ID G3S4J8_GORGO Unreviewed; 550 AA.
AC G3S4J8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=O-acyltransferase {ECO:0000256|PIRNR:PIRNR000439};
GN Name=SOAT1 {ECO:0000313|Ensembl:ENSGGOP00000023001.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000023001.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000023001.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000023001.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000023001.2}
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; CABD030007578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030007579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030007580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018882776.1; XM_019027231.1.
DR AlphaFoldDB; G3S4J8; -.
DR SMR; G3S4J8; -.
DR STRING; 9593.ENSGGOP00000023001; -.
DR Ensembl; ENSGGOT00000029084.2; ENSGGOP00000023001.2; ENSGGOG00000013728.3.
DR GeneID; 101137508; -.
DR KEGG; ggo:101137508; -.
DR CTD; 6646; -.
DR GeneTree; ENSGT00950000183081; -.
DR InParanoid; G3S4J8; -.
DR OMA; SCMIEDV; -.
DR OrthoDB; 9612at2759; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000013728; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0034736; F:cholesterol O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0010878; P:cholesterol storage; IEA:Ensembl.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IEA:Ensembl.
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:UP000001519};
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 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
SQ SEQUENCE 550 AA; 64735 MW; 5F5ACD525D541DEE CRC64;
MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK KIKLTAEAEE
LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL EGEKNNHRAK DLRAPPEQGK
IFIARRSLLD ELLEVDHIRT IYHMFIALLI LFILSTLVVD YIDEGRLVLE FSLLSYAFGK
FPTVVWTWWI MFLSTFSVPY FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT
YVVLAYTLPP ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR NIKQEPFSAR
VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW
NVVVHDWLYY YAYKDFLWFF SKRFKSAAML AVFAVSAVVH EYALAVCLSF FYPVLFVLFM
FFGMAFNFIV NDSRKKPIWN VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR
PRSWTCRYVF
//
