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UniProtKB - Q8ISS3 (ACO11_CHORO)
Protein
Acyl-CoA Delta(11) desaturase
Gene
N/A
Organism
Choristoneura rosaceana (Oblique banded leafroller)
Status
Functioni
Catalyzes the formation of Delta(11) fatty acyl precursors in the pheromone gland, with a preference for myristic acid.
1 PublicationCatalytic activityi
- an 11,12-saturated fatty acyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H+ + O2 = an (11Z)-Δ11-fatty acyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O1 PublicationEC:1.14.19.51 Publication
Cofactori
Fe cationBy similarity
GO - Molecular functioni
- acyl-CoA delta11-desaturase activity Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- myristoyl-CoA 11-(Z) desaturase activity Source: UniProtKB-EC
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB-KW
- fatty acid metabolic process Source: UniProtKB
- pheromone biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.14.19.24, 7754 1.14.19.5, 7754 |
Names & Taxonomyi
Protein namesi | Recommended name: Acyl-CoA Delta(11) desaturase (EC:1.14.19.51 Publication)Alternative name(s): Acyl-CoA Delta-11 desaturase Short name: Delta(11)-desaturase Acyl-CoA Z/E11 desaturase |
Organismi | Choristoneura rosaceana (Oblique banded leafroller) |
Taxonomic identifieri | 27543 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Tortricoidea › Tortricidae › Tortricinae › Choristoneura |
Subcellular locationi
Other locations
- Membrane By similarity; Multi-pass membrane protein By similarity
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 39 – 59 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 64 – 84 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 98 – 118 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 182 – 202 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 213 – 235 | HelicalSequence analysisAdd BLAST | 23 |
Keywords - Cellular componenti
MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000418990 | 1 – 335 | Acyl-CoA Delta(11) desaturaseAdd BLAST | 335 |
Expressioni
Tissue specificityi
Detected in pheromone gland.1 Publication
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 312 – 335 | DisorderedSequence analysisAdd BLAST | 24 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 84 – 89 | Histidine box-1 | 6 | |
Motifi | 121 – 125 | Histidine box-2 | 5 | |
Motifi | 261 – 265 | Histidine box-3 | 5 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 320 – 335 | Polar residuesSequence analysisAdd BLAST | 16 |
Domaini
The histidine box domains may contain the active site and/or be involved in metal ion binding.By similarity
Sequence similaritiesi
Belongs to the fatty acid desaturase type 1 family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
i Sequence
Sequence statusi: Complete.
Q8ISS3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAPNVEDMES DLPESEEKLE KLVAPQAAPR KYQIIYTNLL TFGYWHIAGL
60 70 80 90 100
YGLYLCFTSA KWQTIILALI LNEMAILGIT AGAHRLWAHR SYKATVPLQI
110 120 130 140 150
ILIIFNSLSF QNSAIHWIRD HRMHHKYSDT DGDPHNASRG FFYSHVGWLL
160 170 180 190 200
VKKHPEVKKR AKTIDMSDIY SNPILRFQKK YAIPFIGMIC FVLPTIIPMY
210 220 230 240 250
FWGETLSNAW HITMLRYVFS LNSIFLVNSA AHLYGYRPYD KNILPAENKM
260 270 280 290 300
TFIACLGENF HNYHHVFPWD YRASELGNIG MNWTAKFIDF FAWIGWAYDL
310 320 330
KTASDENIKS RMKRTGDGTD VSGQKYSCES SEVLQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF545481 mRNA Translation: AAN41250.1 FJ999625 Genomic DNA Translation: ADC53485.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF545481 mRNA Translation: AAN41250.1 FJ999625 Genomic DNA Translation: ADC53485.1 |
3D structure databases
SMRi | Q8ISS3 |
ModBasei | Search... |
Enzyme and pathway databases
BRENDAi | 1.14.19.24, 7754 1.14.19.5, 7754 |
Family and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ACO11_CHORO | |
Accessioni | Q8ISS3Primary (citable) accession number: Q8ISS3 Secondary accession number(s): D8L7A5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 5, 2012 |
Last sequence update: | March 1, 2003 | |
Last modified: | February 23, 2022 | |
This is version 59 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |