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O02858 (ACOD_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SCD
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length334 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Iron.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.

Domain

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

Sequence similarities

Belongs to the fatty acid desaturase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›334›334Acyl-CoA desaturase
PRO_0000185399

Regions

Topological domain‹1 – 60›60Cytoplasmic Potential
Transmembrane61 – 8222Helical; Potential
Topological domain83 – 919Lumenal Potential
Transmembrane92 – 10817Helical; Potential
Topological domain109 – 20597Cytoplasmic Potential
Transmembrane206 – 22419Helical; Potential
Topological domain225 – 23915Lumenal Potential
Transmembrane240 – 26223Helical; Potential
Topological domain263 – ›334›72Cytoplasmic Potential
Motif109 – 1146Histidine box-1
Motif146 – 1505Histidine box-2
Motif287 – 2915Histidine box-3

Amino acid modifications

Modified residue1921Phosphoserine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue3341

Sequences

Sequence LengthMass (Da)Tools
O02858 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 79183E3918469977

FASTA33438,482
        10         20         30         40         50         60 
SSYTTTTTIT APSSRVLQNG GGKSEKTPQY VEEDIRPEMK DDIYDPTYQD KEGPQGKLEY 

        70         80         90        100        110        120 
VWRNIILMSL LHLGALYGII LIPTCKIYTL LWAFAYYLLS AVGVTAGAHR LWSHRTYKAR 

       130        140        150        160        170        180 
LPLRVFLIIA NTMAFQNDVY EWARDHRAHH KFSETDADPH NSRRGFFFSH VGWLLVRKHP 

       190        200        210        220        230        240 
AVKEKGGLLN MSDLKAEKLV MFQRRYYKPG ILLMCFILPT IVPWYCWGEA FPQSLFVATF 

       250        260        270        280        290        300 
LRYAIVLNAT WLVNSAAHLY GYRPYDKTIS PRENILVSLG AVGEGFHNYH HTFPYDYSAS 

       310        320        330 
EYRWHINLTT FFIDCMAALG LAYDRKKVSK AAIL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z97186 mRNA. Translation: CAB10004.1.
UniGeneSsc.16159.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1398.
HOVERGENHBG003367.

Family and domain databases

InterProIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSPR00075. FACDDSATRASE.
PROSITEPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOD_PIG
AccessionPrimary (citable) accession number: O02858
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families