOVL4.
PANTHER; PTHR11157; PTHR11157; 1.
Pfam; PF01151; ELO; 1.
PROSITE; PS01188; ELO; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein;
Ichthyosis; Lipid biosynthesis; Lipid metabolism; Membrane;
Mental retardation; Neurodegeneration; Polymorphism;
Reference proteome; Spinocerebellar ataxia; Stargardt disease;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 314 Elongation of very long chain fatty acids
protein 4.
/FTId=PRO_0000207542.
TRANSMEM 42 62 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 78 98 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 127 147 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 165 185 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 188 208 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 217 237 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
TRANSMEM 247 267 Helical. {ECO:0000255|HAMAP-
Rule:MF_03204}.
MOTIF 310 314 Di-lysine motif. {ECO:0000255|HAMAP-
Rule:MF_03204}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03204,
ECO:0000269|PubMed:16036915}.
VARIANT 168 168 L -> F (in SCA34; dbSNP:rs587777598).
{ECO:0000269|PubMed:24566826}.
/FTId=VAR_072565.
VARIANT 267 267 I -> T (in dbSNP:rs148594713).
{ECO:0000269|PubMed:12592226}.
/FTId=VAR_017043.
VARIANT 299 299 M -> V (in dbSNP:rs3812153).
{ECO:0000269|PubMed:11138005,
ECO:0000269|PubMed:12592226}.
/FTId=VAR_012492.
CONFLICT 44 44 Q -> R (in Ref. 6; AAH38506).
{ECO:0000305}.
SEQUENCE 314 AA; 36829 MW; B2EBCE54D868E96E CRC64;
MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL SISTLYLLFV
WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG SYNAGYSYIC QSVDYSNNVH
EVRIAAALWW YFVSKGVEYL DTVFFILRKK NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ
AFFGAQLNSF IHVIMYSYYG LTAFGPWIQK YLWWKRYLTM LQLIQFHVTI GHTALSLYTD
CPFPKWMHWA LIAYAISFIF LFLNFYIRTY KEPKKPKAGK TAMNGISANG VSKSEKQLMI
ENGKKQKNGK AKGD


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EIAAB12844 3-keto acyl-CoA synthase ELOVL5,Elongation of very long chain fatty acids protein 5,ELOVL2,ELOVL5,Fatty acid elongase 1,hELO1,Homo sapiens,Human,PRO0530
EIAAB12841 3-keto acyl-CoA synthase Elovl4,Elongation of very long chain fatty acids protein 4,Elovl4,Mouse,Mus musculus
EIAAB12840 3-keto acyl-CoA synthase ELOVL4,Elongation of very long chain fatty acids protein 4,ELOVL4,Homo sapiens,Human
EIAAB12851 3-keto acyl-CoA synthase ELOVL7,Bos taurus,Bovine,Elongation of very long chain fatty acids protein 7,ELOVL7
EIAAB12852 3-keto acyl-CoA synthase Elovl7,Elongation of very long chain fatty acids protein 7,Elovl7,Mouse,Mus musculus
EIAAB12845 3-keto acyl-CoA synthase ELOVL5,Bos taurus,Bovine,Elongation of very long chain fatty acids protein 5,ELOVL5
EIAAB12843 3-keto acyl-CoA synthase Elovl5,Elongation of very long chain fatty acids protein 5,Elovl5,Mouse,Mus musculus
EIAAB12850 3-keto acyl-CoA synthase ELOVL7,Elongation of very long chain fatty acids protein 7,ELOVL7,Homo sapiens,Human
EIAAB12835 3-keto acyl-CoA synthase Elovl1,Elongation of very long chain fatty acids protein 1,Elovl1,Mouse,Mus musculus,Ssc1
EIAAB12836 3-keto acyl-CoA synthase Elovl2,Elongation of very long chain fatty acids protein 2,Elovl2,Mouse,Mus musculus,Ssc2
EIAAB12834 3-keto acyl-CoA synthase ELOVL1,CGI-88,Elongation of very long chain fatty acids protein 1,ELOVL1,Homo sapiens,Human,SSC1
EIAAB12837 3-keto acyl-CoA synthase ELOVL2,Elongation of very long chain fatty acids protein 2,ELOVL2,Homo sapiens,Human,SSC2
EIAAB12838 3-keto acyl-CoA synthase Elovl3,Cig30,CIN-2,Cold-inducible glycoprotein of 30 kDa,Elongation of very long chain fatty acids protein 3,Elovl3,Mouse,Mus musculus
EIAAB12839 3-keto acyl-CoA synthase ELOVL3,CIG30,Cold-inducible glycoprotein of 30 kDa,Elongation of very long chain fatty acids protein 3,ELOVL3,Homo sapiens,Human
ARP49667_P050 ELOVL5(ELOVL family member 5, elongation of long chain fatty acids) 50 µg
EIAAB12847 3-keto acyl-CoA synthase ELOVL6,Chicken,Elongation of very long chain fatty acids protein 6,ELOVL6,Gallus gallus,RCJMB04_16d24
ELP3 ELOVL7 Gene ELOVL family member 7, elongation of long chain fatty acids (yeast)
ELOVL7 ELOVL5 Gene ELOVL family member 5, elongation of long chain fatty acids (FEN1_Elo2, SUR4_Elo3-like, yeast)
ELP2 ELOVL6 Gene ELOVL family member 6, elongation of long chain fatty acids (FEN1_Elo2, SUR4_Elo3-like, yeast)
CSB-EL007624RA Rat ELOVL family member 6, elongation of long chain fatty acids (FEN1_Elo2, SUR4_Elo3-like, yeast) (ELOVL6) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL007623RA Rat ELOVL family member 5, elongation of long chain fatty acids (FEN1_Elo2, SUR4_Elo3-like, yeast) (ELOVL5) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

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