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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.By similarity

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

Cofactori

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase
Gene namesi
Name:SCD
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 60›60CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei61 – 8222HelicalSequence AnalysisAdd
BLAST
Topological domaini83 – 919LumenalSequence Analysis
Transmembranei92 – 10817HelicalSequence AnalysisAdd
BLAST
Topological domaini109 – 20597CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei206 – 22419HelicalSequence AnalysisAdd
BLAST
Topological domaini225 – 23915LumenalSequence AnalysisAdd
BLAST
Transmembranei240 – 26223HelicalSequence AnalysisAdd
BLAST
Topological domaini263 – ›334›72CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›334›334Acyl-CoA desaturasePRO_0000185399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 1146Histidine box-1
Motifi146 – 1505Histidine box-2
Motifi287 – 2915Histidine box-3

Domaini

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

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1398.
HOVERGENiHBG003367.
InParanoidiO02858.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O02858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SSYTTTTTIT APSSRVLQNG GGKSEKTPQY VEEDIRPEMK DDIYDPTYQD
60 70 80 90 100
KEGPQGKLEY VWRNIILMSL LHLGALYGII LIPTCKIYTL LWAFAYYLLS
110 120 130 140 150
AVGVTAGAHR LWSHRTYKAR LPLRVFLIIA NTMAFQNDVY EWARDHRAHH
160 170 180 190 200
KFSETDADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGLLN MSDLKAEKLV
210 220 230 240 250
MFQRRYYKPG ILLMCFILPT IVPWYCWGEA FPQSLFVATF LRYAIVLNAT
260 270 280 290 300
WLVNSAAHLY GYRPYDKTIS PRENILVSLG AVGEGFHNYH HTFPYDYSAS
310 320 330
EYRWHINLTT FFIDCMAALG LAYDRKKVSK AAIL
Length:334
Mass (Da):38,482
Last modified:July 1, 1997 - v1
Checksum:i79183E3918469977
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei334 – 3341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97186 mRNA. Translation: CAB10004.1.
UniGeneiSsc.16159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97186 mRNA. Translation: CAB10004.1.
UniGeneiSsc.16159.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1398.
HOVERGENiHBG003367.
InParanoidiO02858.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Fumiere O.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiACOD_PIG
AccessioniPrimary (citable) accession number: O02858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 91 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.