P35610 (SOAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sterol O-acyltransferase 1
EC=2.3.1.26

Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 1
Short name=ACAT-1
Cholesterol acyltransferase 1

Gene names

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

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	550 AA.
Sequence status	Complete.
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.
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	Alternative splicing 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 PubMed 11401500. Source: BHF-UCL cholesterol metabolic process Inferred from direct assay PubMed 16647063. Source: BHF-UCL cholesterol storage Inferred from mutant phenotype Ref.1. Source: BHF-UCL macrophage derived foam cell differentiation Inferred from mutant phenotype PubMed 15353128. Source: BHF-UCL positive regulation of amyloid precursor protein biosynthetic process Inferred from mutant phenotype PubMed 17412327. Source: BHF-UCL very-low-density lipoprotein particle assembly Inferred from mutant phenotype PubMed 15308631. Source: BHF-UCL
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay PubMed 17412327. 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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35610-1)

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: P35610-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAE → M

Isoform 3 (identifier: P35610-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

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	Helical; Potential
	Transmembrane	320 – 341	22	Helical; Potential
	Transmembrane	361 – 382	22	Helical; Potential
	Transmembrane	470 – 490	21	Helical; Potential
	Transmembrane	498 – 518	21	Helical; Potential
Sites
	Active site	460	1	Potential
Natural variations
	Alternative sequence	1 – 65	65	Missing in isoform 3.		VSP_045330
	Alternative sequence	1 – 59	59	MVGEE…TAEAE → M in isoform 2.		VSP_045331
	Natural variant	526	1	Q → R. Ref.1 Corresponds to variant rs13306731 [ dbSNP | Ensembl ].		VAR_052031

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 285EF79CC80BF5E8	FASTA	492	58,131
	10 20 30 40 50 60 MELKPFFMKE VGSHFDDFVT NLIEKSASLD NGGCALTTFS VLEGEKNNHR AKDLRAPPEQ 70 80 90 100 110 120 GKIFIARRSL LDELLEVDHI RTIYHMFIAL LILFILSTLV VDYIDEGRLV LEFSLLSYAF 130 140 150 160 170 180 GKFPTVVWTW WIMFLSTFSV PYFLFQHWAT GYSKSSHPLI RSLFHGFLFM IFQIGVLGFG 190 200 210 220 230 240 PTYVVLAYTL PPASRFIIIF EQIRFVMKAH SFVRENVPRV LNSAKEKSST VPIPTVNQYL 250 260 270 280 290 300 YFLFAPTLIY RDSYPRNPTV RWGYVAMKFA QVFGCFFYVY YIFERLCAPL FRNIKQEPFS 310 320 330 340 350 360 ARVLVLCVFN SILPGVLILF LTFFAFLHCW LNAFAEMLRF GDRMFYKDWW NSTSYSNYYR 370 380 390 400 410 420 TWNVVVHDWL YYYAYKDFLW FFSKRFKSAA MLAVFAVSAV VHEYALAVCL SFFYPVLFVL 430 440 450 460 470 480 FMFFGMAFNF IVNDSRKKPI WNVLMWTSLF LGNGVLLCFY SQEWYARQHC PLKNPTFLDY 490 VRPRSWTCRY VF
	Isoform 3 [UniParc]. Checksum: 9C0D0F331D69376A	FASTA	485	57,238
	10 20 30 40 50 60 MKEVGSHFDD FVTNLIEKSA SLDNGGCALT TFSVLEGEKN NHRAKDLRAP PEQGKIFIAR 70 80 90 100 110 120 RSLLDELLEV DHIRTIYHMF IALLILFILS TLVVDYIDEG RLVLEFSLLS YAFGKFPTVV 130 140 150 160 170 180 WTWWIMFLST FSVPYFLFQH WATGYSKSSH PLIRSLFHGF LFMIFQIGVL GFGPTYVVLA 190 200 210 220 230 240 YTLPPASRFI IIFEQIRFVM KAHSFVRENV PRVLNSAKEK SSTVPIPTVN QYLYFLFAPT 250 260 270 280 290 300 LIYRDSYPRN PTVRWGYVAM KFAQVFGCFF YVYYIFERLC APLFRNIKQE PFSARVLVLC 310 320 330 340 350 360 VFNSILPGVL ILFLTFFAFL HCWLNAFAEM LRFGDRMFYK DWWNSTSYSN YYRTWNVVVH 370 380 390 400 410 420 DWLYYYAYKD FLWFFSKRFK SAAMLAVFAV SAVVHEYALA VCLSFFYPVL FVLFMFFGMA 430 440 450 460 470 480 FNFIVNDSRK KPIWNVLMWT SLFLGNGVLL CFYSQEWYAR QHCPLKNPTF LDYVRPRSWT CRYVF

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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]	"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] (ISOFORMS 2 AND 3).
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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: Placenta.
[7]	"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] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L21934 mRNA. Translation: AAC37532.2. AK290659 mRNA. Translation: BAF83348.1. AK300551 mRNA. Translation: BAG62257.1. AL451075, AL512326 Genomic DNA. Translation: CAI12676.1. AL512326, AL451075 Genomic DNA. Translation: CAI13574.1. CH471067 Genomic DNA. Translation: EAW91043.1. CH471067 Genomic DNA. Translation: EAW91044.1. BC028940 mRNA. Translation: AAH28940.1.
IPI	IPI00745125.
PIR	A48026. A59038.
RefSeq	NP_001239440.1. NM_001252511.1. NP_001239441.1. NM_001252512.1. NP_003092.4. NM_003101.5.
UniGene	Hs.445588.
3D structure databases
ProteinModelPortal	P35610.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000356591.
PTM databases
PhosphoSite	P35610.
Polymorphism databases
DMDM	33302623.
Proteomic databases
PaxDb	P35610.
PRIDE	P35610.
Protocols and materials databases
DNASU	6646.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367619; ENSP00000356591; ENSG00000057252. ENST00000539888; ENSP00000441356; ENSG00000057252. ENST00000540564; ENSP00000445315; ENSG00000057252.
GeneID	6646.
KEGG	hsa:6646.
UCSC	uc001gml.3. human.
Organism-specific databases
CTD	6646.
GeneCards	GC01P179262.
HGNC	HGNC:11177. SOAT1.
HPA	CAB009533.
MIM	102642. gene.
neXtProt	NX_P35610.
PharmGKB	PA36015.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5056.
HOGENOM	HOG000020782.
HOVERGEN	HBG058198.
InParanoid	P35610.
KO	K00637.
OMA	FNFILHD.
OrthoDB	EOG4M65H6.
PhylomeDB	P35610.
Enzyme and pathway databases
BRENDA	2.3.1.26. 2681.
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. 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	P35610.
ChEMBL	CHEMBL2782.
ChiTaRS	SOAT1. human.
DrugBank	DB00973. Ezetimibe. DB01094. Hesperetin.
GenomeRNAi	6646.
NextBio	25899.
SOURCE	Search...

Entry information

Entry name

SOAT1_HUMAN

Accession

Primary (citable) accession number: P35610
Secondary accession number(s): A6NC40 , A8K3P4, A9Z1V7, B4DU95, Q5T0X4, Q8N1E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 25, 2003
Last modified:	April 3, 2013
This is version 126 of the entry and version 3 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.