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O75908

- SOAT2_HUMAN

UniProt

O75908 - SOAT2_HUMAN

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Protein

Sterol O-acyltransferase 2

Gene

SOAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 activityi

Acyl-CoA + cholesterol = CoA + cholesterol ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei434 – 4341Sequence Analysis

GO - Molecular functioni

  1. cholesterol binding Source: BHF-UCL
  2. cholesterol O-acyltransferase activity Source: BHF-UCL
  3. fatty-acyl-CoA binding Source: BHF-UCL
  4. transferase activity, transferring acyl groups Source: ProtInc

GO - Biological processi

  1. cholesterol efflux Source: BHF-UCL
  2. cholesterol esterification Source: BHF-UCL
  3. cholesterol homeostasis Source: BHF-UCL
  4. cholesterol metabolic process Source: BHF-UCL
  5. intestinal cholesterol absorption Source: BHF-UCL
  6. macrophage derived foam cell differentiation Source: BHF-UCL
  7. very-low-density lipoprotein particle assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi2.3.1.26. 2681.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SOAT2
Synonyms:ACACT2, ACAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11178. SOAT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 122122CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei123 – 14119HelicalSequence AnalysisAdd
BLAST
Topological domaini142 – 16019LumenalSequence AnalysisAdd
BLAST
Transmembranei161 – 17919HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 20021CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei201 – 21919HelicalSequence AnalysisAdd
BLAST
Topological domaini220 – 340121LumenalSequence AnalysisAdd
BLAST
Transmembranei341 – 36323HelicalSequence AnalysisAdd
BLAST
Topological domaini364 – 475112CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei476 – 49419HelicalSequence AnalysisAdd
BLAST
Topological domaini495 – 52228LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. brush border Source: BHF-UCL
  2. endoplasmic reticulum Source: BHF-UCL
  3. endoplasmic reticulum membrane Source: BHF-UCL
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Sterol O-acyltransferase 2PRO_0000207645Add
BLAST

Proteomic databases

PaxDbiO75908.
PRIDEiO75908.

PTM databases

PhosphoSiteiO75908.

Expressioni

Tissue specificityi

Expression seems confined in hepatocytes and enterocytes.1 Publication

Gene expression databases

BgeeiO75908.
CleanExiHS_ACAT2.
HS_SOAT2.
ExpressionAtlasiO75908. baseline and differential.
GenevestigatoriO75908.

Organism-specific databases

HPAiHPA049462.

Interactioni

Subunit structurei

May form homo- or heterodimers.By similarity

Protein-protein interaction databases

BioGridi114015. 2 interactions.
STRINGi9606.ENSP00000301466.

Structurei

3D structure databases

ProteinModelPortaliO75908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5056.
GeneTreeiENSGT00530000063122.
HOGENOMiHOG000020782.
HOVERGENiHBG058198.
InParanoidiO75908.
KOiK00637.
OMAiLMEVQHF.
PhylomeDBiO75908.
TreeFamiTF315226.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75908-1) [UniParc]FASTAAdd to Basket

Also known as: ACAD2a

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.

« Hide

        10         20         30         40         50
MEPGGARLRL QRTEGLGGER ERQPCGDGNT ETHRAPDLVQ WTRHMEAVKA
60 70 80 90 100
QLLEQAQGQL RELLDRAMRE AIQSYPSQDK PLPPPPPGSL SRTQEPSLGK
110 120 130 140 150
QKVFIIRKSL LDELMEVQHF RTIYHMFIAG LCVFIISTLA IDFIDEGRLL
160 170 180 190 200
LEFDLLIFSF GQLPLALVTW VPMFLSTLLA PYQALRLWAR GTWTQATGLG
210 220 230 240 250
CALLAAHAVV LCALPVHVAV EHQLPPASRC VLVFEQVRFL MKSYSFLREA
260 270 280 290 300
VPGTLRARRG EGIQAPSFSS YLYFLFCPTL IYRETYPRTP YVRWNYVAKN
310 320 330 340 350
FAQALGCVLY ACFILGRLCV PVFANMSREP FSTRALVLSI LHATLPGIFM
360 370 380 390 400
LLLIFFAFLH CWLNAFAEML RFGDRMFYRD WWNSTSFSNY YRTWNVVVHD
410 420 430 440 450
WLYSYVYQDG LRLLGARARG VAMLGVFLVS AVAHEYIFCF VLGFFYPVML
460 470 480 490 500
ILFLVIGGML NFMMHDQRTG PAWNVLMWTM LFLGQGIQVS LYCQEWYARR
510 520
HCPLPQATFW GLVTPRSWSC HT
Length:522
Mass (Da):59,896
Last modified:November 1, 1998 - v1
Checksum:iEEAC2DB569FFE729
GO
Isoform 2 (identifier: O75908-2) [UniParc]FASTAAdd to Basket

Also known as: ACAD2b

The sequence of this isoform differs from the canonical sequence as follows:
     93-112: Missing.

Note: Lower enzymatic activity

Show »
Length:502
Mass (Da):57,614
Checksum:i4E8DA0CFFF4E2688
GO
Isoform 3 (identifier: O75908-3) [UniParc]FASTAAdd to Basket

Also known as: ACAD2c

The sequence of this isoform differs from the canonical sequence as follows:
     93-148: Missing.
     236-261: Missing.

Note: Lower enzymatic activity

Show »
Length:440
Mass (Da):50,351
Checksum:iC891C005392C572C
GO
Isoform 4 (identifier: O75908-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-310: TPYVRWNYVAKNFAQALGCVLY → PWDVCSMPASSWAASVFLSLPT
     311-522: Missing.

Note: No experimental confirmation available

Show »
Length:310
Mass (Da):34,882
Checksum:iA5C0D66A8ECCA6EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → P in AAK48829. (PubMed:11401500)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141E → G.
Corresponds to variant rs9658625 [ dbSNP | Ensembl ].
VAR_020373
Natural varianti254 – 2541T → I.2 Publications
Corresponds to variant rs2272296 [ dbSNP | Ensembl ].
VAR_020374

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 14856Missing in isoform 3. 1 PublicationVSP_057158Add
BLAST
Alternative sequencei93 – 11220Missing in isoform 2. 1 PublicationVSP_057159Add
BLAST
Alternative sequencei236 – 26126Missing in isoform 3. 1 PublicationVSP_057160Add
BLAST
Alternative sequencei289 – 31022TPYVR…GCVLY → PWDVCSMPASSWAASVFLSL PT in isoform 4. 1 PublicationVSP_057161Add
BLAST
Alternative sequencei311 – 522212Missing in isoform 4. 1 PublicationVSP_057162Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AC073573 Genomic DNA. No translation available.
BC096090 mRNA. Translation: AAH96090.1.
BC096091 mRNA. Translation: AAH96091.1.
BC096092 mRNA. Translation: AAH96092.1.
BC099626 mRNA. Translation: AAH99626.1.
CCDSiCCDS8847.1.
RefSeqiNP_003569.1. NM_003578.3.
UniGeneiHs.656544.

Genome annotation databases

EnsembliENST00000301466; ENSP00000301466; ENSG00000167780.
GeneIDi8435.
KEGGihsa:8435.
UCSCiuc001sbv.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
AC073573 Genomic DNA. No translation available.
BC096090 mRNA. Translation: AAH96090.1 .
BC096091 mRNA. Translation: AAH96091.1 .
BC096092 mRNA. Translation: AAH96092.1 .
BC099626 mRNA. Translation: AAH99626.1 .
CCDSi CCDS8847.1.
RefSeqi NP_003569.1. NM_003578.3.
UniGenei Hs.656544.

3D structure databases

ProteinModelPortali O75908.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114015. 2 interactions.
STRINGi 9606.ENSP00000301466.

Chemistry

BindingDBi O75908.
ChEMBLi CHEMBL4465.
DrugBanki DB01094. Hesperetin.

PTM databases

PhosphoSitei O75908.

Proteomic databases

PaxDbi O75908.
PRIDEi O75908.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301466 ; ENSP00000301466 ; ENSG00000167780 .
GeneIDi 8435.
KEGGi hsa:8435.
UCSCi uc001sbv.3. human.

Organism-specific databases

CTDi 8435.
GeneCardsi GC12P053497.
HGNCi HGNC:11178. SOAT2.
HPAi HPA049462.
MIMi 601311. gene.
neXtProti NX_O75908.
PharmGKBi PA36016.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5056.
GeneTreei ENSGT00530000063122.
HOGENOMi HOG000020782.
HOVERGENi HBG058198.
InParanoidi O75908.
KOi K00637.
OMAi LMEVQHF.
PhylomeDBi O75908.
TreeFami TF315226.

Enzyme and pathway databases

BRENDAi 2.3.1.26. 2681.

Miscellaneous databases

GeneWikii SOAT2.
GenomeRNAii 8435.
NextBioi 31558.
PROi O75908.
SOURCEi Search...

Gene expression databases

Bgeei O75908.
CleanExi HS_ACAT2.
HS_SOAT2.
ExpressionAtlasi O75908. baseline and differential.
Genevestigatori O75908.

Family and domain databases

InterProi IPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view ]
PANTHERi PTHR10408. PTHR10408. 1 hit.
Pfami PF03062. MBOAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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 finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 4), VARIANTS GLY-14 AND ILE-254.
  7. "Two human ACAT2 mRNA variants produced by alternative splicing and coding for novel isoenzymes."
    Yao X.M., Wang C.H., Song B.L., Yang X.Y., Wang Z.Z., Qi W., Lin Z.X., Chang C.C., Chang T.Y., Li B.L.
    Acta Biochim. Biophys. Sin. 37:797-806(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).

Entry informationi

Entry nameiSOAT2_HUMAN
AccessioniPrimary (citable) accession number: O75908
Secondary accession number(s): F5H7W4
, I6L9H9, Q4VB99, Q4VBA1, Q96TD4, Q9UNR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3