PLD1_SCHPO
ID PLD1_SCHPO Reviewed; 1369 AA.
AC Q09706;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phospholipase D1;
DE Short=PLD 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=pld1; ORFNames=SPAC2F7.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=20579106; DOI=10.1111/j.1567-1364.2010.00646.x;
RA Harkins A.L., Yuan G., London S.D., Dolan J.W.;
RT "An oleate-stimulated, phosphatidylinositol 4,5-bisphosphate-independent
RT phospholipase D in Schizosaccharomyces pombe.";
RL FEMS Yeast Res. 10:717-726(2010).
CC -!- FUNCTION: Required for meiosis and spore formation. Seems to be
CC involved in the coordinate induction of late meiotic events.
CC {ECO:0000269|PubMed:20579106}.
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:0000269|PubMed:20579106};
CC -!- ACTIVITY REGULATION: Activity is slightly stimulated by oleate.
CC {ECO:0000269|PubMed:20579106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90503.1; -; Genomic_DNA.
DR PIR; T38564; S58160.
DR RefSeq; NP_592986.1; NM_001018386.2.
DR AlphaFoldDB; Q09706; -.
DR SMR; Q09706; -.
DR BioGRID; 278542; 1.
DR STRING; 4896.SPAC2F7.16c.1; -.
DR iPTMnet; Q09706; -.
DR MaxQB; Q09706; -.
DR PaxDb; Q09706; -.
DR PRIDE; Q09706; -.
DR EnsemblFungi; SPAC2F7.16c.1; SPAC2F7.16c.1:pep; SPAC2F7.16c.
DR GeneID; 2542065; -.
DR KEGG; spo:SPAC2F7.16c; -.
DR PomBase; SPAC2F7.16c; pld1.
DR VEuPathDB; FungiDB:SPAC2F7.16c; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_2_1; -.
DR InParanoid; Q09706; -.
DR OMA; CAVHNTE; -.
DR PhylomeDB; Q09706; -.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR PRO; PR:Q09706; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:PomBase.
DR GO; GO:0004630; F:phospholipase D activity; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:PomBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IC:PomBase.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR PANTHER; PTHR18896; PTHR18896; 3.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Meiosis;
KW Reference proteome; Repeat; Sporulation.
FT CHAIN 1..1369
FT /note="Phospholipase D1"
FT /id="PRO_0000218826"
FT DOMAIN 208..379
FT /note="PX"
FT DOMAIN 641..668
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 941..968
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 27..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 157731 MW; DAA4D82B116817BD CRC64;
MTIHQGGNSV IDNVPYSLNT NVNDSIYSEK GTGRKDAEDH TPSKITDLEK NVDHSIPSFP
ENDPKNYSEF VNLNPPKRPD LEHTRGSSWH TASENVNDLA ANDSTRVQTP EFITQTMEDE
NVEVPPLERD ERDAAAAHTS KANRNSARQM WAQLMASVRK FKREDEKPIL KENLPAINLF
EAGIPASLPI AKHFIRDKSG QPVLPIITDL IKVSVLDVEP KHNRIHSTFT IQVEYGTGPH
AIRWLIYRQL RDFINLHSHF LFFEFQHRFS GRRMKLPKFP KEVLPYLVKL RGYQKILYSN
PSDQLIDETH SISDISWESH SQDGDRTTGQ PRHANNGRKK HGNFWTIQGN TLGVYLQEMI
HNLQFFPEVN VLYSFLEFSS LGLYLAGAGT FHGKEGFATL KRNYSPTQYM LCCNTTMMKT
RSQPFWIIVS ESCIILCDNM LSMQPADVFI WDVDFEITRK NFRKAHSKDT NEKIRLSHHS
FKIKNRQKVM KLSVRSGRWL QQFINSVQVA QGLTAWCEIH RFDSFAPVRT NVAVQWMVDA
RDHMWNVSRA IKNAKRCIMI HGWWLSPELQ MRRPYSMAHK WRIDRILNEK AHEGVMVYIM
IYRNIDATIP IDSFHTKEHL QSLHPNIYVI RSPSHFRQNA LFWAHHEKLV VVDDAITFIG
GIDLCFGRYD TPQHILYDDK PVADKTGLCE QTWRGKDYSN ARVHDFFDLT EPYKDMYDRL
AVPRMGWHDV SMCIIGQPAR DAARHFVQRW NYLIQCKKPA RKTPLLIPPP DFTTDQLTDS
QLTGTCEVQV LRSAGLWSLG LVDTVEQSIQ NAYVTCIEKS EHFIYIENQF FVTSTTCEGT
TIENRVGDAL VERIIRAHKN NEKWRGVIMI PLLPGFEGQI DLQEGGSLRL IVECQYRSIC
HGEHSIFGRL NAKGIDGSKY LRFYGLRGWA HLGENHELVT EMIYVHAKIL IADDRVAVIG
SANINERSLL GNRDSEIAAV IRDTLTIDSK MDGKPYKVGK FAHTLRKRLM REHLGLETDV
LEQREYNMDG LDRDTEWKRV EVWTPDEGNA INGSAYTAEE LKMKYRSQSQ FTTTPDILRK
AEKSMKKLDQ RVSLIPSSIE FNIKTQKDKV EFEKNYEKSK KGPDVIANAL VGGIPLSLKT
KEDSLYELSK FSQCGEDQRP MVLKDPDHLV PEPSRPHCGN GLVFYDDIPL LEVNPISGET
IPKFDASSFE DPVCDEFFED IWSKVASNNT TIYRHIFRCV PDDEMLTWES YNEWKKYGKR
FKEEQARWRQ EELSNLHETH EKSENDPKNP KAGSQGSGNT SASEDSKTEK PKTRTNNGLQ
VPDKRVVYDL LRGIRGQLVE LPLKWMSTES NARNWLSSID KIPPLEIYD
