ID   DGT2B_UMBRA             Reviewed;         349 AA.
AC   Q96UY1;
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 2B;
DE            EC=2.3.1.20;
DE   AltName: Full=Diglyceride acyltransferase 2B;
DE   AltName: Full=MrDGAT2B;
GN   Name=DGAT2B;
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; AF391090; AAK84180.1; -; mRNA.
DR   AlphaFoldDB; Q96UY1; -.
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; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..349
FT                   /note="Diacylglycerol O-acyltransferase 2B"
FT                   /id="PRO_0000249056"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   349 AA;  39596 MW;  581B61757224015F CRC64;
     MEQVQVTALL DHIPKVHWAP LRGIPLKRRL QTSAIVTWLA LLPICLIIYL YLFTIPLLWP
     ILIMYTIWLF FDKAPENGGR RISLVRKLPL WKHFANYFPV TLIKEGDLDP KGNYIMSYHP
     HGIISMAAFA NFATEATGFS EQYPGIVPSL LTLASNFRLP LYRDFMMSLG MCSVSRHSCE
     AILRSGPGRS IVIVTGGASE SLSARPGTND LTLKKRLGFI RLAIRNGASL VPIFSFGEND
     IYEQYDNKKG SLIWRYQKWF QKITGFTVPL AHARGIFNYN AGFIPFRHPI VTVVGKPIAV
     PLLAEGETEP SEEQMHQVQA QYIESLQAIY DKYKDIYAKD RIKDMTMIA