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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Capra hircus (Goat)
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

Fe cationBy similarity

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
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7171CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei72 – 9322HelicalSequence AnalysisAdd
BLAST
Topological domaini94 – 1029LumenalSequence Analysis
Transmembranei103 – 11917HelicalSequence AnalysisAdd
BLAST
Topological domaini120 – 21697CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei217 – 23519HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 25015LumenalSequence AnalysisAdd
BLAST
Transmembranei251 – 27323HelicalSequence AnalysisAdd
BLAST
Topological domaini274 – 35986CytoplasmicSequence 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
Chaini1 – 359359Acyl-CoA desaturasePRO_0000232709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Histidine box-1
Motifi157 – 1615Histidine box-2
Motifi298 – 3025Histidine 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

HOVERGENiHBG003367.

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: Complete.

Q95MI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHLLQEEI SSSYTTTTTI TAPPSKVLQN GGGKLEKTPL YLEEDIRPEM
60 70 80 90 100
RDDIYDPTYQ DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT
110 120 130 140 150
FLWVLFYYMM SALGITAGVH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV
160 170 180 190 200
FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVREKGATL
210 220 230 240 250
DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE TFQNSLFFAT
260 270 280 290 300
LLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY
310 320 330 340 350
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAALARMKR

TGEESCKSG
Length:359
Mass (Da):41,586
Last modified:December 1, 2001 - v1
Checksum:i052E5BE2B4463F88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF339909 mRNA. Translation: AAK61862.1.
AF422171
, AF422167, AF422166, AF422168, AF422170, AF422169 Genomic DNA. Translation: AAL29305.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF339909 mRNA. Translation: AAK61862.1.
AF422171
, AF422167, AF422166, AF422168, AF422170, AF422169 Genomic DNA. Translation: AAL29305.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003367.

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. "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].

Entry informationi

Entry nameiACOD_CAPHI
AccessioniPrimary (citable) accession number: Q95MI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: March 4, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.