Q86SK9 (SCD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Stearoyl-CoA desaturase 5
EC=1.14.19.1

Alternative name(s):
Acyl-CoA-desaturase 4
HSCD5
Stearoyl-CoA 9-desaturase

Gene names

Name:	SCD5
Synonyms:	ACOD4, SCD4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Fatty acid delta-9-desaturase that introduces a double bond in fatty acyl-coenzyme A at the delta-9 position. Ref.7
Catalytic activity	Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.
Cofactor	Iron By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.
Tissue specificity	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. Ref.1 Ref.7
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding By similarity.
Sequence similarities	Belongs to the fatty acid desaturase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86SK9-1)

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.

Isoform 2 (identifier: Q86SK9-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	Stearoyl-CoA desaturase 5		PRO_0000312653
Regions
	Transmembrane	50 – 70	21	Helical; Potential
	Transmembrane	73 – 93	21	Helical; Potential
	Transmembrane	194 – 214	21	Helical; Potential
	Transmembrane	216 – 238	23	Helical; Potential
	Motif	94 – 99	6	Histidine box-1 By similarity
	Motif	131 – 135	5	Histidine box-2 By similarity
	Motif	272 – 276	5	Histidine box-3 By similarity
Natural variations
	Alternative sequence	190 – 330	141	KYYKI…GDSSA → NTQHIQKEGRALNQEAACEM LREWHQGHILKVTLPGLHIL ALLHTHCNHSEKCCLMLRAL SVSLEVF in isoform 2.		VSP_029883
Experimental info
	Sequence conflict	82	1	F → L in BAB14961. Ref.2
	Sequence conflict	127	1	W → R in AAP31443. Ref.1
	Sequence conflict	127	1	W → R in BAB14961. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 50652E942C19DB82	FASTA	330	37,610
	10 20 30 40 50 60 MPGPATDAGK IPFCDAKEEI RAGLESSEGG GGPERPGARG QRQNIVWRNV VLMSLLHLGA 70 80 90 100 110 120 VYSLVLIPKA KPLTLLWAYF CFLLAALGVT AGAHRLWSHR SYRAKLPLRI FLAVANSMAF 130 140 150 160 170 180 QNDIFEWSRD HRAHHKYSET DADPHNARRG FFFSHIGWLF VRKHRDVIEK GRKLDVTDLL 190 200 210 220 230 240 ADPVVRIQRK YYKISVVLMC FVVPTLVPWY IWGESLWNSY FLASILRYTI SLNISWLVNS 250 260 270 280 290 300 AAHMYGNRPY DKHISPRQNP LVALGAIGEG FHNYHHTFPF DYSASEFGLN FNPTTWFIDF 310 320 330 MCWLGLATDR KRATKPMIEA RKARTGDSSA
	Isoform 2 [UniParc]. Checksum: B8A6129F645C0ADE	FASTA	256	28,983
	10 20 30 40 50 60 MPGPATDAGK IPFCDAKEEI RAGLESSEGG GGPERPGARG QRQNIVWRNV VLMSLLHLGA 70 80 90 100 110 120 VYSLVLIPKA KPLTLLWAYF CFLLAALGVT AGAHRLWSHR SYRAKLPLRI FLAVANSMAF 130 140 150 160 170 180 QNDIFEWSRD HRAHHKYSET DADPHNARRG FFFSHIGWLF VRKHRDVIEK GRKLDVTDLL 190 200 210 220 230 240 ADPVVRIQRN TQHIQKEGRA LNQEAACEML REWHQGHILK VTLPGLHILA LLHTHCNHSE 250 KCCLMLRALS VSLEVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00016539. IPI00465139.
RefSeq	NP_001032671.2. NM_001037582.2. NP_079182.2. NM_024906.2.
UniGene	Hs.379191.
3D structure databases
ProteinModelPortal	Q86SK9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000316329.
PTM databases
PhosphoSite	Q86SK9.
Polymorphism databases
DMDM	162416247.
Proteomic databases
PaxDb	Q86SK9.
PRIDE	Q86SK9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273908; ENSP00000273908; ENSG00000145284. ENST00000319540; ENSP00000316329; ENSG00000145284.
GeneID	79966.
KEGG	hsa:79966.
UCSC	uc003hna.2. human. uc003hnb.4. human.
Organism-specific databases
CTD	79966.
GeneCards	GC04M083550.
HGNC	HGNC:21088. SCD5.
HPA	HPA042380.
MIM	608370. gene.
neXtProt	NX_Q86SK9.
PharmGKB	PA134934692.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1398.
HOGENOM	HOG000270352.
HOVERGEN	HBG003367.
InParanoid	Q86SK9.
KO	K00507.
OMA	AAYFCFL.
OrthoDB	EOG4Z36F2.
Enzyme and pathway databases
BRENDA	1.14.19.1. 2681.
Gene expression databases
ArrayExpress	Q86SK9.
Bgee	Q86SK9.
CleanEx	HS_SCD5.
Genevestigator	Q86SK9.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q86SK9.
ChEMBL	CHEMBL1275210.
GenomeRNAi	79966.
NextBio	69971.
SOURCE	Search...

Entry information

Entry name

SCD5_HUMAN

Accession

Primary (citable) accession number: Q86SK9
Secondary accession number(s): B2RPG0 , Q4W5Q5, Q8NDS0, Q9H7D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	April 3, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.