ID A0A2I3SXL9_PANTR Unreviewed; 492 AA.
AC A0A2I3SXL9; A0A2J8N6U6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN Name=SOAT1 {ECO:0000313|Ensembl:ENSPTRP00000081315.1,
GN ECO:0000313|VGNC:VGNC:10985};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000081315.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000081315.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000081315.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR EMBL; AACZ04056200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3SXL9; -.
DR SMR; A0A2I3SXL9; -.
DR Ensembl; ENSPTRT00000097714.1; ENSPTRP00000081315.1; ENSPTRG00000001728.6.
DR VGNC; VGNC:10985; SOAT1.
DR GeneTree; ENSGT00950000183081; -.
DR OMA; SCMIEDV; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001728; Expressed in pituitary gland and 22 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:UP000002277};
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 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 492 AA; 58131 MW; 285EF79CC80BF5E8 CRC64;
MELKPFFMKE VGSHFDDFVT NLIEKSASLD NGGCALTTFS VLEGEKNNHR AKDLRAPPEQ
GKIFIARRSL LDELLEVDHI RTIYHMFIAL LILFILSTLV VDYIDEGRLV LEFSLLSYAF
GKFPTVVWTW WIMFLSTFSV PYFLFQHWAT GYSKSSHPLI RSLFHGFLFM IFQIGVLGFG
PTYVVLAYTL PPASRFIIIF EQIRFVMKAH SFVRENVPRV LNSAKEKSST VPIPTVNQYL
YFLFAPTLIY RDSYPRNPTV RWGYVAMKFA QVFGCFFYVY YIFERLCAPL FRNIKQEPFS
ARVLVLCVFN SILPGVLILF LTFFAFLHCW LNAFAEMLRF GDRMFYKDWW NSTSYSNYYR
TWNVVVHDWL YYYAYKDFLW FFSKRFKSAA MLAVFAVSAV VHEYALAVCL SFFYPVLFVL
FMFFGMAFNF IVNDSRKKPI WNVLMWTSLF LGNGVLLCFY SQEWYARQHC PLKNPTFLDY
VRPRSWTCRY VF
//
