ID   PLDY_DICDI              Reviewed;         438 AA.
AC   Q54K50; Q23849;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phospholipase D Y;
DE            EC=3.1.4.4;
DE   AltName: Full=Phosphatase D3;
DE            Short=PLD 3;
DE   Flags: Precursor;
GN   Name=pldY; Synonyms=pld3; ORFNames=DDB_G0287649;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-429, AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX3 / DH1;
RX   PubMed=2926809; DOI=10.1016/0022-2836(89)90364-1;
RA   Giorda R., Ohmachi T., Ennis H.L.;
RT   "Organization of a gene family developmentally regulated during
RT   Dictyostelium discoideum spore germination.";
RL   J. Mol. Biol. 205:63-69(1989).
CC   -!- FUNCTION: Hydrolyzes membrane phospholipids, such as PtdCho
CC       (phosphatidylcholine), producing the free headgroup and PtdOH
CC       (phosphatidic acid; signaling molecule on its own). {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Inhibited by butan-1-ol.
CC   -!- DEVELOPMENTAL STAGE: Expression is observed in spores, increases about
CC       two- to three-fold at 0.5 hour to 1 hour during spore germination, and
CC       then rapidly decreases. The mRNA is not detectable in vegetative cells
CC       or in early multicellular development on filters, but is present late
CC       during development, approximately at the time of sporulation.
CC       {ECO:0000269|PubMed:2926809}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA67429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000103; EAL63633.1; -; Genomic_DNA.
DR   EMBL; M19469; AAA67429.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_637114.1; XM_632022.1.
DR   AlphaFoldDB; Q54K50; -.
DR   SMR; Q54K50; -.
DR   STRING; 44689.DDB0220113; -.
DR   PaxDb; Q54K50; -.
DR   EnsemblProtists; EAL63633; EAL63633; DDB_G0287649.
DR   GeneID; 8626209; -.
DR   KEGG; ddi:DDB_G0287649; -.
DR   dictyBase; DDB_G0287649; pldY.
DR   eggNOG; KOG3603; Eukaryota.
DR   HOGENOM; CLU_027021_0_0_1; -.
DR   InParanoid; Q54K50; -.
DR   OMA; TSCCRRP; -.
DR   PhylomeDB; Q54K50; -.
DR   Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-DDI-2029485; Role of phospholipids in phagocytosis.
DR   PRO; PR:Q54K50; -.
DR   Proteomes; UP000002195; Chromosome 5.
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   InterPro; IPR032803; PLDc_3.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   Pfam; PF13918; PLDc_3; 1.
DR   SMART; SM00155; PLDc; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..438
FT                   /note="Phospholipase D Y"
FT                   /id="PRO_0000367473"
FT   DOMAIN          145..172
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   DOMAIN          373..399
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  49186 MW;  8CA94E4D3C1F2631 CRC64;
     MIINRLFIII VLFFVNVNSK IISESTLNSC QGGTIQIAES IPLGLDISTN LSTHDAWMDL
     ITNAQESIDL GFFYFTLLGG SDLDPVYGGQ LGIDIFNAIV EAHSRGINVR IVQNEPSESF
     PDTETQTLAK LGIQVRSIDW VSLVGSGVLH TKLIIIDESS AYVGSANADW SSLAQVKELG
     IVLKNCPTMV ADTEIAFQQY WNAADFTSLP INDWGSNYQA LFNNTNMASL SLNNNNNNNN
     KNKNNDNDGS GTNQMYEMFL AVSPPQFQST YRTGDIDALM DAINNADQSI CITVMDYTPT
     TLYNDPNTYW PLIDNALRAA AFNRNVQVRM LISHWNYTSP IIPQWLHSLN QVDNIQVRWF
     VVPDFSTNPQ IPYTRVNHAK FMVTEKQSYV GTSNWSQDYF TVTGGLSYNV FNNDFTNQLQ
     SIFNRDWNSP YTQPIQNF