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SOAT1_MACFA
ID   SOAT1_MACFA             Reviewed;         550 AA.
AC   O77761;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Sterol O-acyltransferase 1;
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; Synonyms=ACAT, ACAT1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=9756918; DOI=10.1074/jbc.273.41.26747;
RA   Anderson R.A., Joyce C., Davis M., Reagan J.W., Clark M., Shelness G.S.,
RA   Rudel L.L.;
RT   "Identification of a form of acyl-CoA:cholesterol acyltransferase specific
RT   to liver and intestine in nonhuman primates.";
RL   J. Biol. Chem. 273:26747-26754(1998).
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:0000250|UniProtKB:P35610}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P35610}.
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues, but most strongly in the
CC       adrenal gland. Expressed more strongly in liver Kupffer cells than in
CC       hepatocytes.
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; AF053337; AAC62931.1; -; mRNA.
DR   AlphaFoldDB; O77761; -.
DR   SMR; O77761; -.
DR   STRING; 9541.XP_005540170.1; -.
DR   eggNOG; KOG0380; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0034736; F:cholesterol O-acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004772; F:sterol O-acyltransferase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; 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..550
FT                   /note="Sterol O-acyltransferase 1"
FT                   /id="PRO_0000207641"
FT   TOPO_DOM        1..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        139..160
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        161..180
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        181..206
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        207..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        219..244
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        245..252
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..276
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        277..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        320..352
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        353..369
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        370..395
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        396..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        444..468
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        469..474
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        475..490
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        491..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        497..528
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   TOPO_DOM        529..550
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           403..409
FT                   /note="FYXDWWN motif"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   COMPBIAS        1..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         137
FT                   /ligand="cholesterol"
FT                   /ligand_id="ChEBI:CHEBI:16113"
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         418
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         421
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         425
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         433
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         445
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   BINDING         456
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
FT   DISULFID        528..546
FT                   /evidence="ECO:0000250|UniProtKB:P35610"
SQ   SEQUENCE   550 AA;  64700 MW;  AA655206D58C291D CRC64;
     MVGEEKMSLR NRLSKSRENP EEDEDQRKPA KESLEAPSNG RIDIKQLIAK KIKLTAEAEE
     LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSIL EGEKNNHRAK DLRAPPEQGK
     IFIARRSLLD ELLEVDHIRT IYHMFIALLI LFILSTLVVD YIDEGRLVLE FSLLSYAFGK
     FPTVVWTWWI MFLSTFSVPY FLFQRWATGY SKSSHPLINS LFHGFLFMVF QIGILGFGPT
     YVVLAYTLPP ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
     LFAPTLIYRD SYPRNPTVRW GYVAMQFAQV FGCFFYVYYI FERLCAPLFR NIKQEPFSAR
     VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW
     NVVVHDWLYY YAYKDFLWFF SKRFKSAAML AAFAVSAVVH EYALAVCLSF FYPVLFVLFM
     FFGMAFNFIV NDSRKKPIWN VMMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR
     PRSWTCRYVF
 
 
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