SOAT2_RAT
ID SOAT2_RAT Reviewed; 524 AA.
AC Q7TQM4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Sterol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.26 {ECO:0000250|UniProtKB:O75908};
DE AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 2;
DE Short=ACAT-2;
DE AltName: Full=Cholesterol acyltransferase 2;
GN Name=Soat2 {ECO:0000312|RGD:628865}; Synonyms=Acat2;
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=Sprague-Dawley; TISSUE=Liver;
RA Horiuchi S., Hori M., Hakamata H., Sato M., Miyazaki A.;
RT "Acyl-coenzyme A:cholesterol acyltransferase 2 is responsible for elevated
RT intestinal cholesterol ester formation in streptozotocin-induced diabetic
RT rats.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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) and linolenoyl-CoA ((9Z,12Z,15Z)-
CC octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for
CC lipoprotein secretion from hepatocytes and intestinal mucosa.
CC {ECO:0000250|UniProtKB:O75908}.
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:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817;
CC Evidence={ECO:0000250|UniProtKB:O75908};
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:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730;
CC Evidence={ECO:0000250|UniProtKB:O75908};
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:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437;
CC Evidence={ECO:0000250|UniProtKB:O75908};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol =
CC (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoA;
CC Xref=Rhea:RHEA:46612, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:73862, ChEBI:CHEBI:84969;
CC Evidence={ECO:0000250|UniProtKB:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46613;
CC Evidence={ECO:0000250|UniProtKB:O75908};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-
CC octadecatrienoyl)-cholesterol + CoA; Xref=Rhea:RHEA:46620,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:84341; Evidence={ECO:0000250|UniProtKB:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46621;
CC Evidence={ECO:0000250|UniProtKB:O75908};
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:O75908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817;
CC Evidence={ECO:0000250|UniProtKB:O75908};
CC -!- SUBUNIT: May form homo- or heterodimers (By similarity). Interacts with
CC INSIG1; the interaction is direct and promotes association with
CC AMFR/gp78 (By similarity). {ECO:0000250|UniProtKB:O75908,
CC ECO:0000250|UniProtKB:P35610}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein
CC {ECO:0000255}.
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 -!- PTM: Polyubiquitinated by AMFR/gp78 at Cys-279, leading to its
CC degradation when the lipid levels are low. Association with AMFR/gp78
CC is mediated via interaction with INSIG1. High concentration of
CC cholesterol and fatty acid results in Cys-279 oxidation, preventing
CC ubiquitination at the same site, resulting in protein stabilization.
CC {ECO:0000250|UniProtKB:O75908}.
CC -!- PTM: Oxidized at Cys-279: high concentration of cholesterol and fatty
CC acid induce reactive oxygen species, which oxidizes Cys-279, preventing
CC ubiquitination at the same site, and resulting in protein
CC stabilization. {ECO:0000250|UniProtKB:O75908}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AB101480; BAC78210.1; -; mRNA.
DR RefSeq; NP_714950.2; NM_153728.2.
DR AlphaFoldDB; Q7TQM4; -.
DR SMR; Q7TQM4; -.
DR STRING; 10116.ENSRNOP00000015367; -.
DR BindingDB; Q7TQM4; -.
DR ChEMBL; CHEMBL2856; -.
DR CarbonylDB; Q7TQM4; -.
DR PaxDb; Q7TQM4; -.
DR GeneID; 266770; -.
DR KEGG; rno:266770; -.
DR CTD; 8435; -.
DR RGD; 628865; Soat2.
DR eggNOG; KOG0380; Eukaryota.
DR InParanoid; Q7TQM4; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; Q7TQM4; -.
DR Reactome; R-RNO-8964038; LDL clearance.
DR PRO; PR:Q7TQM4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0034736; F:cholesterol O-acyltransferase activity; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP: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 Acyltransferase; Cholesterol metabolism; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Oxidation; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Thioester bond; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..524
FT /note="Sterol O-acyltransferase 2"
FT /id="PRO_0000255713"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..140
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 141..160
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..186
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 187..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..222
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 223..230
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 231..254
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 255..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..328
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 329..345
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..371
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 372..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..444
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 445..450
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..466
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 467..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..504
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT TOPO_DOM 505..524
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 379..385
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 117
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 391
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 394
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 397
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 401
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 409
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT BINDING 432
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P35610"
FT MOD_RES 279
FT /note="Cysteine sulfenic acid (-SOH); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75908"
FT CROSSLNK 279
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75908"
SQ SEQUENCE 524 AA; 60498 MW; 75CE7DE53F03C88A CRC64;
MEPKAPQLRR RERQGEEQEN GACGEGNTRT HRAPDLVQWT RHMEAVKTQC LEQAQRELAE
LMDRAIWEAV QAYPKQDRPL PSTASDSTRK TQELHPGKRK VFITRKSLLD ELMGVQHFRT
IYHMFIAGLC VLIISTLAID FIDEGRLMLE FDLLLFSFGQ LPLALMMWVP MFLSTLLLPY
QTLRLWARPR SGGAWTLGAS LGCVLLAAHA AVLCVLPVHV SVKHELPPAS RCVLVFEQVR
FLMKSYSFLR ETVPGIFCVR GGKGICTPSF SSYLYFLFCP TLIYRETYPR TPSIRWNYVA
KNFAQALGCL LYACFILGRL CVPVFANMSR EPFSTRALLL SILHATGPGI FMLLLIFFAF
LHCWLNAFAE MLRFGDRMFY RDWWNSTSFS NYYRTWNVVV HDWLYSYVYQ DGLWLLGRQG
RGAAMLGVFL VSALVHEYIF CFVLGFFYPV MLILFLVVGG LLNFTMNDRH TGPAWNILMW
TFLFLGQGIQ VSLYCQEWYA RRHCPLPQPT FWELVTPRSW SCHP
