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DAT2D_SOYBN
ID   DAT2D_SOYBN             Reviewed;         329 AA.
AC   K7K424;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Diacylglycerol O-acyltransferase 2D {ECO:0000305};
DE            Short=GmDGAT2D {ECO:0000303|PubMed:27345221};
DE            EC=2.3.1.20 {ECO:0000269|PubMed:27345221};
GN   Name=DGAT2D {ECO:0000303|PubMed:27345221};
GN   OrderedLocusNames=Glyma01g156000 {ECO:0000312|EMBL:KRH76487.1};
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82;
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Williams 82;
RX   PubMed=27345221; DOI=10.1038/srep28541;
RA   Chen B., Wang J., Zhang G., Liu J., Manan S., Hu H., Zhao J.;
RT   "Two types of soybean diacylglycerol acyltransferases are differentially
RT   involved in triacylglycerol biosynthesis and response to environmental
RT   stresses and hormones.";
RL   Sci. Rep. 6:28541-28541(2016).
CC   -!- FUNCTION: Involved in triacylglycerol (TAG) synthesis. Catalyzes the
CC       acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using
CC       acyl-CoA. Can use oleoyl-CoA and linoleoyl-CoA as substrates. May play
CC       a role in TAG biosynthesis in different tissues in responses to
CC       environmental and hormonal cues. {ECO:0000269|PubMed:27345221}.
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:27345221};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:27345221}; Multi-pass membrane protein
CC       {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q9ASU1}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers and seeds. Expressed at
CC       low levels in roots, stems, leaves and pods.
CC       {ECO:0000269|PubMed:27345221}.
CC   -!- INDUCTION: Induced by heat shock, cold stress, insect biting and
CC       abscisic acid (ABA). Down-regulated by treatment with jasmonate.
CC       {ECO:0000269|PubMed:27345221}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KP752053; AKR16145.1; -; mRNA.
DR   EMBL; CM000834; KRH76487.1; -; Genomic_DNA.
DR   RefSeq; NP_001299586.1; NM_001312657.1.
DR   AlphaFoldDB; K7K424; -.
DR   STRING; 3847.GLYMA01G36011.1; -.
DR   PRIDE; K7K424; -.
DR   EnsemblPlants; KRH76487; KRH76487; GLYMA_01G156000.
DR   GeneID; 100784657; -.
DR   Gramene; KRH76487; KRH76487; GLYMA_01G156000.
DR   KEGG; gmx:100784657; -.
DR   eggNOG; KOG0831; Eukaryota.
DR   HOGENOM; CLU_023995_2_0_1; -.
DR   InParanoid; K7K424; -.
DR   OMA; STMFYVP; -.
DR   OrthoDB; 1347007at2759; -.
DR   BRENDA; 2.3.1.20; 2483.
DR   Proteomes; UP000008827; Chromosome 1.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR007130; DAGAT.
DR   Pfam; PF03982; DAGAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Glycerol metabolism;
KW   Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..329
FT                   /note="Diacylglycerol O-acyltransferase 2D"
FT                   /id="PRO_0000438911"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   329 AA;  36885 MW;  2C45FC7D5A3F7A94 CRC64;
     MAAEPVSDGG AAAEKLISGR EEFGDSSNLF SAILAMVLWL GAIHFNIALI LLAVFFLPLS
     KSLLVFGFLF GFMVLPINEK SRFGRRLSRF ICKHACNYFP ITLHVEDMKA FDPNRAYVFG
     YEPHSVLPIG IVALADHTGF MPLPKVKVLA SSTVFYTPFL RHLWTWLGLT PATKKNFISL
     LASGHSCILI PGGVQEAFHM QHGTEIAFLK ARRGFVRVAM VKGKPLVPVF CFGQSNVYKW
     WKPGGKLFLK FARAIKFTPI CFWGIFGSPL PFRHPMHVVV GRPIEVDKNR EPTTEEVAKI
     HGLFVEALQD LFERHKARAG YPNLELRIV
 
 
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