AWAT2_HUMAN
ID AWAT2_HUMAN Reviewed; 333 AA.
AC Q6E213; Q6IEE3; Q6P437;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acyl-CoA wax alcohol acyltransferase 2;
DE EC=2.3.1.75 {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:15671038, ECO:0000269|PubMed:16106050, ECO:0000269|PubMed:28420705};
DE AltName: Full=11-cis-specific retinyl-ester synthase {ECO:0000303|PubMed:24799687};
DE Short=11-cis-RE-synthase {ECO:0000303|PubMed:24799687};
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase;
DE Short=ARAT;
DE Short=Retinol O-fatty-acyltransferase;
DE EC=2.3.1.76 {ECO:0000269|PubMed:16106050, ECO:0000269|PubMed:24799687};
DE AltName: Full=Diacylglycerol O-acyltransferase 2-like protein 4;
DE AltName: Full=Diacylglycerol O-acyltransferase candidate 4;
DE Short=hDC4;
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase 2;
DE AltName: Full=Multifunctional O-acyltransferase {ECO:0000303|PubMed:16106050};
DE AltName: Full=Wax synthase;
DE Short=hWS;
GN Name=AWAT2; Synonyms=DC4, DGAT2L4, MFAT {ECO:0000303|PubMed:16106050}, WS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=15220349; DOI=10.1074/jbc.m406226200;
RA Cheng J.B., Russell D.W.;
RT "Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs
RT encoding a member of the acyltransferase enzyme family.";
RL J. Biol. Chem. 279:37798-37807(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-333.
RC TISSUE=Skin;
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).
RN [3]
RP IDENTIFICATION.
RX PubMed=14970677; DOI=10.1159/000075723;
RA Winter A., van Eckeveld M., Bininda-Emonds O.R.P., Habermann F.A.,
RA Fries R.;
RT "Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus)
RT and other mammals.";
RL Cytogenet. Genome Res. 102:42-47(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15671038; DOI=10.1074/jbc.m500025200;
RA Turkish A.R., Henneberry A.L., Cromley D., Padamsee M., Oelkers P.,
RA Bazzi H., Christiano A.M., Billheimer J.T., Sturley S.L.;
RT "Identification of two novel human Acyl-CoA wax alcohol acyltransferases:
RT members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily.";
RL J. Biol. Chem. 280:14755-14764(2005).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16106050; DOI=10.1194/jlr.m500168-jlr200;
RA Yen C.-L.E., Brown C.H. IV, Monetti M., Farese R.V. Jr.;
RT "A human skin multifunctional O-acyltransferase that catalyzes the
RT synthesis of acylglycerols, waxes, and retinyl esters.";
RL J. Lipid Res. 46:2388-2397(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24799687; DOI=10.1073/pnas.1319142111;
RA Kaylor J.J., Cook J.D., Makshanoff J., Bischoff N., Yong J., Travis G.H.;
RT "Identification of the 11-cis-specific retinyl-ester synthase in retinal
RT Mueller cells as multifunctional O-acyltransferase (MFAT).";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7302-7307(2014).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28420705; DOI=10.1194/jlr.m073445;
RA Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.;
RT "Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
RT acyltransferases.";
RL J. Lipid Res. 58:1091-1099(2017).
CC -!- FUNCTION: Acyltransferase that catalyzes the formation of ester bonds
CC between fatty alcohols and fatty acyl-CoAs to form wax monoesters
CC (PubMed:15220349, PubMed:15671038, PubMed:16106050, PubMed:28420705).
CC Shows a preference for medium chain acyl-CoAs from C12 to C16 in length
CC and fatty alcohols shorter than C20, as the acyl donors and acceptors,
CC respectively (PubMed:15220349, PubMed:15671038). Also possesses acyl-
CC CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-
CC specific retinyl ester synthesis (PubMed:16106050, PubMed:24799687).
CC Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-
CC retinol, 13-cis-retinol, and all-trans-retinol substrates
CC (PubMed:24799687). {ECO:0000269|PubMed:15220349,
CC ECO:0000269|PubMed:15671038, ECO:0000269|PubMed:16106050,
CC ECO:0000269|PubMed:24799687, ECO:0000269|PubMed:28420705}.
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:0000269|PubMed:15220349, ECO:0000269|PubMed:15671038,
CC ECO:0000269|PubMed:16106050, ECO:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38444;
CC Evidence={ECO:0000305|PubMed:15220349, ECO:0000305|PubMed:15671038,
CC ECO:0000305|PubMed:16106050, ECO:0000305|PubMed:28420705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester +
CC CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76;
CC Evidence={ECO:0000269|PubMed:16106050, ECO:0000269|PubMed:24799687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000305|PubMed:16106050, ECO:0000305|PubMed:24799687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000305|PubMed:16106050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-
CC di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75583;
CC Evidence={ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000305|PubMed:16106050};
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:0000269|PubMed:15671038, ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000305|PubMed:15671038, ECO:0000305|PubMed:16106050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587;
CC Evidence={ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000305|PubMed:16106050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000305|PubMed:16106050};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38228;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38232;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38236;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38240;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38248;
CC Evidence={ECO:0000305|PubMed:15671038};
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:0000269|PubMed:15671038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38252;
CC Evidence={ECO:0000305|PubMed:15671038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol + hexadecanoyl-CoA = 11-cis-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:55324, ChEBI:CHEBI:16254,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:24799687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55325;
CC Evidence={ECO:0000305|PubMed:24799687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC (9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734;
CC Evidence={ECO:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000305|PubMed:28420705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000305|PubMed:28420705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol + tetradecanoyl-CoA = 11-cis-retinyl
CC tetradecanoate + CoA; Xref=Rhea:RHEA:55272, ChEBI:CHEBI:16302,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:138676;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55273;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + tetradecanoyl-CoA = 9-cis-retinyl
CC tetradecanoate + CoA; Xref=Rhea:RHEA:55276, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:78272, ChEBI:CHEBI:138691;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55277;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + tetradecanoyl-CoA = 13-cis-retinyl
CC tetradecanoate + CoA; Xref=Rhea:RHEA:55280, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:138704;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55281;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + tetradecanoyl-CoA = all-trans-retinyl
CC tetradecanoate + CoA; Xref=Rhea:RHEA:55284, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:138718;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55285;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecan-1-ol + tetradecanoyl-CoA = CoA + tetradecanyl
CC tetradecanoate; Xref=Rhea:RHEA:55288, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:77417, ChEBI:CHEBI:138721;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55289;
CC Evidence={ECO:0000250|UniProtKB:Q6E1M8};
CC -!- ACTIVITY REGULATION: 11-cis retinoids act as allosteric modulators of
CC acyl-CoA retinol O-fatty-acyltransferase (ARAT) activity by suppressing
CC esterification of 9-cis, 13-cis, or all-trans retinols concurrently
CC increasing the enzyme specificity toward 11-cis isomer.
CC {ECO:0000250|UniProtKB:Q6E1M8}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for 11-cis-retinol {ECO:0000269|PubMed:24799687};
CC KM=19.8 uM for 9-cis-retinol {ECO:0000269|PubMed:24799687};
CC KM=27.4 uM for 13-cis-retinol {ECO:0000269|PubMed:24799687};
CC KM=24.8 uM for all-trans-retinol {ECO:0000269|PubMed:24799687};
CC Vmax=980 pmol/min/mg enzyme for 11-cis-retinol
CC {ECO:0000269|PubMed:24799687};
CC Vmax=1010 pmol/min/mg enzyme for 9-cis-retinol
CC {ECO:0000269|PubMed:24799687};
CC Vmax=6.4 pmol/min/mg enzyme for 13-cis-retinol
CC {ECO:0000269|PubMed:24799687};
CC Vmax=148 pmol/min/mg enzyme for all-trans-retinol
CC {ECO:0000269|PubMed:24799687};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6E1M8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6E1M8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skin, where it is primarily
CC restricted to undifferentiated peripheral sebocytes. Also expressed at
CC lower level in other tissues except pancreas.
CC {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:15671038,
CC ECO:0000269|PubMed:16106050}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY605053; AAT68764.1; -; mRNA.
DR EMBL; BC063698; AAH63698.1; -; mRNA.
DR EMBL; BN000156; CAD89267.1; -; mRNA.
DR CCDS; CCDS35320.1; -.
DR RefSeq; NP_001002254.1; NM_001002254.1.
DR RefSeq; XP_011529178.1; XM_011530876.2.
DR AlphaFoldDB; Q6E213; -.
DR BioGRID; 127716; 29.
DR STRING; 9606.ENSP00000421172; -.
DR BindingDB; Q6E213; -.
DR ChEMBL; CHEMBL2375204; -.
DR SwissLipids; SLP:000000301; -.
DR iPTMnet; Q6E213; -.
DR PhosphoSitePlus; Q6E213; -.
DR BioMuta; AWAT2; -.
DR DMDM; 74748433; -.
DR jPOST; Q6E213; -.
DR PaxDb; Q6E213; -.
DR PeptideAtlas; Q6E213; -.
DR PRIDE; Q6E213; -.
DR Antibodypedia; 55918; 103 antibodies from 23 providers.
DR DNASU; 158835; -.
DR Ensembl; ENST00000276101.7; ENSP00000421172.1; ENSG00000147160.9.
DR GeneID; 158835; -.
DR KEGG; hsa:158835; -.
DR MANE-Select; ENST00000276101.7; ENSP00000421172.1; NM_001002254.1; NP_001002254.1.
DR UCSC; uc004dxt.1; human.
DR CTD; 158835; -.
DR DisGeNET; 158835; -.
DR GeneCards; AWAT2; -.
DR HGNC; HGNC:23251; AWAT2.
DR HPA; ENSG00000147160; Tissue enriched (skin).
DR MIM; 300925; gene.
DR neXtProt; NX_Q6E213; -.
DR OpenTargets; ENSG00000147160; -.
DR PharmGKB; PA164716410; -.
DR VEuPathDB; HostDB:ENSG00000147160; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; Q6E213; -.
DR OMA; HYCNYFP; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q6E213; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.75; 2681.
DR PathwayCommons; Q6E213; -.
DR Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-HSA-9640463; Wax biosynthesis.
DR BioGRID-ORCS; 158835; 15 hits in 692 CRISPR screens.
DR GenomeRNAi; 158835; -.
DR Pharos; Q6E213; Tbio.
DR PRO; PR:Q6E213; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6E213; protein.
DR Bgee; ENSG00000147160; Expressed in thymus and 24 other tissues.
DR ExpressionAtlas; Q6E213; baseline and differential.
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:0003846; F:2-acylglycerol O-acyltransferase activity; TAS:Reactome.
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; EXP:Reactome.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR GO; GO:0010025; P:wax biosynthetic process; TAS:Reactome.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..333
FT /note="Acyl-CoA wax alcohol acyltransferase 2"
FT /id="PRO_0000249052"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 333 AA; 38094 MW; B2F1BAAF331BAE4C CRC64;
MLLPSKKDLK TALDVFAVFQ WSFSALLITT TVIAVNLYLV VFTPYWPVTV LILTWLAFDW
KTPQRGGRRF TCVRHWRLWK HYSDYFPLKL LKTHDICPSR NYILVCHPHG LFAHGWFGHF
ATEASGFSKI FPGITPYILT LGAFFWMPFL REYVMSTGAC SVSRSSIDFL LTHKGTGNMV
IVVIGGLAEC RYSLPGSSTL VLKNRSGFVR MALQHGVPLI PAYAFGETDL YDQHIFTPGG
FVNRFQKWFQ SMVHIYPCAF YGRGFTKNSW GLLPYSRPVT TIVGEPLPMP KIENPSQEIV
AKYHTLYIDA LRKLFDQHKT KFGISETQEL EII
