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Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)

 ELOV5_HUMAN             Reviewed;         299 AA.
Q9NYP7; B4DZJ2; F6SH78; Q59EL3; Q5TGH5; Q6NXE7; Q7L2S5; Q8NCG4;
Q9UI22;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 143.
RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:20937905};
AltName: Full=3-keto acyl-CoA synthase ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=Fatty acid elongase 1;
Short=hELO1;
AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
Name=ELOVL5 {ECO:0000255|HAMAP-Rule:MF_03205}; Synonyms=ELOVL2;
ORFNames=PRO0530;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
FUNCTION.
TISSUE=Liver;
PubMed=10970790; DOI=10.1042/bj3500765;
Leonard A.E., Bobik E.G., Dorado J., Kroeger P.E., Chuang L.-T.,
Thurmond J.M., Parker-Barnes J.M., Das T., Huang Y.-S., Mukerji P.;
"Cloning of a human cDNA encoding a novel enzyme involved in the
elongation of long-chain polyunsaturated fatty acids.";
Biochem. J. 350:765-770(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Suzuki T., Nitta A., Morita R., Sugimoto Y., Yamakawa K.;
"Homo sapiens mRNA for elongation of very long chain fatty acids
(FEN1/Elo2, SUR4/Elo3, yeast)-like 2 (ELOVL2).";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Eye, Leiomyosarcoma, and Skin;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-299 (ISOFORM 1).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-299 (ISOFORM 1).
TISSUE=Liver;
Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G.,
Zhang Y., Liu M., He F.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN SCA38, AND
VARIANTS SCA38 VAL-72 AND VAL-230.
PubMed=25065913; DOI=10.1016/j.ajhg.2014.07.001;
Di Gregorio E., Borroni B., Giorgio E., Lacerenza D., Ferrero M.,
Lo Buono N., Ragusa N., Mancini C., Gaussen M., Calcia A., Mitro N.,
Hoxha E., Mura I., Coviello D.A., Moon Y.A., Tesson C., Vaula G.,
Couarch P., Orsi L., Duregon E., Papotti M.G., Deleuze J.F.,
Imbert J., Costanzi C., Padovani A., Giunti P., Maillet-Vioud M.,
Durr A., Brice A., Tempia F., Funaro A., Boccone L., Caruso D.,
Stevanin G., Brusco A.;
"ELOVL5 mutations cause spinocerebellar ataxia 38.";
Am. J. Hum. Genet. 95:209-217(2014).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- 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 acts
specifically toward polyunsaturated acyl-CoA with the higher
activity toward C18:3(n-6) acyl-CoA. May participate in the
production of monounsaturated and of polyunsaturated VLCFAs of
different chain lengths that are involved in multiple biological
processes as precursors of membrane lipids and lipid mediators.
{ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:10970790,
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_03205, ECO:0000269|PubMed:20937905}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03205,
ECO:0000269|PubMed:20937905}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:20937905};
Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}.
Cell projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205,
ECO:0000269|PubMed:25065913}. Note=In Purkinje cells, the protein
localizes to the soma and proximal portion of the dendritic tree.
{ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:25065913}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NYP7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NYP7-2; Sequence=VSP_045918;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NYP7-3; Sequence=VSP_045917, VSP_045919;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the adrenal
gland and testis. Weakly expressed in prostate, lung and brain.
Expressed in the cerebellum. {ECO:0000269|PubMed:10970790,
ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25065913}.
-!- DISEASE: Spinocerebellar ataxia 38 (SCA38) [MIM:615957]: 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. SCA38
is an autosomal dominant form characterized by adult-onset of
slowly progressive gait ataxia accompanied by nystagmus. Brain MRI
shows cerebellar atrophy. {ECO:0000269|PubMed:25065913}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03205}.
-!- SEQUENCE CAUTION:
Sequence=AAF16688.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC11178.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF231981; AAF70631.1; -; mRNA.
EMBL; AF338241; AAM00193.1; -; mRNA.
EMBL; AL136939; CAB66873.1; -; mRNA.
EMBL; AK074889; BAC11270.1; -; mRNA.
EMBL; AK302948; BAG64104.1; -; mRNA.
EMBL; AB209798; BAD93035.1; -; mRNA.
EMBL; AL034374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04419.1; -; Genomic_DNA.
EMBL; BC017270; AAH17270.2; -; mRNA.
EMBL; BC067123; AAH67123.2; -; mRNA.
EMBL; BC074503; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK074748; BAC11178.1; ALT_INIT; mRNA.
EMBL; AF111849; AAF16688.1; ALT_INIT; mRNA.
CCDS; CCDS4951.1; -. [Q9NYP7-1]
CCDS; CCDS56433.1; -. [Q9NYP7-2]
CCDS; CCDS56434.1; -. [Q9NYP7-3]
RefSeq; NP_001229757.1; NM_001242828.1. [Q9NYP7-2]
RefSeq; NP_001229759.1; NM_001242830.1.
RefSeq; NP_001229760.1; NM_001242831.1. [Q9NYP7-3]
RefSeq; NP_001288785.1; NM_001301856.1. [Q9NYP7-1]
RefSeq; NP_068586.1; NM_021814.4. [Q9NYP7-1]
UniGene; Hs.520189; -.
ProteinModelPortal; Q9NYP7; -.
SMR; Q9NYP7; -.
BioGrid; 121914; 13.
IntAct; Q9NYP7; 12.
BindingDB; Q9NYP7; -.
ChEMBL; CHEMBL5937; -.
SwissLipids; SLP:000000253; -.
iPTMnet; Q9NYP7; -.
PhosphoSitePlus; Q9NYP7; -.
SwissPalm; Q9NYP7; -.
BioMuta; ELOVL5; -.
DMDM; 74753072; -.
EPD; Q9NYP7; -.
MaxQB; Q9NYP7; -.
PeptideAtlas; Q9NYP7; -.
PRIDE; Q9NYP7; -.
ProteomicsDB; 83259; -.
DNASU; 60481; -.
Ensembl; ENST00000304434; ENSP00000306640; ENSG00000012660. [Q9NYP7-1]
Ensembl; ENST00000370913; ENSP00000359951; ENSG00000012660. [Q9NYP7-3]
Ensembl; ENST00000370918; ENSP00000359956; ENSG00000012660. [Q9NYP7-2]
GeneID; 60481; -.
KEGG; hsa:60481; -.
UCSC; uc003pbr.3; human. [Q9NYP7-1]
CTD; 60481; -.
DisGeNET; 60481; -.
EuPathDB; HostDB:ENSG00000012660.13; -.
GeneCards; ELOVL5; -.
HGNC; HGNC:21308; ELOVL5.
HPA; CAB017042; -.
HPA; HPA047752; -.
HPA; HPA054197; -.
MalaCards; ELOVL5; -.
MIM; 611805; gene.
MIM; 615957; phenotype.
neXtProt; NX_Q9NYP7; -.
OpenTargets; ENSG00000012660; -.
PharmGKB; PA128394703; -.
GeneTree; ENSGT00760000119122; -.
HOGENOM; HOG000139716; -.
HOVERGEN; HBG051468; -.
InParanoid; Q9NYP7; -.
KO; K10244; -.
OMA; NVKPRKQ; -.
OrthoDB; EOG091G0N2V; -.
PhylomeDB; Q9NYP7; -.
TreeFam; TF323454; -.
BioCyc; MetaCyc:ENSG00000012660-MONOMER; -.
BRENDA; 2.3.1.119; 2681.
Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
UniPathway; UPA00658; -.
ChiTaRS; ELOVL5; human.
GeneWiki; ELOVL5; -.
GenomeRNAi; 60481; -.
PRO; PR:Q9NYP7; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000012660; Expressed in 235 organ(s), highest expression level in adipose tissue.
CleanEx; HS_ELOVL2; -.
CleanEx; HS_ELOVL5; -.
ExpressionAtlas; Q9NYP7; baseline and differential.
Genevisible; Q9NYP7; HS.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0097447; C:dendritic tree; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; 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; IDA:UniProtKB.
GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IDA:UniProtKB.
GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IDA:UniProtKB.
GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB.
HAMAP; MF_03205; VLCF_elongase_5; 1.
InterPro; IPR002076; ELO_fam.
InterPro; IPR033677; ELOVL5.
PANTHER; PTHR11157; PTHR11157; 1.
PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
Pfam; PF01151; ELO; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell projection; Complete proteome;
Disease mutation; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
Neurodegeneration; Phosphoprotein; Reference proteome;
Spinocerebellar ataxia; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 299 Elongation of very long chain fatty acids
protein 5.
/FTId=PRO_0000282838.
TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 64 84 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 112 132 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 139 158 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 168 187 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 205 225 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
TRANSMEM 226 246 Helical. {ECO:0000255|HAMAP-
Rule:MF_03205}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:25944712}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 20 88 DTRVKGWFLLDNYIPTFICSVIYLLIVWLGPKYMRNKQPFS
CRGILVVYNLGLTLLSLYMFCELVTGVW -> GISSSVLRM
GPPLHTVVGWLQQLQAAHSEEEEKMFHLCGFKHKEVVSQSS
LPAVIPQNSLATIASHAPA (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045917.
VAR_SEQ 82 82 E -> ESKREQPRRSACASRTDPSTQQQLPENR (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045918.
VAR_SEQ 89 299 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045919.
VARIANT 72 72 L -> V (in SCA38; dbSNP:rs587777671).
{ECO:0000269|PubMed:25065913}.
/FTId=VAR_072361.
VARIANT 230 230 G -> V (in SCA38; dbSNP:rs587777670).
{ECO:0000269|PubMed:25065913}.
/FTId=VAR_072362.
CONFLICT 59 59 F -> L (in Ref. 4; BAG64104).
{ECO:0000305}.
CONFLICT 167 262 YFGATLNSFIHVLMYSYYGLSSVPSMRPYLWWKKYITQGQL
LQFVLTIIQTSCGVIWPCTFPLGWLYFQIGYMISLIALFTN
FYIQTYNKKGASRR -> SVCADNHPDQLRGHLAVHIPSWL
VVFPDWIHDFPDCSLHKLLHSDLQQERGLPKERPPEGPPEW
VHGCCEWTHQQLFTPGKQCEAKEAAEGLKSKN (in Ref.
4; BAD93035). {ECO:0000305}.
CONFLICT 204 206 QGQ -> EFH (in Ref. 9; BAC11178).
{ECO:0000305}.
CONFLICT 227 227 F -> S (in Ref. 9; BAC11178).
{ECO:0000305}.
SEQUENCE 299 AA; 35293 MW; AE5150AA3432E984 CRC64;
MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP KYMRNKQPFS
CRGILVVYNL GLTLLSLYMF CELVTGVWEG KYNFFCQGTR TAGESDMKII RVLWWYYFSK
LIEFMDTFFF ILRKNNHQIT VLHVYHHASM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
YSYYGLSSVP SMRPYLWWKK YITQGQLLQF VLTIIQTSCG VIWPCTFPLG WLYFQIGYMI
SLIALFTNFY IQTYNKKGAS RRKDHLKDHQ NGSMAAVNGH TNSFSPLENN VKPRKLRKD


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