Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q95MI7 (ACOD_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
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 By similarity.

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

Chain1 – 359359Acyl-CoA desaturase
PRO_0000232709

Regions

Topological domain1 – 7171Cytoplasmic Potential
Transmembrane72 – 9322Helical; Potential
Topological domain94 – 1029Lumenal Potential
Transmembrane103 – 11917Helical; Potential
Topological domain120 – 21697Cytoplasmic Potential
Transmembrane217 – 23519Helical; Potential
Topological domain236 – 25015Lumenal Potential
Transmembrane251 – 27323Helical; Potential
Topological domain274 – 35986Cytoplasmic Potential
Motif120 – 1256Histidine box-1
Motif157 – 1615Histidine box-2
Motif298 – 3025Histidine box-3

Amino acid modifications

Modified residue2031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95MI7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 052E5BE2B4463F88

FASTA35941,586
        10         20         30         40         50         60 
MPAHLLQEEI SSSYTTTTTI TAPPSKVLQN GGGKLEKTPL YLEEDIRPEM RDDIYDPTYQ 

        70         80         90        100        110        120 
DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT FLWVLFYYMM SALGITAGVH 

       130        140        150        160        170        180 
RLWSHRTYKA RLPLRVFLII ANTMAFQNDV FEWSRDHRAH HKFSETDADP HNSRRGFFFS 

       190        200        210        220        230        240 
HVGWLLVRKH PAVREKGATL DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE 

       250        260        270        280        290        300 
TFQNSLFFAT LLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY 

       310        320        330        340        350 
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAALARMKR TGEESCKSG 

« Hide

References

[1]"Partial nucleotide sequence of the goat stearoyl coenzyme A desaturase cDNA and gene structure."
Yahyaoui M.H., Sanchez A., Folch J.M.
J. Anim. Sci. 80:866-867(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF339909 mRNA. Translation: AAK61862.1.
AF422171 expand/collapse EMBL AC list , AF422167, AF422166, AF422168, AF422170, AF422169 Genomic DNA. Translation: AAL29305.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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_CAPHI
AccessionPrimary (citable) accession number: Q95MI7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 57 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