ID   DGT2A_UMBRA             Reviewed;         355 AA.
AC   Q96UY2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Diacylglycerol O-acyltransferase 2A;
DE            EC=2.3.1.20;
DE   AltName: Full=Diglyceride acyltransferase 2A;
DE   AltName: Full=MrDGAT2A;
GN   Name=DGAT2A;
OS   Umbelopsis ramanniana (Oleaginous fungus) (Mortierella ramanniana).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Umbelopsidomycetes; Umbelopsidales; Umbelopsidaceae; Umbelopsis.
OX   NCBI_TaxID=41833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ENZYME ACTIVITY.
RX   PubMed=11481333; DOI=10.1074/jbc.m106168200;
RA   Lardizabal K.D., Mai J.T., Wagner N.W., Wyrick A., Voelker T.,
RA   Hawkins D.J.;
RT   "DGAT2 is a new diacylglycerol acyltransferase gene family. purification,
RT   cloning, and expression in insect cells of two polypeptides from
RT   Mortierella ramanniana with diacylglycerol acyltransferase activity.";
RL   J. Biol. Chem. 276:38862-38869(2001).
CC   -!- FUNCTION: Catalyzes the terminal and only committed step in
CC       triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC       substrates. Required for storage lipid synthesis.
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:0000269|PubMed:11481333};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:11481333};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF391089; AAK84179.1; -; mRNA.
DR   AlphaFoldDB; Q96UY2; -.
DR   BRENDA; 2.3.1.20; 3434.
DR   UniPathway; UPA00282; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007130; DAGAT.
DR   Pfam; PF03982; DAGAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycerol metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..355
FT                   /note="Diacylglycerol O-acyltransferase 2A"
FT                   /id="PRO_0000249055"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   355 AA;  40603 MW;  860316C694058EC0 CRC64;
     MASKDQHLQQ KVKHTLEAIP SPRYAPLRVP LRRRLQTLAV LLWCSMMSIC MFIFFFLCSI
     PVLLWFPIIL YLTWILVWDK APENGGRPIR WLRNAAWWKL FAGYFPAHVI KEADLDPSKN
     YIFGYHPHGI ISMGSFCTFS TNATGFDDLF PGIRPSLLTL TSNFNIPLYR DYLMACGLCS
     VSKTSCQNIL TKGGPGRSIA IVVGGASESL NARPGVMDLV LKRRFGFIKI AVQTGASLVP
     TISFGENELY EQIESNENSK LHRWQKKIQH ALGFTMPLFH GRGVFNYDFG LLPHRHPIYT
     IVGKPIPVPS IKYGQTKDEI IRELHDSYMH AVQDLYDRYK DIYAKDRVKE LEFVE