SOAT1_RAT
ID SOAT1_RAT Reviewed; 545 AA.
AC O70536;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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|RGD:621641}; Synonyms=Acact, Acat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Adrenal gland;
RX PubMed=9555010; DOI=10.1016/s0005-2760(98)00007-1;
RA Matsuda H., Hakamata H., Kawasaki T., Sakashita N., Miyazaki A.,
RA Takahashi K., Shichiri M., Horiuchi S.;
RT "Molecular cloning, functional expression and tissue distribution of rat
RT acyl-coenzyme A:cholesterol acyltransferase.";
RL Biochim. Biophys. Acta 1391:193-203(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 susbstrateb a
CC higher activity towards an acyl-CoA substrate with a double bond at the
CC delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated
CC acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z)
CC 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 -!- 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; D86373; BAA25372.1; -; mRNA.
DR RefSeq; NP_112380.1; NM_031118.1.
DR AlphaFoldDB; O70536; -.
DR SMR; O70536; -.
DR STRING; 10116.ENSRNOP00000005677; -.
DR BindingDB; O70536; -.
DR ChEMBL; CHEMBL285; -.
DR jPOST; O70536; -.
DR PaxDb; O70536; -.
DR GeneID; 81782; -.
DR KEGG; rno:81782; -.
DR UCSC; RGD:621641; rat.
DR CTD; 6646; -.
DR RGD; 621641; Soat1.
DR eggNOG; KOG0380; Eukaryota.
DR InParanoid; O70536; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; O70536; -.
DR Reactome; R-RNO-8964038; LDL clearance.
DR PRO; PR:O70536; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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:RGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004772; F:sterol O-acyltransferase activity; IDA:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
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 GO; GO:0010878; P:cholesterol storage; ISO:RGD.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; ISO:RGD.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:RGD.
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..545
FT /note="Sterol O-acyltransferase 1"
FT /id="PRO_0000207643"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 134..155
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 156..175
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..201
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 202..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..239
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 240..247
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..271
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 272..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 315..347
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 348..364
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..390
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 391..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..463
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 464..469
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 470..485
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 486..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 492..523
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 524..545
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 398..404
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT ACT_SITE 455
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 132
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 410
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 413
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 416
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 420
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 428
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 451
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 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT DISULFID 523..541
FT /evidence="ECO:0000250|UniProtKB:P35610"
SQ SEQUENCE 545 AA; 64146 MW; 40129EF21257BEBF CRC64;
MVGEETSLRN RLSRSAENPE QDEAQKNLLD THRNGHITMK QLIAKKRQLA AEAEELKPLF
LKEVGCHFDD FVTNLIDKSA SLDNGGCALT TFSILEEMKN NHRAKDLRAP PEQGKIFISR
RSLLDELFEV DHIRTIYHMF IALLIIFILS TLVVDYIDEG RLVLEFSLLA YAFGQFPIVI
WTWWAMFLST LAIPYFLFQR WAHGYSKSSH PLIYSLIHGA FFLVFQLGIL GFIPTYVVLA
YTLPPASRFI LILEQIRLVM KAHSYVRENV PRVLSAAKEK SSTVPVPTVN QYLYFLFAPT
LIYRDSYPRT PTVRWGYVAM QFLQVFGCLF YVYYIFERLC APLFRNIKQE PFSARVLVLC
VFNSILPGVL MLFLSFFAFL HCWLNAFAEM LRFGDRMFYK DWWNSTSYSN YYRTWNVVVH
DWLYYYVYKD LLWFFSKRFR PAAMLAVFAL SAVVHEYALA VCLSYFYPVL FVLFMFFGMA
FNFIVNDSRK RPVWNIMVRA SLFLGHGVIL CFYSQEWYAR QRCPLKNPTF LDYVRPRTWT
CRYVF
