AWAT1_MOUSE
ID AWAT1_MOUSE Reviewed; 328 AA.
AC A2ADU9; B2RW94;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acyl-CoA wax alcohol acyltransferase 1;
DE EC=2.3.1.75 {ECO:0000250|UniProtKB:Q58HT5};
DE AltName: Full=Diacylglycerol O-acyltransferase 2-like protein 3;
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase 1;
GN Name=Awat1; Synonyms=Dgat2l3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acyltransferase that catalyzes the formation of ester bonds
CC between fatty alcohols and fatty acyl-CoAs to form wax monoesters (By
CC similarity). Shows a strong preference for decyl alcohol (C10), with
CC less activity towards C16 and C18 alcohols (By similarity). Shows a
CC strong preference for saturated acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:Q58HT5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38444;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl
CC (9Z)-octadecenoate; Xref=Rhea:RHEA:38227, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75622;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38228;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + decan-1-ol = 1-O-decyl-(9Z)-
CC octadecenoate + CoA; Xref=Rhea:RHEA:38223, ChEBI:CHEBI:28903,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75620;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38224;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-
CC hexadecenyl (9Z)-octadecenoate + CoA; Xref=Rhea:RHEA:38231,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75623,
CC ChEBI:CHEBI:75624; Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38232;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-
CC octadecenoate + CoA; Xref=Rhea:RHEA:38235, ChEBI:CHEBI:32154,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75625;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38236;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-
CC octadecenyl (9Z)-octadecenoate + CoA; Xref=Rhea:RHEA:38239,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73504,
CC ChEBI:CHEBI:75626; Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38240;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-
CC hexadecenoate + CoA; Xref=Rhea:RHEA:38247, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:75629;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38248;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl
CC octadecanoate; Xref=Rhea:RHEA:38251, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:75631;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38252;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + eicosan-1-ol = 1-O-eicosanyl (9Z)-
CC octadecenoate + CoA; Xref=Rhea:RHEA:38243, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75627, ChEBI:CHEBI:75628;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38244;
CC Evidence={ECO:0000250|UniProtKB:Q58HT5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6E213}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL671299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147680; AAI47681.1; -; mRNA.
DR EMBL; BC147683; AAI47684.1; -; mRNA.
DR EMBL; BC147829; AAI47830.1; -; mRNA.
DR EMBL; BC147832; AAI47833.1; -; mRNA.
DR CCDS; CCDS41074.1; -.
DR RefSeq; NP_001074605.1; NM_001081136.1.
DR AlphaFoldDB; A2ADU9; -.
DR BioGRID; 232791; 1.
DR STRING; 10090.ENSMUSP00000094088; -.
DR PaxDb; A2ADU9; -.
DR PRIDE; A2ADU9; -.
DR ProteomicsDB; 265184; -.
DR Antibodypedia; 27356; 100 antibodies from 20 providers.
DR Ensembl; ENSMUST00000096361; ENSMUSP00000094088; ENSMUSG00000015665.
DR GeneID; 245533; -.
DR KEGG; mmu:245533; -.
DR UCSC; uc009twb.1; mouse.
DR CTD; 158833; -.
DR MGI; MGI:3588200; Awat1.
DR VEuPathDB; HostDB:ENSMUSG00000015665; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; A2ADU9; -.
DR OMA; FYCCVFY; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; A2ADU9; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.75; 3474.
DR Reactome; R-MMU-2142753; Arachidonic acid metabolism.
DR Reactome; R-MMU-9640463; Wax biosynthesis.
DR BioGRID-ORCS; 245533; 0 hits in 74 CRISPR screens.
DR PRO; PR:A2ADU9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2ADU9; protein.
DR Bgee; ENSMUSG00000015665; Expressed in lip and 2 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; ISO:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..328
FT /note="Acyl-CoA wax alcohol acyltransferase 1"
FT /id="PRO_0000320296"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 328 AA; 37573 MW; 6CCFBAA4B4579FE9 CRC64;
MSCSMKTEHL QSLSLLQWPL SYVAMFWIVQ PLLICLLFTP LWPLPTVYFV WLLLDWKTPD
KGGRRSDWVR NWNVWNHIRD YFPITILKTK DLSPSENYIM GVHPHGLLTF GAFCNFCTEA
TGFSKTFPGI TPHLATLSWF FKIPIIRDYI MAKGLCSVSQ ASIDYLLSHG TGNLVGIVVG
GVGEALQSVP NTTTLLLKKR KGFVRTALQH GAHLVPTFTF GETEVYDQVL FHEDSRMFKF
QSLFRRIFGF YCCVFYGQGF HQDCKGLLPY HKPIITVVGE ALPLPQVKNP SPEIVDKYHA
LYMDALYKLF EQHKVQYGCS NTQKLIFL
