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Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D)

 PHLD_HUMAN              Reviewed;         840 AA.
P80108; Q15127; Q15128; Q2M2F2; Q5T3Y0; Q7Z6T8; Q8TCV0; Q8WW82;
Q96ID6; Q9H167; Q9H4M1; Q9UJC9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 3.
27-SEP-2017, entry version 149.
RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
Short=PI-G PLD;
EC=3.1.4.50;
AltName: Full=Glycoprotein phospholipase D;
AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D;
Short=GPI-PLD;
Short=GPI-specific phospholipase D;
Flags: Precursor;
Name=GPLD1; Synonyms=PIGPLD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-30; VAL-350;
MET-461 AND ILE-698.
TISSUE=Liver, and Pancreas;
Tsang T.C., Fung W.-J.C., Levine J., Metz C.N., Davitz M.A.,
Burns D.K., Huang K.-S., Kochan J.P.;
"Isolation and expression of two human glycosylphosphatidylinositol
phospholipase D (GPI-PLD) cDNAs.";
FASEB J. 6:A1922-A1922(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 384-840, AND VARIANTS ILE-30; VAL-694 AND ILE-698.
TISSUE=Liver;
PubMed=11072085; DOI=10.1016/S0167-4781(00)00194-9;
Schofield J.N., Rademacher T.W.;
"Structure and expression of the human glycosylphosphatidylinositol
phospholipase D1 (GPLD1) gene.";
Biochim. Biophys. Acta 1494:189-194(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-698.
TISSUE=Bone marrow;
Tang J.H., Gu S.L., Zhang X.J.;
"Preliminary study of the gene structure of human
glycosylphosphatidylinositol specific phospholipase D.";
Hunan Yi Ke Da Xue Xue Bao 26:96-97(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 266-840 (ISOFORM 1), AND VARIANTS
VAL-17; ILE-30 AND ILE-698.
TISSUE=Eye, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Serum;
PubMed=1606959; DOI=10.1111/j.1432-1033.1992.tb16981.x;
Hoener M.C., Brodbeck U.;
"Phosphatidylinositol-glycan-specific phospholipase D is an
amphiphilic glycoprotein that in serum is associated with high-density
lipoproteins.";
Eur. J. Biochem. 206:747-757(1992).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
-!- FUNCTION: This protein hydrolyzes the inositol phosphate linkage
in proteins anchored by phosphatidylinositol glycans (GPI-anchor)
thus releasing these proteins from the membrane.
-!- CATALYTIC ACTIVITY: 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-
myo-inositol + H(2)O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol +
phosphatidate.
-!- SUBUNIT: Monomer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P80108-1; Sequence=Displayed;
Name=2;
IsoId=P80108-2; Sequence=VSP_023261, VSP_023262;
-!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36444.1; Type=Miscellaneous discrepancy; Note=This sequence has numerous of conflicts with the human genome.; Evidence={ECO:0000305};
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EMBL; L11701; AAA36444.1; ALT_SEQ; mRNA.
EMBL; L11702; AAA36445.1; -; mRNA.
EMBL; AJ308108; CAC87068.1; -; mRNA.
EMBL; AJ400872; CAC14844.1; -; Genomic_DNA.
EMBL; AJ400873; CAC14844.1; JOINED; Genomic_DNA.
EMBL; AJ400874; CAC14844.1; JOINED; Genomic_DNA.
EMBL; AJ400875; CAC14844.1; JOINED; Genomic_DNA.
EMBL; AJ400876; CAC14844.1; JOINED; Genomic_DNA.
EMBL; AY007546; AAG16627.2; -; mRNA.
EMBL; AL359713; CAI17103.1; -; Genomic_DNA.
EMBL; AL031230; CAI17103.1; JOINED; Genomic_DNA.
EMBL; AL031230; CAI22602.1; -; Genomic_DNA.
EMBL; AL359713; CAI22602.1; JOINED; Genomic_DNA.
EMBL; AL031230; CAD92520.1; -; Genomic_DNA.
EMBL; BC007614; AAH07614.1; -; mRNA.
EMBL; BC020748; AAH20748.1; -; mRNA.
EMBL; BC093645; AAH93645.1; -; mRNA.
EMBL; BC112001; AAI12002.1; -; mRNA.
CCDS; CCDS4553.1; -. [P80108-1]
RefSeq; NP_001494.2; NM_001503.3. [P80108-1]
UniGene; Hs.533291; -.
ProteinModelPortal; P80108; -.
BioGrid; 109083; 6.
STRING; 9606.ENSP00000230036; -.
iPTMnet; P80108; -.
PhosphoSitePlus; P80108; -.
BioMuta; GPLD1; -.
DMDM; 126302583; -.
PaxDb; P80108; -.
PeptideAtlas; P80108; -.
PRIDE; P80108; -.
DNASU; 2822; -.
Ensembl; ENST00000230036; ENSP00000230036; ENSG00000112293. [P80108-1]
GeneID; 2822; -.
KEGG; hsa:2822; -.
UCSC; uc003ned.3; human. [P80108-1]
CTD; 2822; -.
DisGeNET; 2822; -.
EuPathDB; HostDB:ENSG00000112293.14; -.
GeneCards; GPLD1; -.
H-InvDB; HIX0032817; -.
HGNC; HGNC:4459; GPLD1.
HPA; CAB008625; -.
HPA; HPA012500; -.
MIM; 602515; gene.
neXtProt; NX_P80108; -.
OpenTargets; ENSG00000112293; -.
PharmGKB; PA28842; -.
eggNOG; ENOG410IPB3; Eukaryota.
eggNOG; ENOG4111ZDA; LUCA.
GeneTree; ENSGT00390000013522; -.
HOVERGEN; HBG008185; -.
InParanoid; P80108; -.
KO; K01127; -.
OMA; AQYVLIS; -.
OrthoDB; EOG091G01DS; -.
PhylomeDB; P80108; -.
TreeFam; TF335726; -.
BRENDA; 3.1.4.50; 2681.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
SignaLink; P80108; -.
GeneWiki; GPLD1; -.
GenomeRNAi; 2822; -.
PRO; PR:P80108; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112293; -.
Genevisible; P80108; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; ISS:UniProtKB.
GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IDA:UniProtKB.
GO; GO:0004630; F:phospholipase D activity; IDA:UniProtKB.
GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0071397; P:cellular response to cholesterol; IMP:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
GO; GO:0071401; P:cellular response to triglyceride; IMP:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
GO; GO:0002430; P:complement receptor mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
GO; GO:0035701; P:hematopoietic stem cell migration; TAS:UniProtKB.
GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; TAS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB.
GO; GO:0001503; P:ossification; ISS:UniProtKB.
GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045919; P:positive regulation of cytolysis; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB.
GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISS:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0051047; P:positive regulation of secretion; ISS:UniProtKB.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
GO; GO:0070633; P:transepithelial transport; ISS:UniProtKB.
InterPro; IPR013517; FG-GAP.
InterPro; IPR001028; Gprt_PLipase_D.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR029002; PLPC/GPLD1.
Pfam; PF01839; FG-GAP; 3.
Pfam; PF00882; Zn_dep_PLPC; 1.
PRINTS; PR00718; PHPHLIPASED.
SMART; SM00191; Int_alpha; 5.
PROSITE; PS51470; FG_GAP; 7.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Glycoprotein; Hydrolase; Polymorphism; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 23
CHAIN 24 840 Phosphatidylinositol-glycan-specific
phospholipase D.
/FTId=PRO_0000022047.
REPEAT 367 428 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 436 497 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 499 559 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 563 623 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 633 693 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 704 770 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 788 840 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 165 176 GDVLSQFEFNFN -> TVYLHLLNFLVV (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_023261.
VAR_SEQ 177 840 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023262.
VARIANT 17 17 L -> V (in dbSNP:rs2235501).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030743.
VARIANT 30 30 V -> I (in dbSNP:rs1126617).
{ECO:0000269|PubMed:11072085,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1}.
/FTId=VAR_030744.
VARIANT 275 275 D -> E (in dbSNP:rs17300770).
/FTId=VAR_030745.
VARIANT 350 350 I -> V (in dbSNP:rs1062496).
{ECO:0000269|Ref.1}.
/FTId=VAR_051278.
VARIANT 396 396 G -> S (in dbSNP:rs6924628).
/FTId=VAR_030746.
VARIANT 461 461 V -> M (in dbSNP:rs1062505).
{ECO:0000269|Ref.1}.
/FTId=VAR_030747.
VARIANT 694 694 M -> V (in dbSNP:rs1042303).
{ECO:0000269|PubMed:11072085}.
/FTId=VAR_030748.
VARIANT 698 698 T -> I (in dbSNP:rs1772256).
{ECO:0000269|PubMed:11072085,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1, ECO:0000269|Ref.3}.
/FTId=VAR_030749.
CONFLICT 531 534 VIGS -> MLGT (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 840 AA; 92336 MW; 11369BAFEC3D6D38 CRC64;
MSAFRLWPGL LIMLGSLCHR GSPCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY
QAGIVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF
GITSHMAADV SWHSLGLEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR
RWYVPVKDLL GIYEKLYGRK VITENVIVDC SHIQFLEMYG EMLAVSKLYP TYSTKSPFLV
EQFQEYFLGG LDDMAFWSTN IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ
KNDFHRNLTT SLTESVDRNI NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL
SQKHVSSPLA SYFLSFPYAR LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHIGRVYLIY
GNDLGLPPVD LDLDKEAHRI LEGFQPSGRF GSALAVLDFN VDGVPDLAVG APSVGSEQLT
YKGAVYVYFG SKQGGMSSSP NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG
GKQKGIVAAF YSGPSLSDKE KLNVEAANWT VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP
TWKNASRLGH LLHIRDEKKS LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG
TLKQVLLVGA PTYDDVSKVA FLTVTLHQGG ATRMYALTSD AQPLLLSTFS GDRRFSRFGG
VLHLSDLDDD GLDEIIMAAP LRIADVTSGL IGGEDGRVYV YNGKETTLGD MTGKCKSWIT
PCPEEKAQYV LISPEASSRF GSSLITVRSK AKNQVVIAAG RSSLGARLSG ALHVYSLGSD


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E0269h ELISA kit 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC1,PLC-148,PLCG1,P 96T
E0269h ELISA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC1,PLC-148,PLCG1,PLC-ga 96T


 

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