SOAT1_HUMAN
ID SOAT1_HUMAN Reviewed; 550 AA.
AC P35610; A6NC40; A8K3P4; A9Z1V7; B4DU95; Q5T0X4; Q8N1E4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Sterol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.26 {ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:18480028, ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614};
DE AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 1 {ECO:0000303|PubMed:11294643, ECO:0000303|PubMed:32433613, ECO:0000303|PubMed:32433614, ECO:0000303|PubMed:9020103};
DE Short=ACAT-1 {ECO:0000303|PubMed:9020103};
DE AltName: Full=Cholesterol acyltransferase 1;
GN Name=SOAT1 {ECO:0000312|HGNC:HGNC:11177};
GN Synonyms=ACACT, ACACT1, ACAT {ECO:0000303|PubMed:9020103},
GN ACAT1 {ECO:0000303|PubMed:11294643, ECO:0000303|PubMed:32433613,
GN ECO:0000303|PubMed:32433614}, SOAT, STAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-526.
RC TISSUE=Macrophage;
RX PubMed=8407899; DOI=10.1016/s0021-9258(19)36846-2;
RA Chang C.C.Y., Huh H.Y., Cadigan K.M., Chang T.-Y.;
RT "Molecular cloning and functional expression of human acyl-coenzyme
RT A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells.";
RL J. Biol. Chem. 268:20747-20755(1993).
RN [2]
RP SEQUENCE REVISION TO 207.
RA Chang C.C.Y., Chang T.-Y.;
RL Submitted (MAY-1999) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9020103; DOI=10.1074/jbc.272.7.3980;
RA Yang H., Cromley D., Wang H., Billheimer J.T., Sturley S.L.;
RT "Functional expression of a cDNA to human acyl-coenzyme A:cholesterol
RT acyltransferase in yeast. Species-dependent substrate specificity and
RT inhibitor sensitivity.";
RL J. Biol. Chem. 272:3980-3985(1997).
RN [8]
RP PRELIMINARY TOPOLOGY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10438503; DOI=10.1074/jbc.274.33.23276;
RA Lin S., Cheng D., Liu M.S., Chen J., Chang T.-Y.;
RT "Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum
RT contains seven transmembrane domains.";
RL J. Biol. Chem. 274:23276-23285(1999).
RN [9]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11294643; DOI=10.1021/bi0022947;
RA Seo T., Oelkers P.M., Giattina M.R., Worgall T.S., Sturley S.L.,
RA Deckelbaum R.J.;
RT "Differential modulation of ACAT1 and ACAT2 transcription and activity by
RT long chain free fatty acids in cultured cells.";
RL Biochemistry 40:4756-4762(2001).
RN [10]
RP SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, DISULFIDE BOND, MUTAGENESIS OF
RP SER-269 AND HIS-460, AND FUNCTION.
RX PubMed=16154994; DOI=10.1074/jbc.m508384200;
RA Guo Z.Y., Lin S., Heinen J.A., Chang C.C., Chang T.Y.;
RT "The active site His-460 of human acyl-coenzyme A:cholesterol
RT acyltransferase 1 resides in a hitherto undisclosed transmembrane domain.";
RL J. Biol. Chem. 280:37814-37826(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF HIS-386 AND
RP HIS-460.
RX PubMed=16647063; DOI=10.1016/j.febslet.2006.04.035;
RA An S., Cho K.H., Lee W.S., Lee J.O., Paik Y.K., Jeong T.S.;
RT "A critical role for the histidine residues in the catalytic function of
RT acyl-CoA:cholesterol acyltransferase catalysis: evidence for catalytic
RT difference between ACAT1 and ACAT2.";
RL FEBS Lett. 580:2741-2749(2006).
RN [12]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-400; SER-456;
RP HIS-460 AND TYR-518.
RX PubMed=18480028; DOI=10.1194/jlr.m800131-jlr200;
RA Das A., Davis M.A., Rudel L.L.;
RT "Identification of putative active site residues of ACAT enzymes.";
RL J. Lipid Res. 49:1770-1781(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP INTERACTION WITH UBIAD1.
RX PubMed=23169578; DOI=10.1002/humu.22230;
RA Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y.,
RA Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G.,
RA Andresson T., Kruth H.S., Okano T., Dean M.;
RT "The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol
RT metabolic enzymes.";
RL Hum. Mutat. 34:317-329(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP FUNCTION.
RX PubMed=32944968; DOI=10.15252/embj.2020106057;
RA Wang S., Li W., Hui H., Tiwari S.K., Zhang Q., Croker B.A., Rawlings S.,
RA Smith D., Carlin A.F., Rana T.M.;
RT "Cholesterol 25-Hydroxylase inhibits SARS-CoV-2 and other coronaviruses by
RT depleting membrane cholesterol.";
RL EMBO J. 39:e106057-e106057(2020).
RN [17] {ECO:0007744|PDB:6P2J, ECO:0007744|PDB:6P2P}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH
RP (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-262;
RP PHE-263; LEU-306; PHE-367; TRP-407; ASN-415; TRP-420; ASN-421; HIS-425;
RP LEU-428; TYR-429; LYS-445; 452-VAL--SER-456; 452-VAL-PHE-453; SER-456;
RP HIS-460; 504-TRP--PHE-508 AND LEU-507.
RX PubMed=32433614; DOI=10.1038/s41586-020-2290-0;
RA Qian H., Zhao X., Yan R., Yao X., Gao S., Sun X., Du X., Yang H.,
RA Wong C.C.L., Yan N.;
RT "Structural basis for catalysis and substrate specificity of human ACAT1.";
RL Nature 581:333-338(2020).
RN [18] {ECO:0007744|PDB:6VUM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) IN COMPLEX WITH
RP NEVANIMIBE; CHOLESTEROL AND (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF
RP ARG-418; ASN-421; HIS-425; LYS-445 AND HIS-460.
RX PubMed=32433613; DOI=10.1038/s41586-020-2295-8;
RA Long T., Sun Y., Hassan A., Qi X., Li X.;
RT "Structure of nevanimibe-bound tetrameric human ACAT1.";
RL Nature 581:339-343(2020).
CC -!- FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters,
CC which are less soluble in membranes than cholesterol (PubMed:16154994,
CC PubMed:16647063, PubMed:9020103, PubMed:32433614, PubMed:32433613,
CC PubMed:32944968). Plays a role in lipoprotein assembly and dietary
CC cholesterol absorption (PubMed:16154994, PubMed:9020103). Utilizes
CC oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows
CC a higher activity towards an acyl-CoA substrate with a double bond at
CC the delta-9 position (9Z) than towards saturated acyl-CoA or an
CC unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11
CC (11Z) positions (PubMed:11294643, PubMed:32433614).
CC {ECO:0000269|PubMed:11294643, ECO:0000269|PubMed:16154994,
CC ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:32433613,
CC ECO:0000269|PubMed:32433614, ECO:0000269|PubMed:32944968,
CC ECO:0000269|PubMed:9020103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA;
CC Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26;
CC Evidence={ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:18480028,
CC ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817;
CC Evidence={ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:18480028,
CC ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA;
CC Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342;
CC Evidence={ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:18480028,
CC ECO:0000269|PubMed:32433613, ECO:0000269|PubMed:32433614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730;
CC Evidence={ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:32433613,
CC ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:18480028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-
CC octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:11294643, ECO:0000269|PubMed:32433614,
CC ECO:0000269|PubMed:9020103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437;
CC Evidence={ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:11294643,
CC ECO:0000305|PubMed:9020103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + hexadecanoyl-CoA = cholesteryl hexadecanoate +
CC CoA; Xref=Rhea:RHEA:42792, ChEBI:CHEBI:3663, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:32433614, ECO:0000269|PubMed:9020103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793;
CC Evidence={ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:9020103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + octadecanoyl-CoA = cholesteryl octadecanoate +
CC CoA; Xref=Rhea:RHEA:42812, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:82750;
CC Evidence={ECO:0000269|PubMed:32433614, ECO:0000269|PubMed:9020103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813;
CC Evidence={ECO:0000269|PubMed:32433614, ECO:0000305|PubMed:9020103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + cholesterol = cholesteryl
CC (9Z,12Z)-octadecadienoate + CoA; Xref=Rhea:RHEA:42796,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:41509, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383; Evidence={ECO:0000269|PubMed:9020103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797;
CC Evidence={ECO:0000305|PubMed:9020103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol =
CC cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA;
CC Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:82751;
CC Evidence={ECO:0000269|PubMed:9020103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817;
CC Evidence={ECO:0000305|PubMed:9020103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + cholesterol = cholesteryl (9Z)-
CC hexadecenoate + CoA; Xref=Rhea:RHEA:64320, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:84323;
CC Evidence={ECO:0000269|PubMed:32433614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321;
CC Evidence={ECO:0000269|PubMed:32433614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-octadecenoyl-CoA + cholesterol = cholesteryl (11Z)-
CC octadecenoate + CoA; Xref=Rhea:RHEA:64324, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:75121, ChEBI:CHEBI:88768;
CC Evidence={ECO:0000269|PubMed:32433614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325;
CC Evidence={ECO:0000269|PubMed:32433614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z)-octadecenoyl-CoA + cholesterol = cholesteryl (7Z)-
CC octadecenoate + CoA; Xref=Rhea:RHEA:64328, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:152049, ChEBI:CHEBI:152050;
CC Evidence={ECO:0000269|PubMed:32433614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329;
CC Evidence={ECO:0000269|PubMed:32433614};
CC -!- ACTIVITY REGULATION: Cholesterol O-acyltransferase activity is
CC inhibited by nevanimibe. {ECO:0000269|PubMed:32433613}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.2 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32433614};
CC KM=20.0 uM for (11Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32433614};
CC KM=16.0 uM for (7Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32433614};
CC KM=50.3 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32433614};
CC KM=20.6 uM for (9Z)-hexadecenoyl-CoA {ECO:0000269|PubMed:32433614};
CC KM=21.1 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:32433614};
CC Vmax=123.1 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC Vmax=96.7 nmol/min/mg enzyme with (11Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC Vmax=66.7 nmol/min/mg enzyme with (7Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC Vmax=92.8 nmol/min/mg enzyme with octadecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC Vmax=97.6 nmol/min/mg enzyme with (9Z)-hexadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC Vmax=86.8 nmol/min/mg enzyme with hexadecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433614};
CC -!- SUBUNIT: Homotetramer; composed of two homodimers (PubMed:32433614,
CC PubMed:32433613). Interacts with UBIAD1 (PubMed:23169578).
CC {ECO:0000269|PubMed:23169578, ECO:0000269|PubMed:32433613,
CC ECO:0000269|PubMed:32433614}.
CC -!- INTERACTION:
CC P35610; P54274: TERF1; NbExp=2; IntAct=EBI-6621955, EBI-710997;
CC P35610; Q9Y5Z9: UBIAD1; NbExp=2; IntAct=EBI-6621955, EBI-2819725;
CC P35610-1; P35610-1: SOAT1; NbExp=4; IntAct=EBI-6621997, EBI-6621997;
CC P35610-1; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-6621997, EBI-2819725;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10438503, ECO:0000269|PubMed:16154994}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:32433613,
CC ECO:0000269|PubMed:32433614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35610-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35610-2; Sequence=VSP_045331;
CC Name=3;
CC IsoId=P35610-3; Sequence=VSP_045330;
CC -!- INDUCTION: Highly activated by the presence of cholesterol.
CC {ECO:0000269|PubMed:10438503}.
CC -!- DOMAIN: Each protomer consists of 9 transmembrane segments, which
CC enclose a cytosolic tunnel and a transmembrane tunnel that converge at
CC the predicted catalytic site: acyl-CoA enters the active site through
CC the cytosolic tunnel, whereas cholesterol enters from the side through
CC the transmembrane tunnel. {ECO:0000305|PubMed:32433614}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; L21934; AAC37532.2; -; mRNA.
DR EMBL; AK290659; BAF83348.1; -; mRNA.
DR EMBL; AK300551; BAG62257.1; -; mRNA.
DR EMBL; AL451075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91043.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91044.1; -; Genomic_DNA.
DR EMBL; BC028940; AAH28940.1; -; mRNA.
DR CCDS; CCDS1330.1; -. [P35610-1]
DR CCDS; CCDS58047.1; -. [P35610-2]
DR CCDS; CCDS58048.1; -. [P35610-3]
DR PIR; A59038; A48026.
DR RefSeq; NP_001239440.1; NM_001252511.1. [P35610-2]
DR RefSeq; NP_001239441.1; NM_001252512.1. [P35610-3]
DR RefSeq; NP_003092.4; NM_003101.5. [P35610-1]
DR RefSeq; XP_011508213.1; XM_011509911.1. [P35610-1]
DR PDB; 6L47; EM; 3.50 A; A/B=66-550.
DR PDB; 6L48; EM; 3.50 A; A/B=66-550.
DR PDB; 6P2J; EM; 3.00 A; A/B=1-550.
DR PDB; 6P2P; EM; 3.10 A; A/B/C/D=1-550.
DR PDB; 6VUM; EM; 3.67 A; A/B/C/D=1-550.
DR PDBsum; 6L47; -.
DR PDBsum; 6L48; -.
DR PDBsum; 6P2J; -.
DR PDBsum; 6P2P; -.
DR PDBsum; 6VUM; -.
DR AlphaFoldDB; P35610; -.
DR SMR; P35610; -.
DR BioGRID; 112529; 300.
DR IntAct; P35610; 182.
DR MINT; P35610; -.
DR STRING; 9606.ENSP00000356591; -.
DR BindingDB; P35610; -.
DR ChEMBL; CHEMBL2782; -.
DR DrugBank; DB00973; Ezetimibe.
DR DrugBank; DB01094; Hesperetin.
DR DrugBank; DB09539; Omega-3-acid ethyl esters.
DR DrugCentral; P35610; -.
DR SwissLipids; SLP:000000702; -.
DR GlyGen; P35610; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P35610; -.
DR PhosphoSitePlus; P35610; -.
DR SwissPalm; P35610; -.
DR BioMuta; SOAT1; -.
DR DMDM; 33302623; -.
DR EPD; P35610; -.
DR jPOST; P35610; -.
DR MassIVE; P35610; -.
DR MaxQB; P35610; -.
DR PaxDb; P35610; -.
DR PeptideAtlas; P35610; -.
DR PRIDE; P35610; -.
DR ProteomicsDB; 1856; -.
DR ProteomicsDB; 5164; -.
DR ProteomicsDB; 55101; -. [P35610-1]
DR Antibodypedia; 4027; 182 antibodies from 29 providers.
DR DNASU; 6646; -.
DR Ensembl; ENST00000367619.8; ENSP00000356591.3; ENSG00000057252.13. [P35610-1]
DR Ensembl; ENST00000539888.5; ENSP00000441356.1; ENSG00000057252.13. [P35610-3]
DR Ensembl; ENST00000540564.5; ENSP00000445315.1; ENSG00000057252.13. [P35610-2]
DR GeneID; 6646; -.
DR KEGG; hsa:6646; -.
DR MANE-Select; ENST00000367619.8; ENSP00000356591.3; NM_003101.6; NP_003092.4.
DR UCSC; uc001gml.4; human. [P35610-1]
DR CTD; 6646; -.
DR DisGeNET; 6646; -.
DR GeneCards; SOAT1; -.
DR HGNC; HGNC:11177; SOAT1.
DR HPA; ENSG00000057252; Tissue enriched (adrenal).
DR MIM; 102642; gene.
DR neXtProt; NX_P35610; -.
DR OpenTargets; ENSG00000057252; -.
DR PharmGKB; PA36015; -.
DR VEuPathDB; HostDB:ENSG00000057252; -.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_031845_1_0_1; -.
DR InParanoid; P35610; -.
DR OMA; PAVWRCY; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; P35610; -.
DR TreeFam; TF105767; -.
DR BioCyc; MetaCyc:HS00706-MON; -.
DR BRENDA; 2.3.1.26; 2681.
DR PathwayCommons; P35610; -.
DR Reactome; R-HSA-8964038; LDL clearance.
DR SABIO-RK; P35610; -.
DR SignaLink; P35610; -.
DR SIGNOR; P35610; -.
DR BioGRID-ORCS; 6646; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; SOAT1; human.
DR GeneWiki; SOAT1; -.
DR GenomeRNAi; 6646; -.
DR Pharos; P35610; Tchem.
DR PRO; PR:P35610; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P35610; protein.
DR Bgee; ENSG00000057252; Expressed in adrenal tissue and 182 other tissues.
DR ExpressionAtlas; P35610; baseline and differential.
DR Genevisible; P35610; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0034736; F:cholesterol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004772; F:sterol O-acyltransferase activity; IDA:MGI.
DR GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0034435; P:cholesterol esterification; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; TAS:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
DR GO; GO:0010878; P:cholesterol storage; IMP:BHF-UCL.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:BHF-UCL.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR InterPro; IPR030687; Sterol_acyltranf_meta.
DR PANTHER; PTHR10408; PTHR10408; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR PIRSF; PIRSF500230; Sterol_acyltranf_ACAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Cholesterol metabolism; Disulfide bond; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..550
FT /note="Sterol O-acyltransferase 1"
FT /id="PRO_0000207640"
FT TOPO_DOM 1..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..160
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 161..180
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..206
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 207..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..244
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 245..252
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..276
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 277..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..352
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 353..369
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..395
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 396..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 444..468
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 469..474
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 475..490
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0000305|PubMed:32433613, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 491..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..528
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT TOPO_DOM 529..550
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 403..409
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000303|PubMed:32433614"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /evidence="ECO:0000269|PubMed:16154994,
FT ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6VUM"
FT BINDING 137
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0007744|PDB:6VUM"
FT BINDING 415
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0007744|PDB:6P2P"
FT BINDING 418
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0007744|PDB:6VUM"
FT BINDING 421
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433614,
FT ECO:0007744|PDB:6P2J"
FT BINDING 425
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT BINDING 433
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0007744|PDB:6VUM"
FT BINDING 445
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614, ECO:0007744|PDB:6P2J,
FT ECO:0007744|PDB:6P2P, ECO:0007744|PDB:6VUM"
FT BINDING 456
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0007744|PDB:6VUM"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 528..546
FT /evidence="ECO:0000269|PubMed:16154994"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045330"
FT VAR_SEQ 1..59
FT /note="MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKI
FT KLTAEAE -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045331"
FT VARIANT 526
FT /note="Q -> R (in dbSNP:rs13306731)"
FT /evidence="ECO:0000269|PubMed:8407899"
FT /id="VAR_052031"
FT MUTAGEN 262
FT /note="R->A: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 263
FT /note="F->A: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 269
FT /note="S->A,T: Nearly normal expression and enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:16154994"
FT MUTAGEN 269
FT /note="S->L: No expression nor activity."
FT /evidence="ECO:0000269|PubMed:16154994"
FT MUTAGEN 306
FT /note="L->N: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 367
FT /note="F->A: Abolished homodimerization; when associated
FT with 504-A--A-508."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 386
FT /note="H->A: Abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16647063"
FT MUTAGEN 400
FT /note="D->N: Low expression, loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18480028"
FT MUTAGEN 407
FT /note="W->A: Almost abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 415
FT /note="N->G: Reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 418
FT /note="R->A: Reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433613"
FT MUTAGEN 420
FT /note="W->A: Almost abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 421
FT /note="N->A: Almost abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614"
FT MUTAGEN 425
FT /note="H->A: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614"
FT MUTAGEN 428
FT /note="L->Q: Almost abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 429
FT /note="Y->A: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 445
FT /note="K->A: Reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614"
FT MUTAGEN 452..456
FT /note="VFAVS->QFAVQ: In QQ mutant; almost abolished
FT cholesterol O-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 452..453
FT /note="VF->AA: Almost abolished cholesterol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 456
FT /note="S->A: Abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:18480028,
FT ECO:0000269|PubMed:32433614"
FT MUTAGEN 460
FT /note="H->A,C,N: Abolished cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16154994,
FT ECO:0000269|PubMed:16647063, ECO:0000269|PubMed:32433613,
FT ECO:0000269|PubMed:32433614"
FT MUTAGEN 504..508
FT /note="WTSLF->ATSLA: Abolished homodimerization; when
FT associated with A-367."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 507
FT /note="L->A: Strongly reduced cholesterol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433614"
FT MUTAGEN 518
FT /note="Y->F: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18480028"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 136..164
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 181..208
FT /evidence="ECO:0007829|PDB:6P2J"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 218..245
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 250..272
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6P2J"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6L47"
FT HELIX 320..344
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6P2J"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 445..468
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:6P2J"
FT HELIX 497..523
FT /evidence="ECO:0007829|PDB:6P2J"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:6P2J"
SQ SEQUENCE 550 AA; 64735 MW; 5F5ACD525D541DEE CRC64;
MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK KIKLTAEAEE
LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL EGEKNNHRAK DLRAPPEQGK
IFIARRSLLD ELLEVDHIRT IYHMFIALLI LFILSTLVVD YIDEGRLVLE FSLLSYAFGK
FPTVVWTWWI MFLSTFSVPY FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT
YVVLAYTLPP ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR NIKQEPFSAR
VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW
NVVVHDWLYY YAYKDFLWFF SKRFKSAAML AVFAVSAVVH EYALAVCLSF FYPVLFVLFM
FFGMAFNFIV NDSRKKPIWN VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR
PRSWTCRYVF
