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P35610 (SOAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.

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
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcholesterol efflux

Inferred from mutant phenotype. Source: BHF-UCL

cholesterol esterification

Inferred from direct assay. Source: BHF-UCL

cholesterol homeostasis

Traceable author statement. Source: BHF-UCL

cholesterol metabolic process

Inferred from direct assay. Source: BHF-UCL

cholesterol storage

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

macrophage derived foam cell differentiation

Inferred from mutant phenotype. Source: BHF-UCL

positive regulation of amyloid precursor protein biosynthetic process

Inferred from mutant phenotype. Source: BHF-UCL

very-low-density lipoprotein particle assembly

Inferred from mutant phenotype. Source: BHF-UCL

   Cellular componentendoplasmic reticulum membrane

Inferred from direct assay. Source: BHF-UCL

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microsome

Inferred from direct assay. Source: BHF-UCL

   Molecular functioncholesterol O-acyltransferase activity

Inferred from direct assay. Source: BHF-UCL

cholesterol binding

Inferred from direct assay. Source: BHF-UCL

fatty-acyl-CoA binding

Inferred from direct assay. Source: BHF-UCL

Complete GO annotation...

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

Natural variations

Natural variant5261Q → R. Ref.1
Corresponds to variant rs13306731 [ dbSNP | Ensembl ].
VAR_052031

Sequences

Sequence LengthMass (Da)Tools
P35610 [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

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: 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. 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: 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. 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].
[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

EMBL
GenBank
DDBJ		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.
IPIIPI00745125.
PIRA48026. A59038.
RefSeqNP_003092.4. NM_003101.5.
UniGeneHs.496383.

3D structure databases

ProteinModelPortalP35610.
ModBaseSearch...

Protein-protein interaction databases

STRINGP35610.

Polymorphism databases

DMDM33302623.

Proteomic databases

PRIDEP35610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367619; ENSP00000356591; ENSG00000057252.
GeneID6646.
KEGGhsa:6646.
UCSCuc001gml.1. human.

Organism-specific databases

CTD6646.
GeneCardsGC01P179262.
H-InvDBHIX0199851.
HGNCHGNC:11177. SOAT1.
HPACAB009533.
MIM102642. gene.
neXtProtNX_P35610.
PharmGKBPA36015.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05820.
GeneTreeENSGT00530000063122.
HOGENOMHBG446698.
HOVERGENHBG058198.
InParanoidP35610.
OMAQVFGCFF.
OrthoDBEOG4M65H6.
PhylomeDBP35610.

Enzyme and pathway databases

BRENDA2.3.1.26. 2681.

Gene expression databases

ArrayExpressP35610.
BgeeP35610.
CleanExHS_ACAT1.
HS_SOAT1.
GenevestigatorP35610.
GermOnlineENSG00000057252. Homo sapiens.

Family and domain databases

InterProIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
KOK00637.
PANTHERPTHR10408. PTHR10408. 1 hit.
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNetSearch...

Other

DrugBankDB00973. Ezetimibe.
DB01094. Hesperetin.
NextBio25899.
SOURCESearch...

Entry information

Entry nameSOAT1_HUMAN
AccessionPrimary (citable) accession number: P35610
Secondary accession number(s): A6NC40 expand/collapse secondary AC list , A9Z1V7, Q5T0X4, Q8N1E4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 25, 2003
Last modified: January 25, 2012
This is version 113 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

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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