AWAT1_HUMAN
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 03-AUG-2022, entry version 122.
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}.
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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; Q58HT5; -.
DR PeptideAtlas; Q58HT5; -.
DR PRIDE; Q58HT5; -.
DR Antibodypedia; 27356; 100 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 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; 1347007at2759; -.
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; 11 hits in 691 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 tissues.
DR Genevisible; Q58HT5; HS.
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; 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 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..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
