ID M3W8J8_FELCA Unreviewed; 549 AA.
AC M3W8J8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN Name=SOAT1 {ECO:0000313|Ensembl:ENSFCAP00000007296.4,
GN ECO:0000313|VGNC:VGNC:65561};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000007296.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000007296.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007296.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000007296.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007296.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000007296.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007296.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036418};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325;
CC Evidence={ECO:0000256|ARBA:ARBA00036418};
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=(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:0000256|ARBA:ARBA00036957};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329;
CC Evidence={ECO:0000256|ARBA:ARBA00036957};
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:0000256|ARBA:ARBA00037015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321;
CC Evidence={ECO:0000256|ARBA:ARBA00037015};
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=(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:0000256|ARBA:ARBA00036867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797;
CC Evidence={ECO:0000256|ARBA:ARBA00036867};
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 -!- 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:0000256|ARBA:ARBA00036161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793;
CC Evidence={ECO:0000256|ARBA:ARBA00036161};
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:0000256|ARBA:ARBA00036931};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813;
CC Evidence={ECO:0000256|ARBA:ARBA00036931};
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; AANG04001043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011289319.1; XM_011291017.2.
DR RefSeq; XP_011289320.1; XM_011291018.2.
DR AlphaFoldDB; M3W8J8; -.
DR PaxDb; 9685-ENSFCAP00000007296; -.
DR Ensembl; ENSFCAT00000007882.6; ENSFCAP00000007296.4; ENSFCAG00000007880.6.
DR GeneID; 101081271; -.
DR KEGG; fca:101081271; -.
DR CTD; 6646; -.
DR VGNC; VGNC:65561; SOAT1.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_031845_1_0_1; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000011712; Chromosome F1.
DR Bgee; ENSFCAG00000007880; Expressed in tip of external ear and 10 other cell types or tissues.
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:SF6; STEROL O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR PIRSF; PIRSF500230; Sterol_acyltranf_ACAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transferase {ECO:0000256|PIRNR:PIRNR000439};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 549 AA; 64809 MW; EA9B56A790BB5B4E CRC64;
MVGEETTSLR KRPSRSGENF EEKEDERKPS EESLGISSNG RIDIKQLMAK KIRLTAEAEE
LKPFFMKEVG SHFDDFVNNL IEKSTSLDSG GCAITSFSVL EGDKNYRAKD LRAPPEHGKI
FVVRRSLLDE LFEVDHIRTI YHMFIALLIL FILSTLVVDY IDEGRLVLEF NLMSYAFGKF
PIAMWTWWTM FLSTLSIPYF LFQHWARGYS RSSHPVVHCL IHGFLFMVFL IGVLGLGPTY
VALAYTLPPA SRSIVILEQI RFIMKAYSFV RENVPRVLNS AKEKSKIVPV PTVNQYLYFL
FAPTLIYRDN YPRTPTVRWG YVAMQFLQVF GCLFYMYYIF ERLCTPLFRN IKQEPFSARV
LVLCVFNSIL PGVLILFLMF FAFLHCWLNA FAEMLCFGDR MFYRDWWNST SYSNYYRTWN
VVVHDWLYYY AYKDFLWFFT KRFKWAAMLA VFAVSAVVHE YALAVCLNFF YPVLFVLFMF
FGMAFNFIVN DSRKRPFWNV MVWTSLFAGN GVILCFYSQE WYARQHCPLK NPTFLDYIRP
RSWTCRYVF
//
