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Protein

Stearoyl-CoA desaturase 5

Gene

SCD5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:15610069). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids.2 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.2 Publications

Cofactori

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49SubstrateBy similarity1
Metal bindingi94Iron 1By similarity1
Metal bindingi99Iron 1By similarity1
Binding sitei122SubstrateBy similarity1
Binding sitei129SubstrateBy similarity1
Binding sitei130SubstrateBy similarity1
Metal bindingi131Iron 1By similarity1
Metal bindingi134Iron 2By similarity1
Metal bindingi135Iron 1By similarity1
Binding sitei162SubstrateBy similarity1
Binding sitei163SubstrateBy similarity1
Binding sitei236SubstrateBy similarity1
Metal bindingi243Iron 2By similarity1
Metal bindingi272Iron 2By similarity1
Metal bindingi275Iron 1By similarity1
Metal bindingi276Iron 2By similarity1

GO - Molecular functioni

  • iron ion binding Source: GO_Central
  • oxidoreductase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS07241-MONOMER.
BRENDAi1.14.19.1. 2681.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Chemistry databases

SwissLipidsiSLP:000001074.

Names & Taxonomyi

Protein namesi
Recommended name:
Stearoyl-CoA desaturase 5Curated (EC:1.14.19.12 Publications)
Alternative name(s):
Acyl-CoA-desaturase 4
HSCD51 Publication
Stearoyl-CoA 9-desaturase1 Publication
Stearoyl-CoA desaturase 21 Publication
Gene namesi
Name:SCD5
Synonyms:ACOD4, SCD21 Publication, SCD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:21088. SCD5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 49CytoplasmicCuratedAdd BLAST49
Transmembranei50 – 70HelicalSequence analysisAdd BLAST21
Topological domaini71 – 72LumenalCurated2
Transmembranei73 – 93HelicalSequence analysisAdd BLAST21
Topological domaini94 – 193CytoplasmicCuratedAdd BLAST100
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Topological domaini215LumenalCurated1
Transmembranei216 – 238HelicalSequence analysisAdd BLAST23
Topological domaini239 – 330CytoplasmicCuratedAdd BLAST92

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi79966.
OpenTargetsiENSG00000145284.
PharmGKBiPA134934692.

Chemistry databases

ChEMBLiCHEMBL1275210.

Polymorphism and mutation databases

BioMutaiSCD5.
DMDMi162416247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003126531 – 330Stearoyl-CoA desaturase 5Add BLAST330

Proteomic databases

EPDiQ86SK9.
MaxQBiQ86SK9.
PaxDbiQ86SK9.
PeptideAtlasiQ86SK9.
PRIDEiQ86SK9.

PTM databases

iPTMnetiQ86SK9.
PhosphoSitePlusiQ86SK9.

Expressioni

Tissue specificityi

Detected in fetal brain, and at lower levels in fetal kidney. Detected in adult brain and pancreas, and at lower levels in kidney and lung.3 Publications

Gene expression databases

BgeeiENSG00000145284.
CleanExiHS_SCD5.
GenevisibleiQ86SK9. HS.

Organism-specific databases

HPAiHPA042380.

Interactioni

Subunit structurei

May self-associate and form homodimers.1 Publication

Protein-protein interaction databases

BioGridi123034. 5 interactors.
IntActiQ86SK9. 2 interactors.
STRINGi9606.ENSP00000316329.

Chemistry databases

BindingDBiQ86SK9.

Structurei

3D structure databases

ProteinModelPortaliQ86SK9.
SMRiQ86SK9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi94 – 99Histidine box-1Curated6
Motifi131 – 135Histidine box-2Curated5
Motifi272 – 276Histidine box-3Curated5

Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiQ86SK9.
KOiK00507.
OMAiGLWWAHI.
OrthoDBiEOG091G0B5S.
PhylomeDBiQ86SK9.
TreeFamiTF313251.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86SK9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGPATDAGK IPFCDAKEEI RAGLESSEGG GGPERPGARG QRQNIVWRNV
60 70 80 90 100
VLMSLLHLGA VYSLVLIPKA KPLTLLWAYF CFLLAALGVT AGAHRLWSHR
110 120 130 140 150
SYRAKLPLRI FLAVANSMAF QNDIFEWSRD HRAHHKYSET DADPHNARRG
160 170 180 190 200
FFFSHIGWLF VRKHRDVIEK GRKLDVTDLL ADPVVRIQRK YYKISVVLMC
210 220 230 240 250
FVVPTLVPWY IWGESLWNSY FLASILRYTI SLNISWLVNS AAHMYGNRPY
260 270 280 290 300
DKHISPRQNP LVALGAIGEG FHNYHHTFPF DYSASEFGLN FNPTTWFIDF
310 320 330
MCWLGLATDR KRATKPMIEA RKARTGDSSA
Length:330
Mass (Da):37,610
Last modified:December 4, 2007 - v2
Checksum:i50652E942C19DB82
GO
Isoform 2 (identifier: Q86SK9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-330: KYYKISVVLM...RKARTGDSSA → NTQHIQKEGR...RALSVSLEVF

Note: No experimental confirmation available.
Show »
Length:256
Mass (Da):28,983
Checksum:iB8A6129F645C0ADE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82F → L in BAB14961 (PubMed:14702039).Curated1
Sequence conflicti127W → R in AAP31443 (PubMed:12727354).Curated1
Sequence conflicti127W → R in BAB14961 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_029883190 – 330KYYKI…GDSSA → NTQHIQKEGRALNQEAACEM LREWHQGHILKVTLPGLHIL ALLHTHCNHSEKCCLMLRAL SVSLEVF in isoform 2. 1 PublicationAdd BLAST141

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF389338 mRNA. Translation: AAP31443.1.
AK024685 mRNA. Translation: BAB14961.1.
AC073413 Genomic DNA. Translation: AAY40977.1.
CH471057 Genomic DNA. Translation: EAX05903.1.
CH471057 Genomic DNA. Translation: EAX05904.1.
BC137429 mRNA. Translation: AAI37430.1.
BC137432 mRNA. Translation: AAI37433.1.
AL831891 mRNA. Translation: CAD38567.1.
CCDSiCCDS34024.1. [Q86SK9-1]
CCDS3595.1. [Q86SK9-2]
RefSeqiNP_001032671.2. NM_001037582.2. [Q86SK9-1]
NP_079182.2. NM_024906.2. [Q86SK9-2]
UniGeneiHs.379191.

Genome annotation databases

EnsembliENST00000273908; ENSP00000273908; ENSG00000145284. [Q86SK9-2]
ENST00000319540; ENSP00000316329; ENSG00000145284. [Q86SK9-1]
GeneIDi79966.
KEGGihsa:79966.
UCSCiuc003hna.3. human. [Q86SK9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF389338 mRNA. Translation: AAP31443.1.
AK024685 mRNA. Translation: BAB14961.1.
AC073413 Genomic DNA. Translation: AAY40977.1.
CH471057 Genomic DNA. Translation: EAX05903.1.
CH471057 Genomic DNA. Translation: EAX05904.1.
BC137429 mRNA. Translation: AAI37430.1.
BC137432 mRNA. Translation: AAI37433.1.
AL831891 mRNA. Translation: CAD38567.1.
CCDSiCCDS34024.1. [Q86SK9-1]
CCDS3595.1. [Q86SK9-2]
RefSeqiNP_001032671.2. NM_001037582.2. [Q86SK9-1]
NP_079182.2. NM_024906.2. [Q86SK9-2]
UniGeneiHs.379191.

3D structure databases

ProteinModelPortaliQ86SK9.
SMRiQ86SK9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123034. 5 interactors.
IntActiQ86SK9. 2 interactors.
STRINGi9606.ENSP00000316329.

Chemistry databases

BindingDBiQ86SK9.
ChEMBLiCHEMBL1275210.
SwissLipidsiSLP:000001074.

PTM databases

iPTMnetiQ86SK9.
PhosphoSitePlusiQ86SK9.

Polymorphism and mutation databases

BioMutaiSCD5.
DMDMi162416247.

Proteomic databases

EPDiQ86SK9.
MaxQBiQ86SK9.
PaxDbiQ86SK9.
PeptideAtlasiQ86SK9.
PRIDEiQ86SK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273908; ENSP00000273908; ENSG00000145284. [Q86SK9-2]
ENST00000319540; ENSP00000316329; ENSG00000145284. [Q86SK9-1]
GeneIDi79966.
KEGGihsa:79966.
UCSCiuc003hna.3. human. [Q86SK9-1]

Organism-specific databases

CTDi79966.
DisGeNETi79966.
GeneCardsiSCD5.
HGNCiHGNC:21088. SCD5.
HPAiHPA042380.
MIMi608370. gene.
neXtProtiNX_Q86SK9.
OpenTargetsiENSG00000145284.
PharmGKBiPA134934692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiQ86SK9.
KOiK00507.
OMAiGLWWAHI.
OrthoDBiEOG091G0B5S.
PhylomeDBiQ86SK9.
TreeFamiTF313251.

Enzyme and pathway databases

BioCyciZFISH:HS07241-MONOMER.
BRENDAi1.14.19.1. 2681.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

GenomeRNAii79966.
PROiQ86SK9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145284.
CleanExiHS_SCD5.
GenevisibleiQ86SK9. HS.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSCD5_HUMAN
AccessioniPrimary (citable) accession number: Q86SK9
Secondary accession number(s): B2RPG0
, Q4W5Q5, Q8NDS0, Q9H7D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: November 30, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.