SOAT1_CRIGR
ID SOAT1_CRIGR Reviewed; 546 AA.
AC Q60457;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8662991; DOI=10.1074/jbc.271.24.14642;
RA Cao G., Goldstein J.L., Brown M.S.;
RT "Complementation of mutation in acyl-CoA:cholesterol acyltransferase (ACAT)
RT fails to restore sterol regulation in ACAT-defective sterol-resistant
RT hamster cells.";
RL J. Biol. Chem. 271:14642-14648(1996).
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 -!- 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; U47320; AAC52670.1; -; mRNA.
DR RefSeq; NP_001233679.1; NM_001246750.1.
DR AlphaFoldDB; Q60457; -.
DR SMR; Q60457; -.
DR STRING; 10029.NP_001233679.1; -.
DR BindingDB; Q60457; -.
DR ChEMBL; CHEMBL1075066; -.
DR GeneID; 100689317; -.
DR KEGG; cge:100689317; -.
DR CTD; 6646; -.
DR eggNOG; KOG0380; Eukaryota.
DR OrthoDB; 1275897at2759; -.
DR PRO; PR:Q60457; -.
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 Steroid metabolism; Sterol metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..546
FT /note="Sterol O-acyltransferase 1"
FT /id="PRO_0000207639"
FT TOPO_DOM 1..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..156
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 157..176
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..202
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 203..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..240
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 241..248
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..272
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 273..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 316..348
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 349..365
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 366..391
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 392..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..464
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 465..470
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..486
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 487..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 493..524
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 525..546
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 399..405
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 133
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
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 414
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 417
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 429
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 441
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 452
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 524..542
FT /evidence="ECO:0000250|UniProtKB:P35610"
SQ SEQUENCE 546 AA; 64111 MW; 4ED6C403AAC7E65B CRC64;
MVGEEKMSLR NRLSKSGENP EQDEAQRSVS DTQSNGRITM KQLIAKKRQL AAEAEELKPL
FLKEVGCHFD DFVTNLIEKS ASLDNGGCAL TTFSILEEMK NNHRAKDLRA PPEKGKIFIS
RRSLLDELFE VDHIRTIYHM FIGLLILFIL STLVVDYIDE GRLVLEFNLL GYAFGKLPTV
IWTWWAMFLS TLSIPYFLFQ RWAHGYSKTS HPLIYSLSHG FFFLVFQLGI LGFVPTYVVL
AYTLPPASRF IVILEQIRMV MKAHSFVREN VPRVLNAAKE KSSTVPVPTV NQYLYFLFAP
TLIYRDSYPR TPTVRWGYVA VQFLQVFGCL FYVYYIFERL CAPLFRNIKQ EPFSARVLVL
CVFNSILPGV LMLFLTFFAF LHCWLNAFAE MLRFGDRMFY KDWWNSTSYS NYYRTWNVVV
HDWLYYYAYK DLLWFFSKRF KSAAMLAVFA LSAVVHEYAL AVCLSYFYPV LFVLFMFFGM
AFNFIVNDSR KRPIWNIMVW ASLFLGHGVI LCFYSQEWYA RQHCPLKNPT FLDYVRPRSW
TCQYVF
