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Database: UniProt
Entry: K7AF65_PHLPR
LinkDB: K7AF65_PHLPR
Original site: K7AF65_PHLPR 
ID   K7AF65_PHLPR            Unreviewed;       597 AA.
AC   K7AF65;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   03-MAY-2023, entry version 20.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE   Flags: Fragment;
OS   Phleum pratense (Common timothy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poodinae;
OC   Phleinae; Phleum.
OX   NCBI_TaxID=15957 {ECO:0000313|EMBL:JAA00169.1};
RN   [1] {ECO:0000313|EMBL:JAA00169.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pollen {ECO:0000313|EMBL:JAA00169.1};
RX   PubMed=23401558; DOI=10.1073/pnas.1300512110;
RA   Schulten V., Greenbaum J.A., Hauser M., McKinney D.M., Sidney J., Kolla R.,
RA   Lindestam Arlehamn C.S., Oseroff C., Alam R., Broide D.H.,
RA   Ferreira-Briza F., Grey H.M., Sette A., Peters B.;
RT   "Previously undescribed grass pollen antigens are the major inducers of T
RT   helper 2 cytokine-producing T cells in allergic individuals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:3459-3464(2013).
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};
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DR   EMBL; GAAJ01000295; JAA00169.1; -; mRNA.
DR   AlphaFoldDB; K7AF65; -.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR024632; PLipase_D_C.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF67; PHOSPHOLIPASE D; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963}.
FT   DOMAIN          113..153
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          443..470
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAA00169.1"
SQ   SEQUENCE   597 AA;  67113 MW;  A8277FD89C285DDD CRC64;
     FAAISNAKHL IYVTGWSVYT EITLLRDANR PKPAGGTVTL GELLKKKASE GVRVLMLVWD
     DRTSVGVLKK DGLMATHDEE TMNYFQDTDV HCVLCPRDPD DSGSIVQDLQ ISTMFTHHQK
     IVVVDHDMPQ PQSASRRRRI MSFVGGLDLC DGRYDTPFHS VFGTLDGAHH DDFHQPNFAT
     SAITKGGPRE PWHDIHCRLE GPVAWDVLYN FEQRWRKQGG KDLLIQLRDL ADEIIPPSPV
     VYAEDREAWN VQLFRSIDGG AAFGFPDTPE DAARAGLVSG KDQIIDRSIQ DAYICTIRRA
     KSFIYIENQY FLGSSYCWKP DGIKPDDVGA LHLIPKELSM KVVSKIEAGE RFTVYVVVPM
     WPEGIPASGS VQAILDWQRR TMEMMYTDIA QAIQAKGIDA NPKDYLTFFC LGNREAKKAG
     EYEPPEPAEP DSDYLKAQQN RRFMIYVHTK MMIVDDEYII VGSANINQRS MDGARDSEIA
     MGAYQPYHLA ASRPARGQVH GFRMALWYEH LGMVDEAFQR PESVECVRKV NAMADRYWNL
     YAGDGPERDL PGHLLTYPVG VTSDGTVTQL PGVEFFPDTQ ARILGAKSDY LPPILTT
//
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