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Q6P7B9

- ACOD2_RAT

UniProt

Q6P7B9 - ACOD2_RAT

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Protein

Acyl-CoA desaturase 2

Gene

Scd2

Organism
Rattus norvegicus (Rat)
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: RGD

GO - Biological processi

  1. fatty acid biosynthetic process Source: RGD
  2. myelination Source: RGD
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 2 (EC:1.14.19.1)
Alternative name(s):
Delta(9)-desaturase 2
Short name:
Delta-9 desaturase 2
Fatty acid desaturase 2
Stearoyl-CoA desaturase 2
Gene namesi
Name:Scd2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621177. Scd2.

Subcellular locationi

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 – 358358Acyl-CoA desaturase 2PRO_0000185401Add
BLAST

Proteomic databases

PaxDbiQ6P7B9.
PRIDEiQ6P7B9.

PTM databases

PhosphoSiteiQ6P7B9.

Expressioni

Gene expression databases

GenevestigatoriQ6P7B9.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018090.

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 7069CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini93 – 1019LumenalSequence Analysis
Topological domaini119 – 21597CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini235 – 24915LumenalSequence AnalysisAdd
BLAST
Topological domaini273 – 35886CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei71 – 9222HelicalSequence AnalysisAdd
BLAST
Transmembranei102 – 11817HelicalSequence AnalysisAdd
BLAST
Transmembranei216 – 23419HelicalSequence AnalysisAdd
BLAST
Transmembranei250 – 27223HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi119 – 1246Histidine box-1
Motifi156 – 1605Histidine box-2
Motifi297 – 3015Histidine 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

eggNOGiCOG1398.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiQ6P7B9.
KOiK00507.
OrthoDBiEOG7ZPNKS.
PhylomeDBiQ6P7B9.
TreeFamiTF313251.

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.

Q6P7B9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAHILQEIS GSYSATTTIT APPSGGQQNG GEKFEKNPHH WGADVRPEIK
60 70 80 90 100
DDLYDPSYQD EEGPPPKLEY VWRNIVLMAL LHIGALYGIT LVPSCKVYTC
110 120 130 140 150
LFAYLYYVIS ALGITAGAHR LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY
160 170 180 190 200
EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD
210 220 230 240 250
MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET FVNSLCVSTF
260 270 280 290 300
LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
310 320 330 340 350
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSK AAVLARIKRT

GEESCKSG
Length:358
Mass (Da):41,013
Last modified:July 5, 2004 - v1
Checksum:i24EAA2329011C4D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761V → I in BAA92436. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB032243 mRNA. Translation: BAA92436.1.
BC061737 mRNA. Translation: AAH61737.1.
S75730 mRNA. Translation: AAB32826.1.
RefSeqiNP_114029.1. NM_031841.1.
UniGeneiRn.83595.

Genome annotation databases

GeneIDi83792.
KEGGirno:83792.
UCSCiRGD:621177. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB032243 mRNA. Translation: BAA92436.1 .
BC061737 mRNA. Translation: AAH61737.1 .
S75730 mRNA. Translation: AAB32826.1 .
RefSeqi NP_114029.1. NM_031841.1.
UniGenei Rn.83595.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000018090.

PTM databases

PhosphoSitei Q6P7B9.

Proteomic databases

PaxDbi Q6P7B9.
PRIDEi Q6P7B9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 83792.
KEGGi rno:83792.
UCSCi RGD:621177. rat.

Organism-specific databases

CTDi 6319.
RGDi 621177. Scd2.

Phylogenomic databases

eggNOGi COG1398.
HOGENOMi HOG000270352.
HOVERGENi HBG003367.
InParanoidi Q6P7B9.
KOi K00507.
OrthoDBi EOG7ZPNKS.
PhylomeDBi Q6P7B9.
TreeFami TF313251.

Miscellaneous databases

NextBioi 616377.

Gene expression databases

Genevestigatori Q6P7B9.

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. "Molecular cloning and tissue expression of rat stearoyl-CoA desaturase 2."
    Hoshino T., Ishiguro K., Ohtsu K.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Identification of novel mRNAs expressed in oligodendrocytes."
    Baba H., Fuss B., Watson J.B., Zane L.T., Macklin W.B.
    Neurochem. Res. 19:1091-1099(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.

Entry informationi

Entry nameiACOD2_RAT
AccessioniPrimary (citable) accession number: Q6P7B9
Secondary accession number(s): Q64066, Q9JMC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 78 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