PLDZ_DICDI
ID PLDZ_DICDI Reviewed; 422 AA.
AC Q54SA1;
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 Z;
DE EC=3.1.4.4;
DE AltName: Full=Phosphatase D3;
DE Short=PLD 3;
DE Flags: Precursor;
GN Name=pldZ; Synonyms=pld3; ORFNames=DDB_G0282579;
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).
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 -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66149.1; -; Genomic_DNA.
DR RefSeq; XP_640138.1; XM_635046.1.
DR AlphaFoldDB; Q54SA1; -.
DR SMR; Q54SA1; -.
DR STRING; 44689.DDB0231505; -.
DR PaxDb; Q54SA1; -.
DR EnsemblProtists; EAL66149; EAL66149; DDB_G0282579.
DR GeneID; 8623675; -.
DR KEGG; ddi:DDB_G0282579; -.
DR dictyBase; DDB_G0282579; pldZ.
DR eggNOG; KOG3603; Eukaryota.
DR HOGENOM; CLU_027021_0_0_1; -.
DR InParanoid; Q54SA1; -.
DR OMA; THFIPNT; -.
DR PhylomeDB; Q54SA1; -.
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:Q54SA1; -.
DR Proteomes; UP000002195; Chromosome 3.
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; PF00614; PLDc; 1.
DR Pfam; PF13918; PLDc_3; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..422
FT /note="Phospholipase D Z"
FT /id="PRO_0000367474"
FT DOMAIN 148..175
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 357..383
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 47101 MW; 844CFF1EE8CAA356 CRC64;
MMMKLLFLIA LFGCVVNSIR INNDNGLSFQ SNCLGGSIQI AESIPLALNL QSNLSTHDAW
MELITNAKKS IDMGIFYMTL TDGGQLDPVY GGQLGLDIYK ALVDANSRGV SIRIVQNQPS
SSMPDTDTQN LAKLGVQVRS INWPSLVGAG ILHTKVIVVD QVSAYLGSAN LDWRSLAQVK
ELGVLFQNCP SMVSDTEIAF QQYWDAAVVT ELPSDWGVQY QAAYNQTNMA SLLLNGNEKF
EMFLAVSPPQ FVSTDRTGDI DALVSAMNGA TKTICISVMD YIPASLYNSP NTFWPVMDNA
LRAAAYNRGV QVRMLISHWN HTNYAIPQWL HSLDQVNNID VRWFVVPDFP NEPQVPFTRV
NHAKYMVTDE QSYVGTSNWS EDYYTNTGGL SYNIYNDEFT SQLQSIFDRD WNSPYSFPVT
TY
