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Protein

Fatty acid desaturase 2

Gene

fads2

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Fatty acid desaturase with both Delta5 and Delta6 activities. Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3).By similarity

Catalytic activityi

Linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O.By similarity
Alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O.By similarity

Pathwayi: polyunsaturated fatty acid biosynthesis

This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway polyunsaturated fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

  • liver development Source: ZFIN
  • unsaturated fatty acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Enzyme and pathway databases

BRENDAi1.14.19.3. 928.
UniPathwayiUPA00658.

Chemistry

SwissLipidsiSLP:000000464.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid desaturase 2 (EC:1.14.19.3)
Alternative name(s):
Acyl-CoA 6-desaturase
Delta(5)/Delta(6) fatty acid desaturase
Short name:
D5D/D6D fatty acid desaturase
Short name:
Delta-5/Delta-6 fatty acid desaturase
Gene namesi
Name:fads2
Synonyms:fadsd6
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-011212-1. fads2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 130130CytoplasmicSequence analysisAdd
BLAST
Transmembranei131 – 15121HelicalSequence analysisAdd
BLAST
Topological domaini152 – 1576LumenalSequence analysis
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 26486CytoplasmicSequence analysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence analysisAdd
BLAST
Topological domaini286 – 30520LumenalSequence analysisAdd
BLAST
Transmembranei306 – 32621HelicalSequence analysisAdd
BLAST
Topological domaini327 – 444118CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Fatty acid desaturase 2PRO_0000185408Add
BLAST

Proteomic databases

PaxDbiQ9DEX7.
PRIDEiQ9DEX7.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000022396.

Structurei

3D structure databases

ProteinModelPortaliQ9DEX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9578Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1845Histidine box-1
Motifi217 – 2215Histidine box-2
Motifi382 – 3865Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ9DEX7.
KOiK10226.
PhylomeDBiQ9DEX7.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DEX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGGGQQTDR ITDTNGRFSS YTWEEVQKHT KHGDQWVVVE RKVYNVSQWV
60 70 80 90 100
KRHPGGLRIL GHYAGEDATE AFTAFHPNLQ LVRKYLKPLL IGELEASEPS
110 120 130 140 150
QDRQKNAALV EDFRALRERL EAEGCFKTQP LFFALHLGHI LLLEAIAFMM
160 170 180 190 200
VWYFGTGWIN TLIVAVILAT AQSQAGWLQH DFGHLSVFKT SGMNHLVHKF
210 220 230 240 250
VIGHLKGASA GWWNHRHFQH HAKPNIFKKD PDVNMLNAFV VGNVQPVEYG
260 270 280 290 300
VKKIKHLPYN HQHKYFFFIG PPLLIPVYFQ FQIFHNMISH GMWVDLLWCI
310 320 330 340 350
SYYVRYFLCY TQFYGVFWAI ILFNFVRFME SHWFVWVTQM SHIPMNIDYE
360 370 380 390 400
KNQDWLSMQL VATCNIEQSA FNDWFSGHLN FQIEHHLFPT VPRHNYWRAA
410 420 430 440
PRVRALCEKY GVKYQEKTLY GAFADIIRSL EKSGELWLDA YLNK
Length:444
Mass (Da):52,032
Last modified:March 1, 2001 - v1
Checksum:i6AA25A1DC1DC0F65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261V → M in AAH49438 (Ref. 2) Curated
Sequence conflicti82 – 821V → M in AAH49438 (Ref. 2) Curated
Sequence conflicti149 – 1491M → V in AAH49438 (Ref. 2) Curated
Sequence conflicti342 – 3421H → R in AAH49438 (Ref. 2) Curated
Sequence conflicti351 – 3511K → Q in AAH49438 (Ref. 2) Curated
Sequence conflicti391 – 3911V → M in AAH49438 (Ref. 2) Curated
Sequence conflicti405 – 4051A → S in AAH49438 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309556 mRNA. Translation: AAG25710.1.
BC049438 mRNA. Translation: AAH49438.1.
RefSeqiNP_571720.2. NM_131645.2.
UniGeneiDr.75661.

Genome annotation databases

GeneIDi140615.
KEGGidre:140615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309556 mRNA. Translation: AAG25710.1.
BC049438 mRNA. Translation: AAH49438.1.
RefSeqiNP_571720.2. NM_131645.2.
UniGeneiDr.75661.

3D structure databases

ProteinModelPortaliQ9DEX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000022396.

Chemistry

SwissLipidsiSLP:000000464.

Proteomic databases

PaxDbiQ9DEX7.
PRIDEiQ9DEX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi140615.
KEGGidre:140615.

Organism-specific databases

CTDi9415.
ZFINiZDB-GENE-011212-1. fads2.

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ9DEX7.
KOiK10226.
PhylomeDBiQ9DEX7.

Enzyme and pathway databases

UniPathwayiUPA00658.
BRENDAi1.14.19.3. 928.

Miscellaneous databases

NextBioi20797026.
PROiQ9DEX7.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiFADS2_DANRE
AccessioniPrimary (citable) accession number: Q9DEX7
Secondary accession number(s): Q7ZWF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 106 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.