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P21147 (ACO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-CoA desaturase 1
EC=1.14.19.1
Alternative name(s):
Fatty acid desaturase 1
Stearoyl-CoA desaturase 1
Gene names
Name:OLE1
Ordered Locus Names:YGL055W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Utilizes O2 and electrons from the reduced cytochrome b5 domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates Probable.

Catalytic activity

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

Cofactor

Iron.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similarities

Belongs to the fatty acid desaturase family.

Contains 1 cytochrome b5 heme-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Acyl-CoA desaturase 1
PRO_0000185406

Regions

Topological domain1 – 112112Cytoplasmic Potential
Transmembrane113 – 13321Helical; Potential
Topological domain134 – 1385Lumenal Potential
Transmembrane139 – 15921Helical; Potential
Topological domain160 – 25596Cytoplasmic Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 2804Lumenal Potential
Transmembrane281 – 30121Helical; Potential
Topological domain302 – 510209Cytoplasmic Potential
Domain409 – 48779Cytochrome b5 heme-binding
Motif161 – 1666Histidine box-1
Motif198 – 2025Histidine box-2
Motif335 – 3395Histidine box-3

Sites

Metal binding4441Iron (heme axial ligand) By similarity
Metal binding4701Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict671D → G in AAT93029. Ref.5
Sequence conflict3041L → M in AAA34826. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21147 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: A6CC78DD4210ECCA

FASTA51058,403
        10         20         30         40         50         60 
MPTSGTTIEL IDDQFPKDDS ASSGIVDEVD LTEANILATG LNKKAPRIVN GFGSLMGSKE 

        70         80         90        100        110        120 
MVSVEFDKKG NEKKSNLDRL LEKDNQEKEE AKTKIHISEQ PWTLNNWHQH LNWLNMVLVC 

       130        140        150        160        170        180 
GMPMIGWYFA LSGKVPLHLN VFLFSVFYYA VGGVSITAGY HRLWSHRSYS AHWPLRLFYA 

       190        200        210        220        230        240 
IFGCASVEGS AKWWGHSHRI HHRYTDTLRD PYDARRGLWY SHMGWMLLKP NPKYKARADI 

       250        260        270        280        290        300 
TDMTDDWTIR FQHRHYILLM LLTAFVIPTL ICGYFFNDYM GGLIYAGFIR VFVIQQATFC 

       310        320        330        340        350        360 
INSLAHYIGT QPFDDRRTPR DNWITAIVTF GEGYHNFHHE FPTDYRNAIK WYQYDPTKVI 

       370        380        390        400        410        420 
IYLTSLVGLA YDLKKFSQNA IEEALIQQEQ KKINKKKAKI NWGPVLTDLP MWDKQTFLAK 

       430        440        450        460        470        480 
SKENKGLVII SGIVHDVSGY ISEHPGGETL IKTALGKDAT KAFSGGVYRH SNAAQNVLAD 

       490        500        510 
MRVAVIKESK NSAIRMASKR GEIYETGKFF

« Hide

References

« Hide 'large scale' references
[1]"The OLE1 gene of Saccharomyces cerevisiae encodes the delta 9 fatty acid desaturase and can be functionally replaced by the rat stearoyl-CoA desaturase gene."
Stukey J.E., McDonough V.M., Martin C.E.
J. Biol. Chem. 265:20144-20149(1990) [PubMed: 1978720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed: 9234674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05676 Genomic DNA. Translation: AAA34826.1.
Z72577 Genomic DNA. Translation: CAA96757.1.
AY693010 Genomic DNA. Translation: AAT93029.1.
BK006941 Genomic DNA. Translation: DAA08047.1.
PIRS64059.
RefSeqNP_011460.1. NM_001180920.1.

3D structure databases

ProteinModelPortalP21147.
SMRP21147. Positions 407-490.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5026N.
IntActP21147. 57 interactions.
MINTMINT-563591.
STRINGP21147.

Proteomic databases

PeptideAtlasP21147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL055W; YGL055W; YGL055W.
GeneID852825.
KEGGsce:YGL055W.
NMPDRfig|4932.3.peg.2566.

Organism-specific databases

CYGDYGL055w.
SGDS000003023. OLE1.

Phylogenomic databases

eggNOGfuNOG04438.
HOGENOMHBG520703.
OMAHRIHHRY.
OrthoDBEOG4W11NG.

Gene expression databases

ArrayExpressP21147.
GenevestigatorP21147.
GermOnlineYGL055W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
Gene3DG3DSA:3.10.120.10. Cyt_B5. 1 hit.
KOK00507.
PfamPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFPIRSF000345. OLE1. 1 hit.
PRINTSPR00075. FACDDSATRASE.
SUPFAMSSF55856. Cyt_B5. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972381.

Entry information

Entry nameACO1_YEAST
AccessionPrimary (citable) accession number: P21147
Secondary accession number(s): D6VU86, E9P911
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents