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Reviewed, UniProtKB/Swiss-Prot O02858 (ACOD_PIG)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-CoA desaturase
    EC=1.14.19.1
Alternative name(s):
    Stearoyl-CoA desaturase
    Fatty acid desaturase
    Delta(9)-desaturase
Gene names
Name: SCD
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length334 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Transmembrane65 – 8521 Potential
Transmembrane87 – 10721 Potential
Transmembrane212 – 23221 Potential
Transmembrane304 – 32421 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
O02858-1 [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

Z97186 mRNA. Translation: CAB10004.1.
UniGeneSsc.16159

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENO02858.

Enzyme and pathway databases

BRENDA1.14.19.1. 249.

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.
ProDomPD002221. Desaturase. 1 hit.
PD001081. FA_desat_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents