PLDC_DICDI
ID PLDC_DICDI Reviewed; 1640 AA.
AC Q54Z25;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phospholipase D C;
DE EC=3.1.4.4;
DE AltName: Full=Phosphatase D1;
DE Short=PLD 1;
GN Name=pldC; Synonyms=pld1; ORFNames=DDB_G0277949;
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 FUNCTION.
RX PubMed=6498208; DOI=10.1016/0005-2760(84)90343-6;
RA Ellingson J.S., Dischinger H.C.;
RT "Comparison of the hydrolysis of phosphatidylethanolamine and
RT phosphatidyl(N-acyl)ethanolamine in Dictyostelium discoideum amoebae.";
RL Biochim. Biophys. Acta 796:155-162(1984).
RN [3]
RP FUNCTION.
RX PubMed=8394342; DOI=10.1016/s0021-9258(19)85353-x;
RA Cubitt A.B., Dharmawardhane S., Firtel R.A.;
RT "Developmentally regulated changes in 1,2-diacylglycerol in Dictyostelium.
RT Regulation by light and G proteins.";
RL J. Biol. Chem. 268:17431-17439(1993).
RN [4]
RP NOMENCLATURE.
RX PubMed=15225639; DOI=10.1016/j.febslet.2004.05.071;
RA Rigden D.J.;
RT "A distant evolutionary relationship between GPI-specific phospholipase D
RT and bacterial phosphatidylcholine-preferring phospholipase C.";
RL FEBS Lett. 569:229-234(2004).
RN [5]
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=15769249; DOI=10.1042/bj20050085;
RA Zouwail S., Pettitt T.R., Dove S.K., Chibalina M.V., Powner D.J.,
RA Haynes L., Wakelam M.J.O., Insall R.H.;
RT "Phospholipase D activity is essential for actin localization and actin-
RT based motility in Dictyostelium.";
RL Biochem. J. 389:207-214(2005).
RN [6]
RP NOMENCLATURE.
RX PubMed=16762450; DOI=10.1016/j.ejcb.2006.04.011;
RA Vlahou G., Rivero F.;
RT "Rho GTPase signaling in Dictyostelium discoideum: insights from the
RT genome.";
RL Eur. J. Cell Biol. 85:947-959(2006).
CC -!- FUNCTION: Plays a role in cell growth. Hydrolyzes membrane
CC phospholipids, such as PtdCho (phosphatidylcholine), producing the free
CC headgroup and PtdOH (phosphatidic acid; signaling molecule on its own).
CC Involved in the inhibition of actin-based motility and endocytosis. Its
CC inhibition causes complete collapse of F-actin organization.
CC {ECO:0000269|PubMed:15769249, ECO:0000269|PubMed:6498208,
CC ECO:0000269|PubMed:8394342}.
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 {ECO:0000269|PubMed:15769249}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68147.1; -; Genomic_DNA.
DR RefSeq; XP_642027.1; XM_636935.1.
DR AlphaFoldDB; Q54Z25; -.
DR SMR; Q54Z25; -.
DR STRING; 44689.DDB0231508; -.
DR PaxDb; Q54Z25; -.
DR EnsemblProtists; EAL68147; EAL68147; DDB_G0277949.
DR GeneID; 8621238; -.
DR KEGG; ddi:DDB_G0277949; -.
DR dictyBase; DDB_G0277949; pldC.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_242871_0_0_1; -.
DR InParanoid; Q54Z25; -.
DR OMA; DYINSCI; -.
DR PhylomeDB; Q54Z25; -.
DR BRENDA; 3.1.4.4; 1939.
DR Reactome; R-DDI-1483166; Synthesis of PA.
DR Reactome; R-DDI-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR PRO; PR:Q54Z25; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; ISS:dictyBase.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:dictyBase.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome; Repeat.
FT CHAIN 1..1640
FT /note="Phospholipase D C"
FT /id="PRO_0000367472"
FT DOMAIN 1009..1036
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 1460..1487
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 122..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1021
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 1640 AA; 188250 MW; 58A9DF1E84EA6776 CRC64;
MYFFTPPQKR TLKPVVDRVL QQQQQQQQQQ QQQSLPKFQP FEVETYSLED EKYLYNISYF
SKEEIKLLYD LFHRINLDLD GFTENIIYQT LSFLVHIPSG IEELSSLFYN EDVIYRKEIN
SSHRSNQSFN HSNSTTPLNT TNNNIKKPTT TTTTNSNNIN NNGNVNGNNT TNLDDILNNH
NDNYSSDNSY LHNIYDDIYE DEDDEDDEDD DDDEDEDDEG KEFEQDDEDE STISSMSLKN
SQAKRLSKKM NSIDLNVDEI SSTHNQNHQN HQNHQNHHHH TTTHMIEKKI TTTINKIKQK
ISNESSGLLC EVVGAGGAGT EGASSSTTTT TTLSNDLQTN ESIKFVEDEK QQLKQQLRKQ
LLKDGNHNSL NNILYDYKHP NDINTPIEEL TAAATTTTTT TSTTTTTNDH QNLEKTIISN
KTIKKLEGVE TIKDTVELEK QQQKQQQTSN VTTAKVKDTI LSSSPKTTTT ATTNNNNNNN
NNNNNNNNNN NNNNSYKYNS YLESSNISNI SNASYTDKPM DDEYYYGEYD DEDDSKPPSQ
EKIESINLYR SQFSIIRDCN LWGGKTLKED EFDYIDSSSE ILKYRMIIKY MVENLFSYIR
KRYNLEANKN PSIIHLIEII SIMTRGTLKE KSELVFKLVR KKSEGVVYKT ELLEMIQGID
ALTVLNVFGL GSIGTPDEVV NNIYREGLST VNSIQRTPSF PRSDSFYQKS MSSEQPFFKD
TSLEMKEFIK RSVSNSDIPR CFGFFDLIYL CYIKPIEDYL KSSIKYKQAS GYLYYEKYLG
IIKAYSLRWF EVRSGFLIGY KRLFSKPSKV ICLFKTNVKI IPKEHPKHHM KLKSLFKGSL
SKQIDGNKEA TDFVLRRFDD TEQTFISLSS HRASNFVNAI RENSKGSYRY HSFASPQEDI
NVVPYINGST YFKGVYKALK HATSEIYIAG WWISPNVSLN RTATSKTPDK YRLDSVLMKK
ASEGVKIYIL IWDETMIAMD LGSRGVKSFF EKMHRRNIKV IRHPHMLPLY WSHHQKVVVV
DQRIAFIGGL DLCFGRYDNE YYFVKDNLEI NFPGADYINS CIAKPVNNLK DCLVDRNTQP
RMPWHDVSIS LDGKAARDVT YNFIQRWNHA KDSNRDYKSY PYLITSLETP LNIPHPQPPT
QFLHPNTNIN NNNNNANNNT NNINNNNNNN NINNLNSSTN TTNNTNNTTT TTNNNNLNTS
TNMLPINNNN NNLNTSTNIL PNNNNNNNNN NNNNNNNNNN NNNNNNNINN NNTTSTTTTT
TTNNNLNSSS NNLNFNISGE IHNNSLPHQL NNQQQQQHHH HHHHHYQPPL PPQQRGTCKV
QIVRSVCGWS AGQVLENSIY KAYLNLINLS QHFIYIQNQF FISSVGFTQP NNQIAFAIYK
RIEKAVLLNQ VFRVILLLPV HCEGDIYDVD TQLIIKYTEK SITGIKTELL KKFPEMDIDQ
YLSINSLRNW DANGDIIFTE QIYVHSKVLI VDDKIAIIGS ANINDRSLNG SRDSEICAII
EDRDLVDSRV NGLPYKAAKF AHNLRCNLWE YHLGLISNPD PLLSDRIKDL VIDSTYHDIW
RNMAQRNSAI YKEIFGTTIP ENCTKTSQYN RGSIKLTSEA LETLCGINGF LIEYNTSMLS
ELETPTSIYS DIITSMKLFL
