O75908 (SOAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sterol O-acyltransferase 2
EC=2.3.1.26

Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 2
Short name=ACAT-2
Cholesterol acyltransferase 2

Gene names

Name:	SOAT2
Synonyms:	ACACT2, ACAT2

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	522 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
Catalytic activity	Acyl-CoA + cholesterol = CoA + cholesterol ester.
Subunit structure	May form homo- or heterodimers By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Sterol metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol efflux Inferred from mutant phenotype PubMed 15308631. Source: BHF-UCL cholesterol esterification Inferred from direct assay PubMed 16647063. Source: BHF-UCL cholesterol homeostasis Traceable author statement Ref.4. Source: BHF-UCL cholesterol metabolic process Inferred from direct assay PubMed 16647063. Source: BHF-UCL intestinal cholesterol absorption Inferred by curator PubMed 14615411. Source: BHF-UCL macrophage derived foam cell differentiation Traceable author statement PubMed 14615411. Source: BHF-UCL very-low-density lipoprotein particle assembly Inferred from mutant phenotype PubMed 15308631. Source: BHF-UCL
Cellular_component	brush border Inferred from direct assay PubMed 14615411. Source: BHF-UCL endoplasmic reticulum membrane Inferred from direct assay PubMed 12808042. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cholesterol O-acyltransferase activity Inferred from direct assay PubMed 16647063. Source: BHF-UCL cholesterol binding Inferred from direct assay PubMed 16647063. Source: BHF-UCL fatty-acyl-CoA binding Inferred from direct assay PubMed 16647063. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 522	522	Sterol O-acyltransferase 2		PRO_0000207645
Regions
	Transmembrane	124 – 144	21	Helical; Potential
	Transmembrane	155 – 175	21	Helical; Potential
	Transmembrane	200 – 220	21	Helical; Potential
	Transmembrane	262 – 282	21	Helical; Potential
	Transmembrane	304 – 324	21	Helical; Potential
	Transmembrane	344 – 366	23	Helical; Potential
	Transmembrane	437 – 457	21	Helical; Potential
	Transmembrane	472 – 492	21	Helical; Potential
Sites
	Active site	434	1	Potential
Natural variations
	Natural variant	14	1	E → G. Corresponds to variant rs9658625 [ dbSNP | Ensembl ].		VAR_020373
	Natural variant	254	1	T → I. Ref.2 Ref.5 Corresponds to variant rs2272296 [ dbSNP | Ensembl ].		VAR_020374
Experimental info
	Sequence conflict	22	1	R → P in AAK48829. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O75908 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: EEAC2DB569FFE729	FASTA	522	59,896
	10 20 30 40 50 60 MEPGGARLRL QRTEGLGGER ERQPCGDGNT ETHRAPDLVQ WTRHMEAVKA QLLEQAQGQL 70 80 90 100 110 120 RELLDRAMRE AIQSYPSQDK PLPPPPPGSL SRTQEPSLGK QKVFIIRKSL LDELMEVQHF 130 140 150 160 170 180 RTIYHMFIAG LCVFIISTLA IDFIDEGRLL LEFDLLIFSF GQLPLALVTW VPMFLSTLLA 190 200 210 220 230 240 PYQALRLWAR GTWTQATGLG CALLAAHAVV LCALPVHVAV EHQLPPASRC VLVFEQVRFL 250 260 270 280 290 300 MKSYSFLREA VPGTLRARRG EGIQAPSFSS YLYFLFCPTL IYRETYPRTP YVRWNYVAKN 310 320 330 340 350 360 FAQALGCVLY ACFILGRLCV PVFANMSREP FSTRALVLSI LHATLPGIFM LLLIFFAFLH 370 380 390 400 410 420 CWLNAFAEML RFGDRMFYRD WWNSTSFSNY YRTWNVVVHD WLYSYVYQDG LRLLGARARG 430 440 450 460 470 480 VAMLGVFLVS AVAHEYIFCF VLGFFYPVML ILFLVIGGML NFMMHDQRTG PAWNVLMWTM 490 500 510 520 LFLGQGIQVS LYCQEWYARR HCPLPQATFW GLVTPRSWSC HT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes." Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L. J. Biol. Chem. 273:26765-26771(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine." Chang C.C.Y., Sakashita N., Ornvold K., Lee O., Chang E.T., Dong R., Lin S., Lee C.-Y.G., Strom S.C., Kashyap R., Fung J.J., Farese R.V. Jr., Patoiseau J.-F., Delhon A., Chang T.-Y. J. Biol. Chem. 275:28083-28092(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-254. Tissue: Intestine.
[3]	"Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia." Katsuren K., Tamura T., Arashiro R., Takata K., Matsuura T., Niikawa N., Ohta T. Biochim. Biophys. Acta 1531:230-240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Organization of human ACAT-2 gene and its cell-type-specific promoter activity." Song B.L., Qi W., Yang X.Y., Chang C.C.Y., Zhu J.Q., Chang T.Y., Li B.L. Biochem. Biophys. Res. Commun. 282:580-588(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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], VARIANT ILE-254.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF059203 mRNA. Translation: AAC63998.1. AF099031 mRNA. Translation: AAC78335.2. AF331516 , AF331502, AF331503, AF331504, AF331505, AF331506, AF331507, AF331508, AF331509, AF331510, AF331511, AF331512, AF331513, AF331514, AF331515 Genomic DNA. Translation: AAK18275.1. AF332858, AF332857 Genomic DNA. Translation: AAK48829.1. BC096091 mRNA. Translation: AAH96091.1. BC096092 mRNA. Translation: AAH96092.1.
IPI	IPI00020669.
RefSeq	NP_003569.1. NM_003578.3.
UniGene	Hs.656544.
3D structure databases
ProteinModelPortal	O75908.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000301466.
PTM databases
PhosphoSite	O75908.
Proteomic databases
PaxDb	O75908.
PRIDE	O75908.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301466; ENSP00000301466; ENSG00000167780.
GeneID	8435.
KEGG	hsa:8435.
UCSC	uc001sbv.3. human.
Organism-specific databases
CTD	8435.
GeneCards	GC12P053497.
HGNC	HGNC:11178. SOAT2.
HPA	HPA049462.
MIM	601311. gene.
neXtProt	NX_O75908.
PharmGKB	PA36016.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5056.
HOGENOM	HOG000020782.
HOVERGEN	HBG058198.
InParanoid	O75908.
KO	K00637.
OMA	CFILGRL.
OrthoDB	EOG4548ZG.
PhylomeDB	O75908.
Enzyme and pathway databases
BRENDA	2.3.1.26. 2681.
Gene expression databases
ArrayExpress	O75908.
Bgee	O75908.
CleanEx	HS_ACAT2. HS_SOAT2.
Genevestigator	O75908.
GermOnline	ENSG00000167780. Homo sapiens.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. IPR014371. Oat_ACAT_DAG_ARE. [Graphical view]
PANTHER	PTHR10408. PTHR10408. 1 hit.
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
PIRSF	PIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNet	Search...
Other
BindingDB	O75908.
ChEMBL	CHEMBL4465.
GenomeRNAi	8435.
NextBio	31558.
SOURCE	Search...

Entry information

Entry name

SOAT2_HUMAN

Accession

Primary (citable) accession number: O75908
Secondary accession number(s): Q4VB99, Q96TD4, Q9UNR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 107 of the entry and version 1 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.