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Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)

 SOAT2_HUMAN             Reviewed;         522 AA.
O75908; F5H7W4; I6L9H9; Q4VB99; Q4VBA1; Q96TD4; Q9UNR2;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
20-JUN-2018, entry version 145.
RecName: Full=Sterol O-acyltransferase 2;
EC=2.3.1.26;
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 2;
Short=ACAT-2;
AltName: Full=Cholesterol acyltransferase 2;
Name=SOAT2; Synonyms=ACACT2, ACAT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9756920; DOI=10.1074/jbc.273.41.26765;
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.;
"Characterization of two human genes encoding acyl coenzyme
A:cholesterol acyltransferase-related enzymes.";
J. Biol. Chem. 273:26765-26771(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-254.
TISSUE=Intestine;
PubMed=10846185; DOI=10.1074/jbc.M003927200;
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.;
"Immunological quantitation and localization of ACAT-1 and ACAT-2 in
human liver and small intestine.";
J. Biol. Chem. 275:28083-28092(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11325614; DOI=10.1016/S1388-1981(01)00106-8;
Katsuren K., Tamura T., Arashiro R., Takata K., Matsuura T.,
Niikawa N., Ohta T.;
"Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-
2) gene and its relation to dyslipidemia.";
Biochim. Biophys. Acta 1531:230-240(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11401500; DOI=10.1006/bbrc.2001.4612;
Song B.L., Qi W., Yang X.Y., Chang C.C.Y., Zhu J.Q., Chang T.Y.,
Li B.L.;
"Organization of human ACAT-2 gene and its cell-type-specific promoter
activity.";
Biochem. Biophys. Res. Commun. 282:580-588(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND
VARIANTS GLY-14 AND ILE-254.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
PubMed=16331323; DOI=10.1111/j.1745-7270.2005.00118.x;
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.;
"Two human ACAT2 mRNA variants produced by alternative splicing and
coding for novel isoenzymes.";
Acta Biochim. Biophys. Sin. 37:797-806(2005).
-!- 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: May form homo- or heterodimers. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=ACAD2a;
IsoId=O75908-1; Sequence=Displayed;
Name=2; Synonyms=ACAD2b;
IsoId=O75908-2; Sequence=VSP_057159;
Note=Lower enzymatic activity.;
Name=3; Synonyms=ACAD2c;
IsoId=O75908-3; Sequence=VSP_057158, VSP_057160;
Note=Lower enzymatic activity.;
Name=4;
IsoId=O75908-4; Sequence=VSP_057161, VSP_057162;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression seems confined in hepatocytes and
enterocytes. {ECO:0000269|PubMed:16331323}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
Sterol o-acyltransferase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF059203; AAC63998.1; -; mRNA.
EMBL; AF099031; AAC78335.2; -; mRNA.
EMBL; AF331516; AAK18275.1; -; Genomic_DNA.
EMBL; AF331502; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331503; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331504; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331505; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331506; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331507; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331508; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331509; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331510; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331511; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331512; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331513; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331514; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331515; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF332858; AAK48829.1; -; Genomic_DNA.
EMBL; AF332857; AAK48829.1; JOINED; Genomic_DNA.
EMBL; AC073573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC096090; AAH96090.1; -; mRNA.
EMBL; BC096091; AAH96091.1; -; mRNA.
EMBL; BC096092; AAH96092.1; -; mRNA.
EMBL; BC099626; AAH99626.1; -; mRNA.
CCDS; CCDS8847.1; -. [O75908-1]
RefSeq; NP_003569.1; NM_003578.3. [O75908-1]
UniGene; Hs.656544; -.
ProteinModelPortal; O75908; -.
BioGrid; 114015; 1.
IntAct; O75908; 3.
MINT; O75908; -.
STRING; 9606.ENSP00000301466; -.
BindingDB; O75908; -.
ChEMBL; CHEMBL4465; -.
DrugBank; DB01094; Hesperetin.
SwissLipids; SLP:000001262; -. [O75908-1]
iPTMnet; O75908; -.
PhosphoSitePlus; O75908; -.
SwissPalm; O75908; -.
BioMuta; SOAT2; -.
PaxDb; O75908; -.
PeptideAtlas; O75908; -.
PRIDE; O75908; -.
ProteomicsDB; 50258; -.
Ensembl; ENST00000301466; ENSP00000301466; ENSG00000167780. [O75908-1]
Ensembl; ENST00000542365; ENSP00000442234; ENSG00000167780. [O75908-4]
GeneID; 8435; -.
KEGG; hsa:8435; -.
UCSC; uc001sbv.4; human. [O75908-1]
CTD; 8435; -.
DisGeNET; 8435; -.
EuPathDB; HostDB:ENSG00000167780.11; -.
GeneCards; SOAT2; -.
HGNC; HGNC:11178; SOAT2.
MIM; 601311; gene.
neXtProt; NX_O75908; -.
OpenTargets; ENSG00000167780; -.
PharmGKB; PA36016; -.
eggNOG; KOG0380; Eukaryota.
eggNOG; COG5056; LUCA.
GeneTree; ENSGT00530000063122; -.
HOGENOM; HOG000020782; -.
HOVERGEN; HBG058198; -.
InParanoid; O75908; -.
KO; K00637; -.
OMA; DRAMWEA; -.
OrthoDB; EOG091G0991; -.
PhylomeDB; O75908; -.
TreeFam; TF315226; -.
BRENDA; 2.3.1.26; 2681.
Reactome; R-HSA-8964038; LDL clearance.
GeneWiki; SOAT2; -.
GenomeRNAi; 8435; -.
PRO; PR:O75908; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167780; -.
CleanEx; HS_ACAT2; -.
CleanEx; HS_SOAT2; -.
ExpressionAtlas; O75908; baseline and differential.
Genevisible; O75908; HS.
GO; GO:0005903; C:brush border; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0034736; F:cholesterol O-acyltransferase activity; IDA:BHF-UCL.
GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:ProtInc.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0034435; P:cholesterol esterification; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; TAS:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0010742; P:macrophage derived foam cell differentiation; TAS:BHF-UCL.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:BHF-UCL.
InterPro; IPR004299; MBOAT_fam.
InterPro; IPR014371; Oat_ACAT_DAG_ARE.
InterPro; IPR030687; Sterol_acyltranf_meta.
PANTHER; PTHR10408; PTHR10408; 1.
Pfam; PF03062; MBOAT; 1.
PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PIRSF; PIRSF500230; Sterol_acyltranf_ACAT; 1.
2: Evidence at transcript level;
Acyltransferase; Alternative splicing; Cholesterol metabolism;
Complete proteome; Endoplasmic reticulum; Lipid metabolism; Membrane;
Polymorphism; Reference proteome; Steroid metabolism;
Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 522 Sterol O-acyltransferase 2.
/FTId=PRO_0000207645.
TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.
TRANSMEM 123 141 Helical. {ECO:0000255}.
TOPO_DOM 142 160 Lumenal. {ECO:0000255}.
TRANSMEM 161 179 Helical. {ECO:0000255}.
TOPO_DOM 180 200 Cytoplasmic. {ECO:0000255}.
TRANSMEM 201 219 Helical. {ECO:0000255}.
TOPO_DOM 220 340 Lumenal. {ECO:0000255}.
TRANSMEM 341 363 Helical. {ECO:0000255}.
TOPO_DOM 364 475 Cytoplasmic. {ECO:0000255}.
TRANSMEM 476 494 Helical. {ECO:0000255}.
TOPO_DOM 495 522 Lumenal. {ECO:0000255}.
ACT_SITE 434 434 {ECO:0000255}.
VAR_SEQ 93 148 Missing (in isoform 3).
{ECO:0000269|PubMed:16331323}.
/FTId=VSP_057158.
VAR_SEQ 93 112 Missing (in isoform 2).
{ECO:0000269|PubMed:16331323}.
/FTId=VSP_057159.
VAR_SEQ 236 261 Missing (in isoform 3).
{ECO:0000269|PubMed:16331323}.
/FTId=VSP_057160.
VAR_SEQ 289 310 TPYVRWNYVAKNFAQALGCVLY -> PWDVCSMPASSWAAS
VFLSLPT (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057161.
VAR_SEQ 311 522 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057162.
VARIANT 14 14 E -> G (in dbSNP:rs9658625).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_020373.
VARIANT 254 254 T -> I (in dbSNP:rs2272296).
{ECO:0000269|PubMed:10846185,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_020374.
CONFLICT 22 22 R -> P (in Ref. 4; AAK48829).
{ECO:0000305}.
SEQUENCE 522 AA; 59896 MW; EEAC2DB569FFE729 CRC64;
MEPGGARLRL QRTEGLGGER ERQPCGDGNT ETHRAPDLVQ WTRHMEAVKA QLLEQAQGQL
RELLDRAMRE AIQSYPSQDK PLPPPPPGSL SRTQEPSLGK QKVFIIRKSL LDELMEVQHF
RTIYHMFIAG LCVFIISTLA IDFIDEGRLL LEFDLLIFSF GQLPLALVTW VPMFLSTLLA
PYQALRLWAR GTWTQATGLG CALLAAHAVV LCALPVHVAV EHQLPPASRC VLVFEQVRFL
MKSYSFLREA VPGTLRARRG EGIQAPSFSS YLYFLFCPTL IYRETYPRTP YVRWNYVAKN
FAQALGCVLY ACFILGRLCV PVFANMSREP FSTRALVLSI LHATLPGIFM LLLIFFAFLH
CWLNAFAEML RFGDRMFYRD WWNSTSFSNY YRTWNVVVHD WLYSYVYQDG LRLLGARARG
VAMLGVFLVS AVAHEYIFCF VLGFFYPVML ILFLVIGGML NFMMHDQRTG PAWNVLMWTM
LFLGQGIQVS LYCQEWYARR HCPLPQATFW GLVTPRSWSC HT


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