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Database: UniProt
Entry: U5DET4_AMBTC
LinkDB: U5DET4_AMBTC
Original site: U5DET4_AMBTC 
ID   U5DET4_AMBTC            Unreviewed;       848 AA.
AC   U5DET4;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN   ORFNames=AMTR_s00071p00126030 {ECO:0000313|EMBL:ERN19957.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN19957.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC       phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798,
CC         ECO:0000256|PIRNR:PIRNR036470};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913,
CC         ECO:0000256|PIRNR:PIRNR036470};
CC   -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR   EMBL; KI392062; ERN19957.1; -; Genomic_DNA.
DR   RefSeq; XP_006858490.1; XM_006858428.2.
DR   AlphaFoldDB; U5DET4; -.
DR   STRING; 13333.U5DET4; -.
DR   EnsemblPlants; ERN19957; ERN19957; AMTR_s00071p00126030.
DR   GeneID; 18448359; -.
DR   Gramene; ERN19957; ERN19957; AMTR_s00071p00126030.
DR   KEGG; atr:18448359; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_004684_0_0_1; -.
DR   OMA; MDMMYRI; -.
DR   OrthoDB; 3014064at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   CDD; cd04015; C2_plant_PLD; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR024632; PLipase_D_C.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR011402; PLipase_D_pln.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF153; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   PIRSF; PIRSF036470; PLD_plant; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR036470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT   DOMAIN          1..147
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          352..387
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          694..721
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   848 AA;  95871 MW;  41C2BB70C05AD7C1 CRC64;
     MAESIHGSES EKVIFLHGDL DLSILEAKSL PNMDLVSERM RKCFTMFGTC KIPCKHGEKH
     KGSKHKIITS DPYVSVCLAG ATVAQTRIIS NCEDPSWDEQ FHVSIAHPVS KVEFQVKDND
     VLGAELIGVV SISAEKIQTG NTITGWFPIL GQYGNPFKPY PELHLSMQFR PVENNPLYKD
     GVGAGPDYLG VPNTYFPLRR GGKVTLYQDA HVPDELLPEI QLDGGKLLQH NKCWEDICHA
     ILEAHHLIYI IGWSIFHKVK LVREPTRPLP NGGELSLGDL LKFKSQEGVR VVLLIWDDKT
     SHDMLLLKTE GVMQTHDEQT LKFFKHSSVH CALSPRYASN KLSIFKQQVV GTLFTHHQKC
     VLVDTQASGN NRKITAFIGG LDLCDGRYDT PEHRLFRDLD SVFANDFHNP TFATCTRGPR
     QPWHDLHCKI EGPAAYDILT NFEQRWRKAT KWREFKLKKV THWHDDALIK LERISWILSP
     STSVPSDDFN LWVSHEDDGE CWHVQVFRSI DSGSVKGFPK VGQEAEAKNL VCGKNLVIDK
     SIHAAYVKAI RSAQHFIYIE NQYFLGSSYH WPSYKNAGAD NLIPMELALK IASKIVANER
     FAVYIVIPMW PEGVPASASV QEILFWQGQT MDMMYRIIGQ ALQQAGLAGK SHPQDYLNFY
     CLGNRERGPR ERLASTSQPS ENSVLGLTQK FRRFMVYVHS KGMIVDDEYV ILGSANINQR
     SMDGSRDTEI AMGAYQPHHK WAGSKGPPHG QVYGYRVSLW AEHLGFLEEC FHTPESMECV
     TRVNHFAEYN WRTFISEEVK DMKGHLMRYP IKVDSEGRVG PLPGHECFPD VGGRILGSHN
     SLPDSLTT
//
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