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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_MOUSE              Reviewed;         837 AA.
O70362;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 128.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Glucagonoma;
PubMed=9716655; DOI=10.1007/s003359900851;
LeBoeuf R.C., Caldwell M., Guo Y., Metz C., Davitz M.A., Olson L.K.,
Deeg M.A.;
"Mouse glycosylphosphatidylinositol-specific phospholipase D (Gpld1)
characterization.";
Mamm. Genome 9:710-714(1998).
[2]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-655.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-496.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: This protein hydrolyzes the inositol phosphate linkage
in proteins anchored by phosphatidylinositol glycans (GPI-anchor)
thus releasing these proteins from the membrane.
{ECO:0000269|PubMed:9716655}.
-!- 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. Note=Associated with the High-
Density Lipoproteins (HDL). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9716655}.
-!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
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EMBL; AF050666; AAC77799.1; -; mRNA.
UniGene; Mm.291831; -.
ProteinModelPortal; O70362; -.
STRING; 10090.ENSMUSP00000021773; -.
iPTMnet; O70362; -.
PhosphoSitePlus; O70362; -.
MaxQB; O70362; -.
PaxDb; O70362; -.
PeptideAtlas; O70362; -.
PRIDE; O70362; -.
MGI; MGI:106604; Gpld1.
eggNOG; ENOG410IPB3; Eukaryota.
eggNOG; ENOG4111ZDA; LUCA.
HOVERGEN; HBG008185; -.
InParanoid; O70362; -.
BRENDA; 3.1.4.50; 3474.
PRO; PR:O70362; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:UniProtKB.
GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IDA:UniProtKB.
GO; GO:0004630; F:phospholipase D activity; IDA:MGI.
GO; GO:0017080; F:sodium channel regulator activity; IMP:UniProtKB.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
GO; GO:0071401; P:cellular response to triglyceride; ISS:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; IEP:UniProtKB.
GO; GO:0002430; P:complement receptor mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IDA:UniProtKB.
GO; GO:0001503; P:ossification; IEP: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; ISS:UniProtKB.
GO; GO:0045919; P:positive regulation of cytolysis; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:UniProtKB.
GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; IMP:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
GO; GO:0070633; P:transepithelial transport; IMP: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;
Complete proteome; Glycoprotein; HDL; Hydrolase; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000250}.
CHAIN 24 837 Phosphatidylinositol-glycan-specific
phospholipase D.
/FTId=PRO_0000022054.
REPEAT 364 425 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 431 492 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 494 554 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 561 619 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 629 689 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 701 767 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 785 837 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 586 586 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 655 655 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
SEQUENCE 837 AA; 93255 MW; 9D007F479556CCC1 CRC64;
MSAGRLWSSL LLLLPLFCSK SSSCGLSTHV EIGHRALEFL RLQDGRINYK ELILEHQDAY
QAGTVFPDAF YPSICKRGKY HDVSERTHWT PFLNASIHYI RENYPLPWEK DTEKLVAFLF
GITSHMVADL SWHNLGFLRT MGAIDFYNSY SDAHSAGDFG GDVLSQFEFN FNYLSRRWYV
PVRDLLRIYD NLYGRKVITK DVLVDCTYLQ FLEMHGEMFA VSKLYSTYST KSPFLVEQFQ
DYFLGGLDDM AFWSTNIYRL TSFMLENGTS DCNLPENPLF ISCDGRNHTL SGSKVQKNDF
HRNLTMFISR DIRKNLNYTE RGVFYSTGSW ARPESVTFMY QTLERNLRLM LAGSSQKNLN
HVSSPSASYT LSVPYARLGW VMTSADLNQD GHGDLVVGAP GYSHPGRFQI GRVYIIYGND
LGLPPIDLDL NKEGILEGFQ PSGRFGSALA VLDFNQDGLP DLAVGAPSVG SGQLTYNGSV
YVYYGSQQGR LSSSPNVTIS CKDTYCNLGW TLLATDADGD GRHDLVISSP FAPGGRKQKG
IVATFYSHPR RNDKELLTLE EADWKVNGEE DFSWFGYSLH GVTVANRSLL LIGSPTWKNV
SRMARSSHKK NQEEKSLGKV YGYFLPNRQS TITISGDKAM GKLGTSLSSG YVRVNGTLTQ
VLLVGAPTHD DVSKMAFLTM TLHQGGATRM YELAPEKTQP ALLSTFSGDR RFSRFGSVLH
LTDLDDDGLD EIIMAAPLRI TDVTSGLLGG EDGRVYIYNG MYTTLGDMTG KCKSWMTPCP
EEKAQYVLTS PEASSRFGSS LVSVRSKGRN QVVVAAGRSS WGARLSGALH VYSFSSD


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