PLDG_DICDI
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 03-AUG-2022, entry version 114.
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 (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=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=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a
CC 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997,
CC 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}.
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DR EMBL; AAFI02000019; EAL68961.1; -; Genomic_DNA.
DR RefSeq; XP_642807.1; XM_637715.1.
DR AlphaFoldDB; Q86AV9; -.
DR STRING; 44689.DDB0229914; -.
DR PaxDb; Q86AV9; -.
DR EnsemblProtists; EAL68961; EAL68961; DDB_G0276919.
DR GeneID; 8620669; -.
DR KEGG; ddi:DDB_G0276919; -.
DR dictyBase; DDB_G0276919; pldG.
DR eggNOG; KOG3637; Eukaryota.
DR HOGENOM; CLU_011756_0_0_1; -.
DR InParanoid; Q86AV9; -.
DR OMA; SQSWFTI; -.
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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IBA:GO_Central.
DR GO; GO:0004630; F:phospholipase D activity; ISS:dictyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006507; P:GPI anchor release; ISS:dictyBase.
DR Gene3D; 2.130.10.130; -; 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 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; SSF69318; 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
