Reviewed, UniProtKB/Swiss-Prot Q86SK9 (SCD5_HUMAN)

Names and origin

Protein names

Recommended name:
    Stearoyl-CoA desaturase 5
    EC=1.14.19.1
Alternative name(s):
    HSCD5
    Acyl-CoA-desaturase 4
    Stearoyl-CoA 9-desaturase

Gene names

Name:	SCD5
Synonyms:	ACOD4, SCD4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.6
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.6
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.6 Ref.1
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 Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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: UniProtKB-KW 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	Potential
	Transmembrane	73 – 93	21	Potential
	Transmembrane	194 – 214	21	Potential
	Transmembrane	216 – 238	23	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. 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: 12727354] [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: 14702039] [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: 15815621] [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 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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-330. Tissue: Brain.
[6]	"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: 15907797] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF389338 mRNA. Translation: AAP31443.1. AK024685 mRNA. Translation: BAB14961.1. AC073413 Genomic DNA. Translation: AAY40977.1. CH471057 Genomic DNA. Translation: EAX05903.1. AL831891 mRNA. Translation: CAD38567.1.
IPI	IPI00016539. IPI00465139.
RefSeq	NP_001032671.2.
UniGene	Hs.379191
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000145284. Homo sapiens. [Contig view]
GeneID	79966.
KEGG	hsa:79966.
Organism-specific databases
GeneCards	GC04M083770.
HGNC	HGNC:21088. SCD5.
MIM	608370. gene.
PharmGKB	PA134934692.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q86SK9.
HOVERGEN	Q86SK9.
OMA	Q86SK9. CFFISAL.
Enzyme and pathway databases
BRENDA	1.14.19.1. 247.
Gene expression databases
ArrayExpress	Q86SK9.
Bgee	Q86SK9.
CleanEx	HS_SCD5.
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.
ProDom	PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	69971.
SOURCE	Search...

Entry information

Entry name

SCD5_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)