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P35610 (SOAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with UBIAD1. Ref.9

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 processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol 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_componentendoplasmic reticulum

Inferred from direct assay PubMed 10623671. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from direct assay PubMed 17412327. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 9756919. Source: MGI

   Molecular_functioncholesterol 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

sterol O-acyltransferase activity

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBIAD1Q9Y5Z93EBI-6621997,EBI-2819725

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Sterol O-acyltransferase 1
PRO_0000207640

Regions

Transmembrane141 – 15919Helical; Potential
Transmembrane320 – 34122Helical; Potential
Transmembrane361 – 38222Helical; Potential
Transmembrane470 – 49021Helical; Potential
Transmembrane498 – 51821Helical; Potential

Sites

Active site4601 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Natural variations

Alternative sequence1 – 6565Missing in isoform 3.
VSP_045330
Alternative sequence1 – 5959MVGEE…TAEAE → M in isoform 2.
VSP_045331
Natural variant5261Q → R. Ref.1
Corresponds to variant rs13306731 [ dbSNP | Ensembl ].
VAR_052031

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 25, 2003. Version 3.
Checksum: 5F5ACD525D541DEE

FASTA55064,735
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 285EF79CC80BF5E8
Show »

FASTA49258,131
Isoform 3 [UniParc].

Checksum: 9C0D0F331D69376A
Show »

FASTA48557,238

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol metabolic enzymes."
Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y., Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G., Andresson T., Kruth H.S., Okano T., Dean M.
Hum. Mutat. 34:317-329(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBIAD1.
+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.
PIRA48026. A59038.
RefSeqNP_001239440.1. NM_001252511.1.
NP_001239441.1. NM_001252512.1.
NP_003092.4. NM_003101.5.
UniGeneHs.445588.

3D structure databases

ProteinModelPortalP35610.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112529. 4 interactions.
IntActP35610. 2 interactions.
STRING9606.ENSP00000356591.

Chemistry

BindingDBP35610.
ChEMBLCHEMBL2782.
DrugBankDB00973. Ezetimibe.
DB01094. Hesperetin.

PTM databases

PhosphoSiteP35610.

Polymorphism databases

DMDM33302623.

Proteomic databases

PaxDbP35610.
PRIDEP35610.

Protocols and materials databases

DNASU6646.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367619; ENSP00000356591; ENSG00000057252. [P35610-1]
ENST00000539888; ENSP00000441356; ENSG00000057252. [P35610-3]
ENST00000540564; ENSP00000445315; ENSG00000057252. [P35610-2]
GeneID6646.
KEGGhsa:6646.
UCSCuc001gml.3. human. [P35610-1]
uc001gmm.3. human.

Organism-specific databases

CTD6646.
GeneCardsGC01P179262.
HGNCHGNC:11177. SOAT1.
HPACAB009533.
HPA047171.
MIM102642. gene.
neXtProtNX_P35610.
PharmGKBPA36015.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5056.
HOGENOMHOG000020782.
HOVERGENHBG058198.
InParanoidP35610.
KOK00637.
OMAFNFILHD.
OrthoDBEOG7ZPNJP.
PhylomeDBP35610.
TreeFamTF105767.

Enzyme and pathway databases

BRENDA2.3.1.26. 2681.

Gene expression databases

ArrayExpressP35610.
BgeeP35610.
CleanExHS_ACAT1.
HS_SOAT1.
GenevestigatorP35610.

Family and domain databases

InterProIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERPTHR10408. PTHR10408. 1 hit.
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSOAT1. human.
GeneWikiSOAT1.
GenomeRNAi6646.
NextBio25899.
PROP35610.
SOURCESearch...

Entry information

Entry nameSOAT1_HUMAN
AccessionPrimary (citable) accession number: P35610
Secondary accession number(s): A6NC40 expand/collapse secondary AC list , A8K3P4, A9Z1V7, B4DU95, Q5T0X4, Q8N1E4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 25, 2003
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM