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Database: UniProt
Entry: A0A072UXT5_MEDTR
LinkDB: A0A072UXT5_MEDTR
Original site: A0A072UXT5_MEDTR 
ID   A0A072UXT5_MEDTR        Unreviewed;       323 AA.
AC   A0A072UXT5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=O-acyltransferase WSD1-like protein {ECO:0000313|EMBL:KEH30690.1};
GN   Name=11440683 {ECO:0000313|EnsemblPlants:KEH30690};
GN   OrderedLocusNames=MTR_4g078390 {ECO:0000313|EMBL:KEH30690.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH30690.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH30690.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH30690.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH30690,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:KEH30690.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH30690.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH30690,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:KEH30690}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH30690};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001039};
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:0000256|ARBA:ARBA00029340};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004771}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00024360}.
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DR   EMBL; CM001220; KEH30690.1; -; Genomic_DNA.
DR   RefSeq; XP_013456659.1; XM_013601205.1.
DR   AlphaFoldDB; A0A072UXT5; -.
DR   EnsemblPlants; KEH30690; KEH30690; MTR_4g078390.
DR   Gramene; KEH30690; KEH30690; MTR_4g078390.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000002051; Chromosome 4.
DR   ExpressionAtlas; A0A072UXT5; differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR   PANTHER; PTHR31650:SF27; O-ACYLTRANSFERASE WSD1-LIKE PROTEIN; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   Pfam; PF03007; WS_DGAT_cat; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..191
FT                   /note="O-acyltransferase WSD1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03007"
FT   DOMAIN          245..314
FT                   /note="O-acyltransferase WSD1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06974"
SQ   SEQUENCE   323 AA;  36905 MW;  AEF9E94035DC28C2 CRC64;
     MRWQRVEVKL EEHIKIPKFP ETTNSSSILY DNYLSDYVTS ILTSRTPQDK PLWEIHLIKY
     PTSNAKGTLI FKLHHALGDG YSLMGALLSC LQRADDPSLP LSFPSRPQLN SKYAKKGLFK
     KLCLDISSFF SSISDFGSSL IKTRMIEDDK TPIRSGYEGT ESQPFTLSNI SLSLDQIKEI
     KSKLGVTIND VLSGVIFYGI RLYMEEMNEK TKKSNSTAVV MLNTRNIEGY QSLKEMQKPE
     SKSLWGNQIS FLQIPIPKLS QSDPLEFVWK ARKLIKRKRR SFGVYLIGLL LNLEMKLKGS
     EVCHTLFNHS SKNLMLYLFS LIL
//
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