ID   Q8K1M9_RAT              Unreviewed;       524 AA.
AC   Q8K1M9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
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 {ECO:0000313|EMBL:BAC00846.1};
RN   [1] {ECO:0000313|EMBL:BAC00846.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Katsunori M., Takeshi O., Yukio F.;
RT   "Cloning and sequence of rat intestinal ACAT2.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000230};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817;
CC         Evidence={ECO:0000256|ARBA:ARBA00000230};
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:0000256|ARBA:ARBA00000339};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437;
CC         Evidence={ECO:0000256|ARBA:ARBA00000339};
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:0000256|ARBA:ARBA00024275};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817;
CC         Evidence={ECO:0000256|ARBA:ARBA00024275};
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:0000256|ARBA:ARBA00024260};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730;
CC         Evidence={ECO:0000256|ARBA:ARBA00024260};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|PIRNR:PIRNR000439}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010,
CC       ECO:0000256|PIRNR:PIRNR000439}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB075946; BAC00846.1; -; mRNA.
DR   AlphaFoldDB; Q8K1M9; -.
DR   SMR; Q8K1M9; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034736; F:cholesterol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   InterPro; IPR030687; Sterol_acyltranf_meta.
DR   PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10408:SF10; STEROL O-ACYLTRANSFERASE 2; 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 {ECO:0000256|PIRNR:PIRNR000439,
KW   ECO:0000313|EMBL:BAC00846.1};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR000439};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000439};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000439, ECO:0000313|EMBL:BAC00846.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        436
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ   SEQUENCE   524 AA;  60484 MW;  CA89A05AE92337B0 CRC64;
     MEPKAPQLRR RERQGEEQEN GACGEGNTRT HRAPDLVQWT RHMEAVKTQC LEQAQRELAE
     LMDRAIWEAV QAYPKQDRPL PSTASDSTRK TQELHPGKRK VFITRKSLLD ELMEVQHFRT
     IYHMFIAGLC VLIISTLAID FIDEGRLMLA FDLLLFSFGQ LPLALMMWVP MFLSTLLLPY
     QTLRLWARPR SGGAWTLGAS LGCVLLAAHA AVLCVLPVHV SVKHELPPAS RCVLVFEQVR
     FLMKSYSFLR ETVPGIFCVR GGKGICTPSF SSYLYFLFCP TLIYRETYPR TPSIRWNYVA
     KNFAQALGCL LYACFILGRL CVPVFANMSR EPFSTRALLL SILHATGPGI FMLLLIFFAF
     LHCWLNAFAE MLRFGDRMFY RDWWNSTSFS NYYRTWNAVV HDWLYSYVYQ DGLWLLGRQG
     RGAAMLGVFL VSALVHEYIF CFVLGFFYPV MLILFLVVGG LLNFTMNDRH TGPAWNILMW
     TFLFLGQGIQ VSLYCQEWYA RRHCPLPQPT FWELVTPRSW SCHP
//