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Q9TT94

- ACOD_BOVIN

UniProt

Q9TT94 - ACOD_BOVIN

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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Bos taurus (Bovine)
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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

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 Source: UniProtKB-KW
  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_0000185394Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

ExpressionAtlasiQ9TT94. baseline.

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.
InParanoidiQ9TT94.
KOiK00507.

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.

Q9TT94-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAHLLQEEI SSSYTTTTTI TAPPSRVLQN GGGKLEKTPL YLEEDIRPEM
60 70 80 90 100
RDDIYDPTYQ DKEGPKPKLE YVWRNIILMS LLHLGALYGI TLIPTCKIYT
110 120 130 140 150
YIWVLFYYLM GALGITAGAH RLWSHRTYKA RLPLRVFLII GNTMAFQNDV
160 170 180 190 200
FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVKEKGSTL
210 220 230 240 250
NLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWDE TFQNSLFFAT
260 270 280 290 300
LFRYALGLNV TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAAGEGFHNY
310 320 330 340 350
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAILARIKR

TGEESYKSG
Length:359
Mass (Da):41,705
Last modified:June 27, 2006 - v2
Checksum:iC7C9E9FA3A8FD205
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → M in AAF22305. (PubMed:10945276)Curated
Sequence conflicti293 – 2931A → V in AAF22305. (PubMed:10945276)Curated
Sequence conflicti293 – 2931A → V in AAL99940. 1 PublicationCurated
Sequence conflicti356 – 3561Y → H in AAF22305. (PubMed:10945276)Curated
Sequence conflicti359 – 3591G → S in AAF22305. (PubMed:10945276)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188710 mRNA. Translation: AAF22305.1.
AF481919
, AF481915, AF481916, AF481917, AF481918 Genomic DNA. Translation: AAL99940.1.
AY241932 Genomic DNA. Translation: AAO63569.1.
AY241933 mRNA. Translation: AAO63570.1.
BC112700 mRNA. Translation: AAI12701.1.
PIRiPC7092.
RefSeqiNP_776384.3. NM_173959.4.
UniGeneiBt.65021.

Genome annotation databases

GeneIDi280924.
KEGGibta:280924.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188710 mRNA. Translation: AAF22305.1 .
AF481919
, AF481915 , AF481916 , AF481917 , AF481918 Genomic DNA. Translation: AAL99940.1 .
AY241932 Genomic DNA. Translation: AAO63569.1 .
AY241933 mRNA. Translation: AAO63570.1 .
BC112700 mRNA. Translation: AAI12701.1 .
PIRi PC7092.
RefSeqi NP_776384.3. NM_173959.4.
UniGenei Bt.65021.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 280924.
KEGGi bta:280924.

Organism-specific databases

CTDi 6319.

Phylogenomic databases

HOVERGENi HBG003367.
InParanoidi Q9TT94.
KOi K00507.

Miscellaneous databases

NextBioi 20805045.

Gene expression databases

ExpressionAtlasi Q9TT94. baseline.

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

« Hide 'large scale' publications
  1. "Cloning and characterization of bovine stearoyl CoA desaturasel cDNA from adipose tissues."
    Chung M.I., Ha S.H., Jeong S., Bok J., Cho K., Baik M.G., Choi Y.J.
    Biosci. Biotechnol. Biochem. 64:1526-1530(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipose tissue.
  2. "Bovine stearoyl-CoA desaturase gene structure and large scale SNP analysis."
    Glimm D., Dong F., Kennelly J.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Genomic structure and expression of the bovine stearoyl-CoA desaturase gene."
    Medrano J.F., Islas-Trejo A.D., Johnson A.M., DePeters E.J.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiACOD_BOVIN
AccessioniPrimary (citable) accession number: Q9TT94
Secondary accession number(s): Q861R6, Q8SQ76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: November 26, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3