ID   PLDG_DICDI              Reviewed;         948 AA.
AC   Q86AV9; Q550X5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 129.
DE   RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
DE            Short=PI-G PLD;
DE            EC=3.1.4.50;
DE   AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D;
DE            Short=GPI-PLD;
DE            Short=GPI-specific phospholipase D;
DE   AltName: Full=Phospholipase G;
DE   Flags: Precursor;
GN   Name=pldG; ORFNames=DDB_G0276919;
OS   Dictyostelium discoideum (Social amoeba).
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
RP   IDENTIFICATION.
RX   PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA   Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA   Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT   "Changing patterns of gene expression in Dictyostelium prestalk cell
RT   subtypes recognized by in situ hybridization with genes from microarray
RT   analyses.";
RL   Eukaryot. Cell 2:627-637(2003).
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).
CC   -!- FUNCTION: Hydrolyzes the inositol phosphate linkage in proteins
CC       anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing
CC       these proteins from the membrane. May also cleave GPI anchor
CC       intermediates intracellularly.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-(alpha-D-glucosaminyl)-1-(1,2-diacyl-sn-glycero-3-
CC         phospho)-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-
CC         inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+);
CC         Xref=Rhea:RHEA:10832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57997, ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds Ca(2+). {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GPLD1 family. {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; AAFI02000019; EAL68961.1; -; Genomic_DNA.
DR   RefSeq; XP_642807.1; XM_637715.1.
DR   AlphaFoldDB; Q86AV9; -.
DR   STRING; 44689.Q86AV9; -.
DR   GlyCosmos; Q86AV9; 10 sites, No reported glycans.
DR   GlyGen; Q86AV9; 10 sites.
DR   PaxDb; 44689-Q86AV9; -.
DR   GeneID; 8620669; -.
DR   KEGG; ddi:DDB_G0276919; -.
DR   dictyBase; DDB_G0276919; pldG.
DR   VEuPathDB; AmoebaDB:DDB_G0276919; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   HOGENOM; CLU_011756_0_0_1; -.
DR   InParanoid; Q86AV9; -.
DR   OMA; CGMTTHN; -.
DR   PhylomeDB; Q86AV9; -.
DR   Reactome; R-DDI-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   PRO; PR:Q86AV9; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0004630; F:D-type glycerophospholipase activity; ISS:dictyBase.
DR   GO; GO:0140336; F:glycosylphosphatidylinositol phospholipase D activity; IEA:RHEA.
DR   GO; GO:0004621; F:GPI anchor phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   FunFam; 2.130.10.130:FF:000031; Phosphatidylinositol-glycan-specific phospholipase D; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 3.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR029002; PLPC/GPLD1.
DR   PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF00882; Zn_dep_PLPC; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 6.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR   PROSITE; PS51470; FG_GAP; 6.
PE   3: Inferred from homology;
KW   Calcium; Glycoprotein; Hydrolase; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..948
FT                   /note="Phosphatidylinositol-glycan-specific phospholipase
FT                   D"
FT                   /id="PRO_0000367826"
FT   REPEAT          451..512
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          526..588
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          596..656
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          663..724
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          799..861
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          895..948
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        535
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        749
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        788
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   948 AA;  105705 MW;  4592198420D3F9F2 CRC64;
     MKNKIILLWL LLIVILCTIS NVKGCGMTTH NTVARRAYNF SSFDGFEQYQ KYVSENFDVF
     DAGAAFPDFG YDCGGLANES EAAHWPPFLR AATKYLLETY PQPWSLDGIR LAVFLLGVTS
     HQIADISWHS IGGIQQGLIR AMAGQDFNGT YELAHGNADE GGEFELAYNY DLSWLSDKWY
     VPITDIKNIF HSMNYPRVDD ENLLRCNAIL YAGAMGVKIG GRFFYPEIAK KSPFLVDHYQ
     DYFIGGLDDM SIWTSYCWPV LMGWMDGEDI GDFCFIQPDP NNDDDNQHLR LHHKHSILKN
     GSKIKEALSK SILNEMKITN NGKGVTFSLP NSMEKAINQV LNKFNQNPIG TLLEKYLPNL
     FNNKNKFYQE NENEQYNHDE EELNIIDIDI DIEEEEQEEE EDKPIRMLSK NNNFKNYEYL
     NDKKKSSSSK LKNKSKKNII KLNSDSNDLG TNFTTIYGQN MYSYFGKDIR SKDLNGDGFD
     DLIISSPGFG VPGSMQTGCV YYIISNGSSV TIDGGSGFTS EFDIDQVATG KLCGNETHAK
     FGWNIDVLDF NLDGIFDIII GAPSSSNANL QYLGMIYIYL GEKNNPAGEW STESDLPSIT
     IQGIEYADTI GTVLRVADCN ADSNADLILG SPHSAGGGTQ RGTVQIFYSS KKRISGIPIS
     LNDADYYGHG EVDYEWFGYE IKVAGQGDSS TLLVGSPNYH DEETAIVNIG KITSFPYNVN
     LNSFDLNPKF VMVGVNKNDK LGYSYNMVNG SLFGLDNVND IMVLSLPTRG FGDDFDQVGE
     VVLIDIDNLS GFVEIKNVNL LLSIKGTTKY SRFGESLLIG KLESTDEFAR LFVGAPLWTD
     SIDTGPGCVF TFLPNQHLTN DPAVLKQNII NNTPVVIYDS THSIKTFRID DDSGSSGGRS
     FNNKRKDSRF GFRILLSDFN NDGKNDLIVS ADRDSSKILE GGSINIFQ
//