ID AWAT1_HUMAN Reviewed; 328 AA. AC Q58HT5; Q5JT21; Q6IEE4; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 24-JAN-2024, entry version 130. DE RecName: Full=Acyl-CoA wax alcohol acyltransferase 1; DE EC=2.3.1.75 {ECO:0000269|PubMed:15671038}; DE AltName: Full=Diacylglycerol O-acyltransferase 2-like protein 3; DE AltName: Full=Diacylglycerol acyltransferase 2; DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase 1; GN Name=AWAT1; Synonyms=DGA2, DGAT2L3; 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=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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-328. 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 [4] 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). CC -!- FUNCTION: Acyltransferase that catalyzes the formation of ester bonds CC between fatty alcohols and fatty acyl-CoAs to form wax monoesters CC (PubMed:15671038). Shows a strong preference for decyl alcohol (C10), CC with less activity towards C16 and C18 alcohols (PubMed:15671038). CC Shows a strong preference for saturated acyl-CoAs (PubMed:15671038). CC {ECO:0000269|PubMed:15671038}. 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:15671038}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38444; CC Evidence={ECO:0000305|PubMed:15671038}; 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)-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:0000269|PubMed:15671038}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38224; 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=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}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168; 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=(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:0000269|PubMed:15671038}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38244; CC Evidence={ECO:0000305|PubMed:15671038}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q6E213}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Predominantly expressed in skin, where it is CC limited to the sebaceous gland. Expressed in more mature, centrally CC located cells just before their rupture and sebum release. Also CC expressed in all tissues except spleen. Expressed at higher level in CC thymus, prostate and testis. {ECO:0000269|PubMed:15671038}. CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY947638; AAX48018.1; -; mRNA. DR EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC039181; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BN000155; CAD89266.1; -; mRNA. DR CCDS; CCDS35321.1; -. DR RefSeq; NP_001013597.1; NM_001013579.2. DR AlphaFoldDB; Q58HT5; -. DR BioGRID; 127715; 3. DR STRING; 9606.ENSP00000363645; -. DR BindingDB; Q58HT5; -. DR ChEMBL; CHEMBL2375205; -. DR SwissLipids; SLP:000000306; -. DR BioMuta; AWAT1; -. DR DMDM; 74741070; -. DR PaxDb; 9606-ENSP00000363645; -. DR PeptideAtlas; Q58HT5; -. DR Antibodypedia; 27356; 116 antibodies from 20 providers. DR DNASU; 158833; -. DR Ensembl; ENST00000374521.4; ENSP00000363645.3; ENSG00000204195.4. DR GeneID; 158833; -. DR KEGG; hsa:158833; -. DR MANE-Select; ENST00000374521.4; ENSP00000363645.3; NM_001013579.3; NP_001013597.1. DR UCSC; uc004dxy.4; human. DR AGR; HGNC:23252; -. DR CTD; 158833; -. DR DisGeNET; 158833; -. DR GeneCards; AWAT1; -. DR HGNC; HGNC:23252; AWAT1. DR HPA; ENSG00000204195; Tissue enhanced (skin). DR MIM; 300924; gene. DR neXtProt; NX_Q58HT5; -. DR OpenTargets; ENSG00000204195; -. DR PharmGKB; PA164716409; -. DR VEuPathDB; HostDB:ENSG00000204195; -. DR eggNOG; KOG0831; Eukaryota. DR GeneTree; ENSGT01030000234582; -. DR HOGENOM; CLU_023995_0_0_1; -. DR InParanoid; Q58HT5; -. DR OMA; FYCCVFY; -. DR OrthoDB; 601258at2759; -. DR PhylomeDB; Q58HT5; -. DR TreeFam; TF314707; -. DR BRENDA; 2.3.1.75; 2681. DR PathwayCommons; Q58HT5; -. DR Reactome; R-HSA-2142753; Arachidonic acid metabolism. DR Reactome; R-HSA-9640463; Wax biosynthesis. DR BioGRID-ORCS; 158833; 12 hits in 764 CRISPR screens. DR GenomeRNAi; 158833; -. DR Pharos; Q58HT5; Tbio. DR PRO; PR:Q58HT5; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q58HT5; Protein. DR Bgee; ENSG00000204195; Expressed in upper leg skin and 36 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. 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:0019369; P:arachidonic acid metabolic process; TAS:Reactome. DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central. DR GO; GO:0010025; P:wax biosynthetic process; TAS:Reactome. DR CDD; cd07987; LPLAT_MGAT-like; 1. DR InterPro; IPR007130; DAGAT. DR PANTHER; PTHR12317:SF16; ACYL-COA WAX ALCOHOL ACYLTRANSFERASE 1; 1. DR PANTHER; PTHR12317; DIACYLGLYCEROL O-ACYLTRANSFERASE; 1. DR Pfam; PF03982; DAGAT; 1. DR Genevisible; Q58HT5; HS. 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..328 FT /note="Acyl-CoA wax alcohol acyltransferase 1" FT /id="PRO_0000249051" 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; 37759 MW; 51475CFD31667215 CRC64; MAHSKQPSHF QSLMLLQWPL SYLAIFWILQ PLFVYLLFTS LWPLPVLYFA WLFLDWKTPE RGGRRSAWVR NWCVWTHIRD YFPITILKTK DLSPEHNYLM GVHPHGLLTF GAFCNFCTEA TGFSKTFPGI TPHLATLSWF FKIPFVREYL MAKGVCSVSQ PAINYLLSHG TGNLVGIVVG GVGEALQSVP NTTTLILQKR KGFVRTALQH GAHLVPTFTF GETEVYDQVL FHKDSRMYKF QSCFRRIFGF YCCVFYGQSF CQGSTGLLPY SRPIVTVVGE PLPLPQIEKP SQEMVDKYHA LYMDALHKLF DQHKTHYGCS ETQKLFFL //