Reviewed, UniProtKB/Swiss-Prot Q95MI7 (ACOD_CAPHI)

Names and origin

Protein names

Recommended 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

Organism

Capra hircus (Goat)

Taxonomic identifier

9925 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Capra

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Iron
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW stearoyl-CoA 9-desaturase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Acyl-CoA desaturase		PRO_0000232709
Regions
	Transmembrane	76 – 96	21	Potential
	Transmembrane	98 – 118	21	Potential
	Transmembrane	223 – 243	21	Potential
	Transmembrane	315 – 335	21	Potential
	Motif	120 – 125	6	Histidine box-1
	Motif	157 – 161	5	Histidine box-2
	Motif	298 – 302	5	Histidine box-3
Amino acid modifications
	Modified residue	199	1	Phosphothreonine By similarity
	Modified residue	203	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q95MI7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 052E5BE2B4463F88	FASTA	359	41,586
	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

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: 11890426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF339909 mRNA. Translation: AAK61862.1. AF422171 , AF422167, AF422166, AF422168, AF422170, AF422169 Genomic DNA. Translation: AAL29305.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q95MI7.
Enzyme and pathway databases
BRENDA	1.14.19.1. 1312.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
ProDom	PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACOD_CAPHI

Accession

Primary (citable) accession number: Q95MI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)