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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491SubstrateBy similarity
Metal bindingi94 – 941Iron 1By similarity
Metal bindingi99 – 991Iron 1By similarity
Binding sitei122 – 1221SubstrateBy similarity
Binding sitei129 – 1291SubstrateBy similarity
Binding sitei130 – 1301SubstrateBy similarity
Metal bindingi131 – 1311Iron 1By similarity
Metal bindingi134 – 1341Iron 2By similarity
Metal bindingi135 – 1351Iron 1By similarity
Binding sitei162 – 1621SubstrateBy similarity
Binding sitei163 – 1631SubstrateBy similarity
Binding sitei236 – 2361SubstrateBy similarity
Metal bindingi243 – 2431Iron 2By similarity
Metal bindingi272 – 2721Iron 2By similarity
Metal bindingi275 – 2751Iron 1By similarity
Metal bindingi276 – 2761Iron 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

  • unsaturated fatty acid biosynthetic process Source: UniProtKB
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

BRENDAi1.14.19.1. 2681.

Chemistry

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949CytoplasmicCuratedAdd
BLAST
Transmembranei50 – 7021HelicalSequence analysisAdd
BLAST
Topological domaini71 – 722LumenalCurated
Transmembranei73 – 9321HelicalSequence analysisAdd
BLAST
Topological domaini94 – 193100CytoplasmicCuratedAdd
BLAST
Transmembranei194 – 21421HelicalSequence analysisAdd
BLAST
Topological domaini215 – 2151LumenalCurated
Transmembranei216 – 23823HelicalSequence analysisAdd
BLAST
Topological domaini239 – 33092CytoplasmicCuratedAdd
BLAST

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

PharmGKBiPA134934692.

Chemistry

ChEMBLiCHEMBL1275210.

Polymorphism and mutation databases

BioMutaiSCD5.
DMDMi162416247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Stearoyl-CoA desaturase 5PRO_0000312653Add
BLAST

Proteomic databases

EPDiQ86SK9.
MaxQBiQ86SK9.
PaxDbiQ86SK9.
PRIDEiQ86SK9.

PTM databases

iPTMnetiQ86SK9.
PhosphoSiteiQ86SK9.

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

BgeeiQ86SK9.
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 interactions.
IntActiQ86SK9. 2 interactions.
STRINGi9606.ENSP00000316329.

Chemistry

BindingDBiQ86SK9.

Structurei

3D structure databases

ProteinModelPortaliQ86SK9.
SMRiQ86SK9. Positions 46-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 996Histidine box-1Curated
Motifi131 – 1355Histidine box-2Curated
Motifi272 – 2765Histidine box-3Curated

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.
OMAiMTPNIIG.
OrthoDBiEOG7ZPNKS.
PhylomeDBiQ86SK9.
TreeFamiTF313251.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821F → L in BAB14961 (PubMed:14702039).Curated
Sequence conflicti127 – 1271W → R in AAP31443 (PubMed:12727354).Curated
Sequence conflicti127 – 1271W → R in BAB14961 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei190 – 330141KYYKI…GDSSA → NTQHIQKEGRALNQEAACEM LREWHQGHILKVTLPGLHIL ALLHTHCNHSEKCCLMLRAL SVSLEVF in isoform 2. 1 PublicationVSP_029883Add
BLAST

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. Positions 46-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123034. 5 interactions.
IntActiQ86SK9. 2 interactions.
STRINGi9606.ENSP00000316329.

Chemistry

BindingDBiQ86SK9.
ChEMBLiCHEMBL1275210.
SwissLipidsiSLP:000001074.

PTM databases

iPTMnetiQ86SK9.
PhosphoSiteiQ86SK9.

Polymorphism and mutation databases

BioMutaiSCD5.
DMDMi162416247.

Proteomic databases

EPDiQ86SK9.
MaxQBiQ86SK9.
PaxDbiQ86SK9.
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.
GeneCardsiSCD5.
HGNCiHGNC:21088. SCD5.
HPAiHPA042380.
MIMi608370. gene.
neXtProtiNX_Q86SK9.
PharmGKBiPA134934692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiQ86SK9.
KOiK00507.
OMAiMTPNIIG.
OrthoDBiEOG7ZPNKS.
PhylomeDBiQ86SK9.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 2681.

Miscellaneous databases

GenomeRNAii79966.
NextBioi69971.
PROiQ86SK9.
SOURCEiSearch...

Gene expression databases

BgeeiQ86SK9.
CleanExiHS_SCD5.
GenevisibleiQ86SK9. HS.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel gene disrupted by a pericentric inversion inv(4)(p13.1q21.1) in a family with cleft lip."
    Beiraghi S., Zhou M., Talmadge C.B., Went-Sumegi N., Davis J.R., Huang D., Saal H., Seemayer T.A., Sumegi J.
    Gene 309:11-21(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Endothelial cell.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-330.
    Tissue: Brain.
  7. "Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to primates."
    Wang J., Yu L., Schmidt R.E., Su C., Huang X., Gould K., Cao G.
    Biochem. Biophys. Res. Commun. 332:735-742(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Characterization of human SCD2, an oligomeric desaturase with improved stability and enzyme activity by cross-linking in intact cells."
    Zhang S., Yang Y., Shi Y.
    Biochem. J. 388:135-142(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBUNIT.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: April 13, 2016
This is version 105 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.