AWAT2_MOUSE
ID AWAT2_MOUSE Reviewed; 333 AA.
AC Q6E1M8; Q8BM49;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acyl-CoA wax alcohol acyltransferase 2;
DE EC=2.3.1.75 {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:28096191};
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:28096191};
DE AltName: Full=Diacylglycerol O-acyltransferase 2-like protein 4;
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase 2;
DE AltName: Full=Wax synthase;
DE Short=mWS;
GN Name=Awat2; Synonyms=Dgat2l4, Ws;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=28096191; DOI=10.1194/jlr.m073692;
RA Arne J.M., Widjaja-Adhi M.A., Hughes T., Huynh K.W., Silvaroli J.A.,
RA Chelstowska S., Moiseenkova-Bell V.Y., Golczak M.;
RT "Allosteric modulation of the substrate specificity of acyl-CoA wax alcohol
RT acyltransferase 2.";
RL J. Lipid Res. 58:719-730(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). Shows a preference for medium chain acyl-CoAs from
CC C12 to C16 in length and fatty alcohols shorter than C20, as the acyl
CC donor and acceptor, respectively (PubMed:15220349). Also possesses
CC acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-
CC specific retinyl ester synthesis (PubMed:28096191). Shows higher
CC catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol,
CC 13- cis-retinol and all-trans-retinol substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q6E213, ECO:0000269|PubMed:15220349,
CC ECO:0000269|PubMed:28096191}.
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:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38444;
CC Evidence={ECO:0000305|PubMed:15220349, ECO:0000305|PubMed:28096191};
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:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38228;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38236;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38240;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:Q6E213};
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:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38252;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55325;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000250|UniProtKB:Q6E213};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000250|UniProtKB:Q6E213};
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:0000269|PubMed:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55273;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000269|PubMed:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55277;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000269|PubMed:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55281;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000269|PubMed:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55285;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000269|PubMed:28096191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55289;
CC Evidence={ECO:0000305|PubMed:28096191};
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:0000269|PubMed:28096191}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26.22 uM for 11-cis-retinol {ECO:0000269|PubMed:28096191};
CC KM=22.25 uM for 9-cis-retinol {ECO:0000269|PubMed:28096191};
CC KM=24.32 uM for 9-cis-retinol (in the presence of 2 uM of 11-cis-
CC retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC KM=21.87 uM for 9-cis-retinol (in the presence of 4 uM of 11-cis-
CC retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC KM=18.74 uM for 9-cis-retinol (in the presence of 6 uM of 11-cis-
CC retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC KM=15.26 uM for 9-cis-retinol (in the presence of 10 uM of 11-cis-
CC retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC KM=35.18 uM for 13-cis-retinol {ECO:0000269|PubMed:28096191};
CC KM=23.59 uM for all-trans-retinol {ECO:0000269|PubMed:28096191};
CC Vmax=14.52 nmol/min/mg enzyme for 11-cis-retinol
CC {ECO:0000269|PubMed:28096191};
CC Vmax=4.53 nmol/min/mg enzyme for 9-cis-retinol
CC {ECO:0000269|PubMed:28096191};
CC Vmax=3.81 nmol/min/mg enzyme for 9-cis-retinol (in the presence of 2
CC uM of 11-cis-retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC Vmax=2.61 nmol/min/mg enzyme for 9-cis-retinol (in the presence of 4
CC uM of 11-cis-retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC Vmax=1.82 nmol/min/mg enzyme for 9-cis-retinol (in the presence of 6
CC uM of 11-cis-retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC Vmax=0.96 nmol/min/mg enzyme for 9-cis-retinol (in the presence of 10
CC uM of 11-cis-retinyl palmitate) {ECO:0000269|PubMed:28096191};
CC Vmax=1.06 nmol/min/mg enzyme for 13-cis-retinol
CC {ECO:0000269|PubMed:28096191};
CC Vmax=0.66 nmol/min/mg enzyme for all-trans-retinol
CC {ECO:0000269|PubMed:28096191};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28096191}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15220349}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6E1M8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6E1M8-2; Sequence=VSP_020357;
CC -!- TISSUE SPECIFICITY: Expressed in Mueller cells of the retina (at
CC protein level) (PubMed:24799687). Abundant in tissues rich in sebaceous
CC glands such as the preputial gland and eyelid (PubMed:15220349).
CC {ECO:0000269|PubMed:15220349, ECO:0000269|PubMed:24799687}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY611031; AAT68765.1; -; mRNA.
DR EMBL; AY611032; AAT68766.1; -; mRNA.
DR EMBL; AK034920; BAC28882.1; -; mRNA.
DR CCDS; CCDS30300.1; -. [Q6E1M8-1]
DR CCDS; CCDS72412.1; -. [Q6E1M8-2]
DR RefSeq; NP_001277324.1; NM_001290395.1. [Q6E1M8-2]
DR RefSeq; NP_808414.2; NM_177746.4. [Q6E1M8-1]
DR RefSeq; XP_011245890.1; XM_011247588.2. [Q6E1M8-2]
DR RefSeq; XP_011245892.1; XM_011247590.2. [Q6E1M8-2]
DR RefSeq; XP_011245893.1; XM_011247591.2. [Q6E1M8-2]
DR RefSeq; XP_011245894.1; XM_011247592.2. [Q6E1M8-2]
DR RefSeq; XP_017173978.1; XM_017318489.1. [Q6E1M8-2]
DR AlphaFoldDB; Q6E1M8; -.
DR STRING; 10090.ENSMUSP00000033567; -.
DR SwissLipids; SLP:000001829; -.
DR PhosphoSitePlus; Q6E1M8; -.
DR PaxDb; Q6E1M8; -.
DR PRIDE; Q6E1M8; -.
DR ProteomicsDB; 273508; -. [Q6E1M8-1]
DR ProteomicsDB; 273509; -. [Q6E1M8-2]
DR Antibodypedia; 55918; 103 antibodies from 23 providers.
DR Ensembl; ENSMUST00000033567; ENSMUSP00000033567; ENSMUSG00000031220. [Q6E1M8-1]
DR Ensembl; ENSMUST00000147103; ENSMUSP00000128516; ENSMUSG00000031220. [Q6E1M8-2]
DR GeneID; 245532; -.
DR KEGG; mmu:245532; -.
DR UCSC; uc009tvx.2; mouse. [Q6E1M8-1]
DR CTD; 158835; -.
DR MGI; MGI:3045345; Awat2.
DR VEuPathDB; HostDB:ENSMUSG00000031220; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; Q6E1M8; -.
DR OMA; HYCNYFP; -.
DR PhylomeDB; Q6E1M8; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.75; 3474.
DR Reactome; R-MMU-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-MMU-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-MMU-9640463; Wax biosynthesis.
DR BioGRID-ORCS; 245532; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q6E1M8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6E1M8; protein.
DR Bgee; ENSMUSG00000031220; Expressed in lip and 46 other tissues.
DR ExpressionAtlas; Q6E1M8; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
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:0050252; F:retinol O-fatty-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; IDA:MGI.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..333
FT /note="Acyl-CoA wax alcohol acyltransferase 2"
FT /id="PRO_0000249053"
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"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020357"
SQ SEQUENCE 333 AA; 38145 MW; A2A2036B28F424A4 CRC64;
MFWPTKKDLK TAMEVFALFQ WALSALVIVT TVIIVNLYLV VFTSYWPVTV LMLTWLAFDW
KTPERGGRRF TCVRKWRLWK HYSDYFPLKM VKTKDISPDR NYILVCHPHG LMAHSCFGHF
ATDTTGFSKT FPGITPYMLT LGAFFWVPFL RDYVMSTGSC SVSRSSMDFL LTQKGTGNML
VVVVGGLAEC RYSTPGSTTL FLKKRQGFVR TALKHGVSLI PAYAFGETDL YDQHIFTPGG
FVNRFQKWFQ KMVHIYPCAF YGRGLTKNSW GLLPYSQPVT TVVGEPLPLP KIENPSEEIV
AKYHTLYIDA LRKLFDQHKT KFGISETQEL VIV
