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   10-FEB-2021, entry version 123.
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 long chain fatty alcohol + an acyl-CoA = a wax ester + CoA;
CC         Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; 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   SMR; Q6E213; -.
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   ProteomicsDB; 66274; -.
DR   Antibodypedia; 55918; 97 antibodies.
DR   DNASU; 158835; -.
DR   Ensembl; ENST00000276101; ENSP00000421172; ENSG00000147160.
DR   GeneID; 158835; -.
DR   KEGG; hsa:158835; -.
DR   UCSC; uc004dxt.1; human.
DR   CTD; 158835; -.
DR   DisGeNET; 158835; -.
DR   GeneCards; AWAT2; -.
DR   HGNC; HGNC:23251; AWAT2.
DR   HPA; ENSG00000147160; Group enriched (breast, skin).
DR   MIM; 300925; gene.
DR   neXtProt; NX_Q6E213; -.
DR   OpenTargets; ENSG00000147160; -.
DR   PharmGKB; PA164716410; -.
DR   VEuPathDB; HostDB:ENSG00000147160.9; -.
DR   eggNOG; KOG0831; Eukaryota.
DR   GeneTree; ENSGT00950000182761; -.
DR   HOGENOM; CLU_023995_0_0_1; -.
DR   InParanoid; Q6E213; -.
DR   OMA; EVFAVFQ; -.
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; 7 hits in 498 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 lung and 24 other tissues.
DR   ExpressionAtlas; Q6E213; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0008374; F:O-acyltransferase activity; IBA:GO_Central.
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
//