SOAT1_MOUSE
ID SOAT1_MOUSE Reviewed; 540 AA.
AC Q61263; Q5XK32; Q64180;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sterol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.26 {ECO:0000250|UniProtKB:P35610};
DE AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 1;
DE Short=ACAT-1;
DE AltName: Full=Cholesterol acyltransferase 1;
GN Name=Soat1 {ECO:0000312|MGI:MGI:104665}; Synonyms=Acact;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7592824; DOI=10.1074/jbc.270.44.26192;
RA Uelmen P.J., Oka K., Sullivan M.C., Chang T.-Y., Chang C.C.Y., Chan L.;
RT "Tissue-specific expression and cholesterol regulation of acylcoenzyme
RT A:cholesterol acyltransferase (ACAT) in mice. Molecular cloning of mouse
RT ACAT cDNA, chromosomal localization, and regulation of ACAT in vivo and in
RT vitro.";
RL J. Biol. Chem. 270:26192-26201(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8579615; DOI=10.1006/bbrc.1996.0163;
RA Green S., Steinberg D., Quehenberger O.;
RT "Cloning and expression in Xenopus oocytes of a mouse homologue of the
RT human acylcoenzyme A: cholesterol acyltransferase and its potential role in
RT metabolism of oxidized LDL.";
RL Biochem. Biophys. Res. Commun. 218:924-929(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=11071899; DOI=10.1091/mbc.11.11.3675;
RA Joyce C.W., Shelness G.S., Davis M.A., Lee R.G., Skinner K., Anderson R.A.,
RA Rudel L.L.;
RT "ACAT1 and ACAT2 membrane topology segregates a serine residue essential
RT for activity to opposite sides of the endoplasmic reticulum membrane.";
RL Mol. Biol. Cell 11:3675-3687(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters,
CC which are less soluble in membranes than cholesterol. Plays a role in
CC lipoprotein assembly and dietary cholesterol absorption. 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. {ECO:0000250|UniProtKB:P35610}.
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325;
CC Evidence={ECO:0000250|UniProtKB:P35610};
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:0000250|UniProtKB:P35610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329;
CC Evidence={ECO:0000250|UniProtKB:P35610};
CC -!- SUBUNIT: May form homo- or heterodimers. Interacts with UBIAD1.
CC {ECO:0000250|UniProtKB:P35610}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11071899}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11071899}.
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:0000250|UniProtKB:P35610}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; L42293; AAC42075.1; -; mRNA.
DR EMBL; S81092; AAB36050.1; -; mRNA.
DR EMBL; AK142486; BAE25081.1; -; mRNA.
DR EMBL; AK159393; BAE35047.1; -; mRNA.
DR EMBL; AK159529; BAE35158.1; -; mRNA.
DR EMBL; AK160017; BAE35563.1; -; mRNA.
DR EMBL; BC083092; AAH83092.1; -; mRNA.
DR CCDS; CCDS35743.1; -.
DR PIR; I49454; I49454.
DR RefSeq; NP_033256.2; NM_009230.3.
DR AlphaFoldDB; Q61263; -.
DR SMR; Q61263; -.
DR BioGRID; 203385; 6.
DR IntAct; Q61263; 17.
DR STRING; 10090.ENSMUSP00000140721; -.
DR BindingDB; Q61263; -.
DR ChEMBL; CHEMBL4464; -.
DR iPTMnet; Q61263; -.
DR PhosphoSitePlus; Q61263; -.
DR SwissPalm; Q61263; -.
DR EPD; Q61263; -.
DR MaxQB; Q61263; -.
DR PaxDb; Q61263; -.
DR PRIDE; Q61263; -.
DR ProteomicsDB; 261474; -.
DR Antibodypedia; 4027; 182 antibodies from 29 providers.
DR DNASU; 20652; -.
DR Ensembl; ENSMUST00000051396; ENSMUSP00000058344; ENSMUSG00000026600.
DR Ensembl; ENSMUST00000189661; ENSMUSP00000140721; ENSMUSG00000026600.
DR GeneID; 20652; -.
DR KEGG; mmu:20652; -.
DR UCSC; uc007dcj.1; mouse.
DR CTD; 6646; -.
DR MGI; MGI:104665; Soat1.
DR VEuPathDB; HostDB:ENSMUSG00000026600; -.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_031845_1_0_1; -.
DR InParanoid; Q61263; -.
DR OMA; PAVWRCY; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; Q61263; -.
DR TreeFam; TF105767; -.
DR BRENDA; 2.3.1.26; 3474.
DR Reactome; R-MMU-8964038; LDL clearance.
DR BioGRID-ORCS; 20652; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Soat1; mouse.
DR PRO; PR:Q61263; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61263; protein.
DR Bgee; ENSMUSG00000026600; Expressed in metanephric ureteric bud and 249 other tissues.
DR ExpressionAtlas; Q61263; baseline and differential.
DR Genevisible; Q61263; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0034736; F:cholesterol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0034435; P:cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
DR GO; GO:0010878; P:cholesterol storage; ISO:MGI.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; ISO:MGI.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:MGI.
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 Acyltransferase; Cholesterol metabolism; Disulfide bond;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="Sterol O-acyltransferase 1"
FT /id="PRO_0000207642"
FT TOPO_DOM 1..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..150
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 151..170
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..196
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 197..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..234
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 235..242
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..266
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 267..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 310..342
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 343..359
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 360..385
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 386..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..458
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 459..464
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 465..480
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 481..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 487..518
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 519..540
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 393..399
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 450
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 127
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 405
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 408
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 411
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 415
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 423
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 435
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 446
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT DISULFID 518..536
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT CONFLICT 195
FT /note="R -> P (in Ref. 1; AAC42075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 63799 MW; F2A6C91774762E23 CRC64;
MSLRNRLSKS GENPEQDEAQ KNFMDTYRNG HITMKQLIAK KRLLAAEAEE LKPLFMKEVG
CHFDDFVTNL IEKSASLDNG GCALTTFSIL EEMKKNHRAK DLRAPPEQGK IFISRQSLLD
ELFEVDHIRT IYHMFIALLI LFVLSTIVVD YIDEGRLVLE FNLLAYAFGK FPTVIWTWWA
MFLSTLSIPY FLFQRWAHGY SKSSHPLIYS LVHGLLFLVF QLGVLGFVPT YVVLAYTLPP
ASRFILILEQ IRLIMKAHSF VRENIPRVLN AAKEKSSKDP LPTVNQYLYF LFAPTLIYRD
NYPRTPTVRW GYVAMQFLQV FGCLFYVYYI FERLCAPLFR NIKQEPFSAR VLVLCVFNSI
LPGVLILFLS FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW NVVVHDWLYY
YVYKDLLWFF SKRFKSAAML AVFALSAVVH EYALAICLSY FYPVLFVLFM FFGMAFNFIV
NDSRKRPIWN IMVWASLFLG YGLILCFYSQ EWYARQHCPL KNPTFLDYVR PRTWTCRYVF
