SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O02858

- ACOD_PIG

UniProt

O02858 - ACOD_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acyl-CoA desaturase
Gene
SCD
Organism
Sus scrofa (Pig)
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.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 60›60Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei61 – 8222Helical; Reviewed prediction
Add
BLAST
Topological domaini83 – 919Lumenal Reviewed prediction
Transmembranei92 – 10817Helical; Reviewed prediction
Add
BLAST
Topological domaini109 – 20597Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei206 – 22419Helical; Reviewed prediction
Add
BLAST
Topological domaini225 – 23915Lumenal Reviewed prediction
Add
BLAST
Transmembranei240 – 26223Helical; Reviewed prediction
Add
BLAST
Topological domaini263 – ›334›72Cytoplasmic Reviewed prediction
Add
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
Chaini‹1 – ›334›334Acyl-CoA desaturase
PRO_0000185399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 1146Histidine box-1
Motifi146 – 1505Histidine box-2
Motifi287 – 2915Histidine 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

eggNOGiCOG1398.
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: Fragment.

O02858-1 [UniParc]FASTAAdd to Basket

« Hide

SSYTTTTTIT APSSRVLQNG GGKSEKTPQY VEEDIRPEMK DDIYDPTYQD    50
KEGPQGKLEY VWRNIILMSL LHLGALYGII LIPTCKIYTL LWAFAYYLLS 100
AVGVTAGAHR LWSHRTYKAR LPLRVFLIIA NTMAFQNDVY EWARDHRAHH 150
KFSETDADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGLLN MSDLKAEKLV 200
MFQRRYYKPG ILLMCFILPT IVPWYCWGEA FPQSLFVATF LRYAIVLNAT 250
WLVNSAAHLY GYRPYDKTIS PRENILVSLG AVGEGFHNYH HTFPYDYSAS 300
EYRWHINLTT FFIDCMAALG LAYDRKKVSK AAIL 334
Length:334
Mass (Da):38,482
Last modified:July 1, 1997 - v1
Checksum:i79183E3918469977
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei334 – 3341

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97186 mRNA. Translation: CAB10004.1.
UniGeneiSsc.16159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97186 mRNA. Translation: CAB10004.1 .
UniGenei Ssc.16159.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1398.
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. Fumiere O.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiACOD_PIG
AccessioniPrimary (citable) accession number: O02858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 86 of the entry and version 1 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

Similar proteinsi