Reviewed, UniProtKB/Swiss-Prot P35610 (SOAT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Sterol O-acyltransferase 1
    EC=2.3.1.26
Alternative name(s):
    Cholesterol acyltransferase 1
    Acyl coenzyme A:cholesterol acyltransferase 1
      Short name=ACAT-1

Gene names

Name:	SOAT1
Synonyms:	ACACT, ACACT1, ACAT, ACAT1, SOAT, STAT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase.
Catalytic activity	Acyl-CoA + cholesterol = CoA + cholesterol ester.
Subunit structure	May form homo- or heterodimers.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Induction	Highly activated by the presence of cholesterol.
Involvement in disease	Accumulation of insoluble cholesterol esters in macrophages and smooth muscle is a characteristic feature of early lesions of atherosclerotic plaque.
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cholesterol efflux Inferred from mutant phenotype. Source: UniProtKB cholesterol esterification Ref.1 Inferred from direct assay. Source: UniProtKB cholesterol homeostasis Traceable author statement. Source: UniProtKB cholesterol metabolic process Ref.1 Inferred from direct assay. Source: UniProtKB cholesterol storage Ref.1 Inferred from mutant phenotype. Source: UniProtKB macrophage derived foam cell differentiation Ref.1 Inferred from mutant phenotype. Source: UniProtKB positive regulation of amyloid precursor protein biosynthetic process Inferred from mutant phenotype. Source: UniProtKB very-low-density lipoprotein particle assembly Inferred from mutant phenotype. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: UniProtKB
Molecular function	acyl-CoA binding Inferred from direct assay. Source: UniProtKB cholesterol O-acyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB cholesterol binding Inferred from direct assay. Source: UniProtKB ergosterol O-acyltransferase activity Inferred from electronic annotation. Source: EC lanosterol O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 550	550	Sterol O-acyltransferase 1		PRO_0000207640
Regions
	Transmembrane	141 – 159	19	Potential
	Transmembrane	320 – 341	22	Potential
	Transmembrane	361 – 382	22	Potential
	Transmembrane	470 – 490	21	Potential
	Transmembrane	498 – 518	21	Potential
Sites
	Active site	460	1	Potential
Natural variations
	Natural variant	526	1	Q → R: dbSNP rs13306731. Ref.1		VAR_052031

Sequences

	Sequence		Length	Mass (Da)
	P35610-1 [UniParc]. Last modified July 25, 2003. Version 3. Checksum: 5F5ACD525D541DEE	FASTA	550	64,735
	10 20 30 40 50 60 MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK KIKLTAEAEE 70 80 90 100 110 120 LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL EGEKNNHRAK DLRAPPEQGK 130 140 150 160 170 180 IFIARRSLLD ELLEVDHIRT IYHMFIALLI LFILSTLVVD YIDEGRLVLE FSLLSYAFGK 190 200 210 220 230 240 FPTVVWTWWI MFLSTFSVPY FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT 250 260 270 280 290 300 YVVLAYTLPP ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF 310 320 330 340 350 360 LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR NIKQEPFSAR 370 380 390 400 410 420 VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW 430 440 450 460 470 480 NVVVHDWLYY YAYKDFLWFF SKRFKSAAML AVFAVSAVVH EYALAVCLSF FYPVLFVLFM 490 500 510 520 530 540 FFGMAFNFIV NDSRKKPIWN VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR 550 PRSWTCRYVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells." Chang C.C.Y., Huh H.Y., Cadigan K.M., Chang T.-Y. J. Biol. Chem. 268:20747-20755(1993) [PubMed: 8407899] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-526. Tissue: Macrophage.
[2]	Chang C.C.Y., Chang T.-Y. Submitted (MAY-1999) to UniProtKB Cited for: SEQUENCE REVISION TO 207.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[6]	"Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains." Lin S., Cheng D., Liu M.S., Chen J., Chang T.-Y. J. Biol. Chem. 274:23276-23285(1999) [PubMed: 10438503] [Abstract] Cited for: TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L21934 mRNA. Translation: AAC37532.2. AL451075, AL512326 Genomic DNA. Translation: CAI12676.1. AL512326, AL451075 Genomic DNA. Translation: CAI13574.1. CH471067 Genomic DNA. Translation: EAW91044.1. BC028940 mRNA. Translation: AAH28940.1.
IPI	IPI00745125.
PIR	A48026. A59038.
RefSeq	NP_003092.4.
UniGene	Hs.496383
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P35610.
PTM databases
PhosphoSite	P35610.
Proteomic databases
PRIDE	P35610.
Genome annotation databases
Ensembl	ENST00000367619; ENSP00000356591; ENSG00000057252; Homo sapiens. [Genome view] ENST00000426956; ENSP00000411309; ENSG00000057252; Homo sapiens. [Genome view]
GeneID	6646.
KEGG	hsa:6646.
UCSC	uc001gml.1. human.
Organism-specific databases
CTD	6646.
GeneCards	GC01P177529.
H-InvDB	HIX0001375.
HGNC	HGNC:11177. SOAT1.
HPA	CAB009533.
MIM	102642. gene.
PharmGKB	PA36015.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P35610.
OMA	FLDYVRP.
Enzyme and pathway databases
BRENDA	2.3.1.26. 247.
Gene expression databases
ArrayExpress	P35610.
Bgee	P35610.
CleanEx	HS_ACAT1. HS_SOAT1.
Genevestigator	P35610.
GermOnline	ENSG00000057252. Homo sapiens.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00973. Ezetimibe. DB01094. Hesperetin.
NextBio	25899.
SOURCE	Search...

Entry information

Entry name

SOAT1_HUMAN

Accession

Primary (citable) accession number: P35610
Secondary accession number(s): A6NC40 , A9Z1V7, Q5T0X4, Q8N1E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 25, 2003
Last modified:	November 3, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.