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Q95MI7

- ACOD_CAPHI

UniProt

Q95MI7 - ACOD_CAPHI

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Protein

Acyl-CoA desaturase

Gene
SCD
Organism
Capra hircus (Goat)
Status
Reviewed - 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

Iron By 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 – 7171Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei72 – 9322Helical; Reviewed predictionAdd
BLAST
Topological domaini94 – 1029Lumenal Reviewed prediction
Transmembranei103 – 11917Helical; Reviewed predictionAdd
BLAST
Topological domaini120 – 21697Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei217 – 23519Helical; Reviewed predictionAdd
BLAST
Topological domaini236 – 25015Lumenal Reviewed predictionAdd
BLAST
Transmembranei251 – 27323Helical; Reviewed predictionAdd
BLAST
Topological domaini274 – 35986Cytoplasmic Reviewed predictionAdd
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 – 2031Phosphoserine By 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

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

MPAHLLQEEI SSSYTTTTTI TAPPSKVLQN GGGKLEKTPL YLEEDIRPEM    50
RDDIYDPTYQ DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT 100
FLWVLFYYMM SALGITAGVH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV 150
FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVREKGATL 200
DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE TFQNSLFFAT 250
LLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY 300
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAALARMKR 350
TGEESCKSG 359
Length:359
Mass (Da):41,586
Last modified:December 1, 2001 - v1
Checksum:i052E5BE2B4463F88
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF339909 mRNA. Translation: AAK61862.1 .
AF422171
, AF422167 , AF422166 , AF422168 , AF422170 , AF422169 Genomic DNA. Translation: AAL29305.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG003367.

Family and domain databases

InterProi IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view ]
Pfami PF00487. FA_desaturase. 1 hit.
[Graphical view ]
PRINTSi PR00075. FACDDSATRASE.
PROSITEi PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: February 19, 2014
This is version 57 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

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