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Protein

Elongation of very long chain fatty acids protein 7

Gene

Elovl7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate to the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.UniRule annotation

Catalytic activityi

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

Pathwayi: fatty acid biosynthesis

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

ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 7UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
Alternative name(s):
3-keto acyl-CoA synthase Elovl7UniRule annotation
ELOVL fatty acid elongase 7UniRule annotation
Short name:
ELOVL FA elongase 7UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 7UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 7UniRule annotation
Gene namesi
Name:Elovl7UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1921809. Elovl7.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei28 – 4821HelicalUniRule annotationAdd
BLAST
Transmembranei73 – 9321HelicalUniRule annotationAdd
BLAST
Transmembranei116 – 13621HelicalUniRule annotationAdd
BLAST
Transmembranei143 – 16220HelicalUniRule annotationAdd
BLAST
Transmembranei172 – 19423HelicalUniRule annotationAdd
BLAST
Transmembranei207 – 22721HelicalUniRule annotationAdd
BLAST
Transmembranei237 – 25721HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Elongation of very long chain fatty acids protein 7PRO_0000311989Add
BLAST

Proteomic databases

MaxQBiQ9D2Y9.
PaxDbiQ9D2Y9.
PRIDEiQ9D2Y9.

PTM databases

PhosphoSiteiQ9D2Y9.

Expressioni

Gene expression databases

BgeeiQ9D2Y9.
GenevisibleiQ9D2Y9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022207.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi277 – 2815Di-lysine motifUniRule annotation

Domaini

The C-terminal di-lysine motif may confer endoplasmic reticulum localization.UniRule annotation

Sequence similaritiesi

Belongs to the ELO family. ELOVL7 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9D2Y9.
KOiK10250.
OMAiIFFMEDC.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9D2Y9.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03207. VLCF_elongase_7.
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.

Q9D2Y9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSDLTSRT VRFYDNWIKD ADPRVEDYLL MSSPLPQTII LGLYVYFVTS
60 70 80 90 100
LGPKLMENRK PFELKKAMIT YNFFIVLFSV YMCYEFVMSG WGTGYSFRCD
110 120 130 140 150
IVDYSQSPRA MRMVHTCWLY YFSKFIELLD TIFFVLRKKN SQVTFLHVFH
160 170 180 190 200
HTIMPWTWWF GVKFAAGGLG TFHAFLNTAV HVVMYSYYGL CAMGPAYQKY
210 220 230 240 250
LWWKKHLTSL QLVQFVLVTI HIGQIFFMED CNYQYPVFLY IIMSYGCIFL
260 270 280
LLFLHFWYRA YTKGQRLPKT LENGNCKSKR H
Length:281
Mass (Da):33,479
Last modified:June 1, 2001 - v1
Checksum:i025B3239F29BCB90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251V → F in BAC29727 (PubMed:16141072).Curated
Sequence conflicti249 – 2491F → S in BAC33552 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018616 mRNA. Translation: BAB31310.1.
AK037162 mRNA. Translation: BAC29727.1.
AK049118 mRNA. Translation: BAC33552.1.
AK137668 mRNA. Translation: BAE23454.1.
BC005602 mRNA. Translation: AAH05602.1.
CCDSiCCDS36779.1.
RefSeqiNP_083277.3. NM_029001.5.
UniGeneiMm.286127.

Genome annotation databases

EnsembliENSMUST00000022207; ENSMUSP00000022207; ENSMUSG00000021696.
GeneIDi74559.
KEGGimmu:74559.
UCSCiuc007rva.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018616 mRNA. Translation: BAB31310.1.
AK037162 mRNA. Translation: BAC29727.1.
AK049118 mRNA. Translation: BAC33552.1.
AK137668 mRNA. Translation: BAE23454.1.
BC005602 mRNA. Translation: AAH05602.1.
CCDSiCCDS36779.1.
RefSeqiNP_083277.3. NM_029001.5.
UniGeneiMm.286127.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022207.

PTM databases

PhosphoSiteiQ9D2Y9.

Proteomic databases

MaxQBiQ9D2Y9.
PaxDbiQ9D2Y9.
PRIDEiQ9D2Y9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022207; ENSMUSP00000022207; ENSMUSG00000021696.
GeneIDi74559.
KEGGimmu:74559.
UCSCiuc007rva.2. mouse.

Organism-specific databases

CTDi79993.
MGIiMGI:1921809. Elovl7.

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9D2Y9.
KOiK10250.
OMAiIFFMEDC.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9D2Y9.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiQ9D2Y9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D2Y9.
GenevisibleiQ9D2Y9. MM.

Family and domain databases

HAMAPiMF_03207. VLCF_elongase_7.
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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum, Skin and Vagina.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiELOV7_MOUSE
AccessioniPrimary (citable) accession number: Q9D2Y9
Secondary accession number(s): Q8BX38, Q8BYY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.