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Protein

Elongation of very long chain fatty acids protein 6

Gene

ELOVL6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. 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.UniRule annotation1 Publication

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation1 Publication
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

BioCyciMetaCyc:HS10142-MONOMER.
BRENDAi2.3.1.119. 2681.
2.3.1.16. 2681.
ReactomeiR-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000254.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 6UniRule annotationCurated (EC:2.3.1.199UniRule annotation1 Publication)
Alternative name(s):
3-keto acyl-CoA synthase ELOVL6UniRule annotation
ELOVL fatty acid elongase 6UniRule annotation
Short name:
ELOVL FA elongase 6UniRule annotation
Fatty acid elongase 2
Short name:
hELO2
Fatty acyl-CoA elongase
Long-chain fatty-acyl elongase
Very long chain 3-ketoacyl-CoA synthase 6UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 6UniRule annotation
Gene namesi
Name:ELOVL6UniRule annotation
Synonyms:FACE, LCE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:15829. ELOVL6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5118HelicalUniRule annotationAdd
BLAST
Transmembranei70 – 9021HelicalUniRule annotationAdd
BLAST
Transmembranei111 – 13121HelicalUniRule annotationAdd
BLAST
Transmembranei136 – 15621HelicalUniRule annotationAdd
BLAST
Transmembranei159 – 17921HelicalUniRule annotationAdd
BLAST
Transmembranei197 – 21721HelicalUniRule annotationAdd
BLAST
Transmembranei232 – 25221HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134939058.

Chemistry

ChEMBLiCHEMBL5704.

Polymorphism and mutation databases

BioMutaiELOVL6.
DMDMi74733585.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265Elongation of very long chain fatty acids protein 6PRO_0000282845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi2 – 21N-linked (GlcNAc...)UniRule annotation

Post-translational modificationi

N-Glycosylated.UniRule annotation1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9H5J4.
MaxQBiQ9H5J4.
PaxDbiQ9H5J4.
PeptideAtlasiQ9H5J4.
PRIDEiQ9H5J4.

PTM databases

iPTMnetiQ9H5J4.
PhosphoSiteiQ9H5J4.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9H5J4.
CleanExiHS_ELOVL6.
ExpressionAtlasiQ9H5J4. baseline and differential.
GenevisibleiQ9H5J4. HS.

Organism-specific databases

HPAiHPA042355.

Interactioni

Protein-protein interaction databases

BioGridi122522. 1 interaction.
STRINGi9606.ENSP00000304736.

Chemistry

BindingDBiQ9H5J4.

Structurei

3D structure databases

ProteinModelPortaliQ9H5J4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELO family. ELOVL6 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3072. Eukaryota.
ENOG410Z3FZ. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038943.
HOVERGENiHBG099423.
InParanoidiQ9H5J4.
KOiK10203.
OMAiHGQCHSH.
OrthoDBiEOG7MKW6F.
PhylomeDBiQ9H5J4.
TreeFamiTF106467.

Family and domain databases

HAMAPiMF_03206. VLCF_elongase_6.
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.

Q9H5J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL
60 70 80 90 100
MNKRAKFELR KPLVLWSLTL AVFSIFGALR TGAYMVYILM TKGLKQSVCD
110 120 130 140 150
QGFYNGPVSK FWAYAFVLSK APELGDTIFI ILRKQKLIFL HWYHHITVLL
160 170 180 190 200
YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY YALRAAGFRV SRKFAMFITL
210 220 230 240 250
SQITQMLMGC VVNYLVFCWM QHDQCHSHFQ NIFWSSLMYL SYLVLFCHFF
260
FEAYIGKMRK TTKAE
Length:265
Mass (Da):31,376
Last modified:March 1, 2001 - v1
Checksum:i01234E0EEF6CE341
GO

Sequence cautioni

The sequence BAC11225.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112EY → KN in BAC11225 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074813 mRNA. Translation: BAC11225.1. Different initiation.
AK027031 mRNA. Translation: BAB15632.1.
AC004050 Genomic DNA. No translation available.
AC093770 Genomic DNA. Translation: AAY40928.1.
BC001305 mRNA. Translation: AAH01305.1.
CCDSiCCDS3690.1.
RefSeqiNP_001124193.1. NM_001130721.1.
NP_076995.1. NM_024090.2.
XP_011530535.1. XM_011532233.1.
XP_011530536.1. XM_011532234.1.
UniGeneiHs.412939.
Hs.652828.

Genome annotation databases

EnsembliENST00000302274; ENSP00000304736; ENSG00000170522.
ENST00000394607; ENSP00000378105; ENSG00000170522.
GeneIDi79071.
KEGGihsa:79071.
UCSCiuc003hzz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074813 mRNA. Translation: BAC11225.1. Different initiation.
AK027031 mRNA. Translation: BAB15632.1.
AC004050 Genomic DNA. No translation available.
AC093770 Genomic DNA. Translation: AAY40928.1.
BC001305 mRNA. Translation: AAH01305.1.
CCDSiCCDS3690.1.
RefSeqiNP_001124193.1. NM_001130721.1.
NP_076995.1. NM_024090.2.
XP_011530535.1. XM_011532233.1.
XP_011530536.1. XM_011532234.1.
UniGeneiHs.412939.
Hs.652828.

3D structure databases

ProteinModelPortaliQ9H5J4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122522. 1 interaction.
STRINGi9606.ENSP00000304736.

Chemistry

BindingDBiQ9H5J4.
ChEMBLiCHEMBL5704.
SwissLipidsiSLP:000000254.

PTM databases

iPTMnetiQ9H5J4.
PhosphoSiteiQ9H5J4.

Polymorphism and mutation databases

BioMutaiELOVL6.
DMDMi74733585.

Proteomic databases

EPDiQ9H5J4.
MaxQBiQ9H5J4.
PaxDbiQ9H5J4.
PeptideAtlasiQ9H5J4.
PRIDEiQ9H5J4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302274; ENSP00000304736; ENSG00000170522.
ENST00000394607; ENSP00000378105; ENSG00000170522.
GeneIDi79071.
KEGGihsa:79071.
UCSCiuc003hzz.4. human.

Organism-specific databases

CTDi79071.
GeneCardsiELOVL6.
HGNCiHGNC:15829. ELOVL6.
HPAiHPA042355.
MIMi611546. gene.
neXtProtiNX_Q9H5J4.
PharmGKBiPA134939058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3072. Eukaryota.
ENOG410Z3FZ. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038943.
HOVERGENiHBG099423.
InParanoidiQ9H5J4.
KOiK10203.
OMAiHGQCHSH.
OrthoDBiEOG7MKW6F.
PhylomeDBiQ9H5J4.
TreeFamiTF106467.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:HS10142-MONOMER.
BRENDAi2.3.1.119. 2681.
2.3.1.16. 2681.
ReactomeiR-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

GenomeRNAii79071.
PROiQ9H5J4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H5J4.
CleanExiHS_ELOVL6.
ExpressionAtlasiQ9H5J4. baseline and differential.
GenevisibleiQ9H5J4. HS.

Family and domain databases

HAMAPiMF_03206. VLCF_elongase_6.
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. "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].
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Placenta.
  4. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiELOV6_HUMAN
AccessioniPrimary (citable) accession number: Q9H5J4
Secondary accession number(s): Q4W5L0, Q8NCD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 109 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.