PHLD_BOVIN
ID PHLD_BOVIN Reviewed; 839 AA.
AC P80109;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
DE Short=PI-G PLD;
DE EC=3.1.4.50 {ECO:0000269|PubMed:2017684, ECO:0000269|PubMed:2170394};
DE AltName: Full=Glycoprotein phospholipase D;
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D;
DE Short=GPI-PLD;
DE Short=GPI-specific phospholipase D;
DE Flags: Precursor;
GN Name=GPLD1; Synonyms=PIGPLD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=2017684; DOI=10.1126/science.2017684;
RA Scallon B.J., Fung W.-J.C., Tsang T.C., Li S., Kado-Fong H., Huang K.-S.,
RA Kochan J.P.;
RT "Primary structure and functional activity of a phosphatidylinositol-
RT glycan-specific phospholipase D.";
RL Science 252:446-448(1991).
RN [2]
RP PROTEIN SEQUENCE OF 36-50; 56-77; 126-138; 181-185; 235-261; 380-408;
RP 449-477; 623-636; 678-692 AND 776-807, GLYCOSYLATION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Serum;
RX PubMed=2170394; DOI=10.1016/s0021-9258(18)38225-5;
RA Huang K.S., Li S., Fung W.J., Hulmes J.D., Reik L., Pan Y.C., Low M.G.;
RT "Purification and characterization of glycosyl-phosphatidylinositol-
RT specific phospholipase D.";
RL J. Biol. Chem. 265:17738-17745(1990).
RN [3]
RP PROTEIN SEQUENCE OF 24-50; 126-138; 145-164; 353-367; 569-579; 693-708 AND
RP 750-773.
RC TISSUE=Serum;
RX PubMed=1606959; DOI=10.1111/j.1432-1033.1992.tb16981.x;
RA Hoener M.C., Brodbeck U.;
RT "Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic
RT glycoprotein that in serum is associated with high-density lipoproteins.";
RL Eur. J. Biochem. 206:747-757(1992).
RN [4]
RP FUNCTION, MUTAGENESIS OF TYR-834, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=9042330; DOI=10.1016/s0167-4889(96)00119-x;
RA Stadelmann B., Buetikofer P., Koenig A., Brodbeck U.;
RT "The C-terminus of glycosylphosphatidylinositol-specific phospholipase D is
RT essential for biological activity.";
RL Biochim. Biophys. Acta 1355:107-113(1997).
CC -!- FUNCTION: This protein hydrolyzes the inositol phosphate linkage in
CC proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus
CC releasing these proteins from the membrane.
CC {ECO:0000269|PubMed:9042330}.
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 Evidence={ECO:0000269|PubMed:2017684, ECO:0000269|PubMed:2170394};
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9042330}.
CC Note=Associated with the High-Density Lipoproteins (HDL).
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:2170394,
CC ECO:0000269|PubMed:9042330}.
CC -!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
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DR EMBL; M60804; AAA30721.1; -; mRNA.
DR PIR; A56337; A56337.
DR RefSeq; NP_777241.1; NM_174816.2.
DR AlphaFoldDB; P80109; -.
DR STRING; 9913.ENSBTAP00000006557; -.
DR iPTMnet; P80109; -.
DR PaxDb; P80109; -.
DR PRIDE; P80109; -.
DR GeneID; 287025; -.
DR KEGG; bta:287025; -.
DR CTD; 2822; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P80109; -.
DR OrthoDB; 743479at2759; -.
DR BRENDA; 3.1.4.50; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IDA:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR GO; GO:0071401; P:cellular response to triglyceride; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR GO; GO:0070633; P:transepithelial transport; ISS:UniProtKB.
DR Gene3D; 2.130.10.130; -; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001028; Gprt_PLipase_D.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR029002; PLPC/GPLD1.
DR Pfam; PF01839; FG-GAP; 4.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00718; PHPHLIPASED.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; HDL; Hydrolase; Lipid metabolism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1606959"
FT CHAIN 24..839
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /id="PRO_0000022053"
FT REPEAT 365..427
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 434..496
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 498..558
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 562..622
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 632..692
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 703..769
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 787..839
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 834
FT /note="Y->A: Severe loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:9042330"
FT CONFLICT 181
FT /note="H -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="V -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="W -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="W -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="P -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 92602 MW; F9BFF8A00226BF40 CRC64;
MSAFRFWSGL LMLLGFLCPR SSPCGISTHI EIGHRALEFL HLQDGSINYK ELLLRHQDAY
QAGSVFPDSF YPSICERGQF HDVSESTHWT PFLNASVHYI RKNYPLPWDE DTEKLVAFLF
GITSHMVADV NWHSLGIEQG FLRTMAAIDF HNSYPEAHPA GDFGGDVLSQ FEFKFNYLSR
HWYVPAEDLL GIYRELYGRI VITKKAIVDC SYLQFLEMYA EMLAISKLYP TYSVKSPFLV
EQFQEYFLGG LEDMAFWSTN IYHLTSYMLK NGTSNCNLPE NPLFITCGGQ QNNTHGSKVQ
KNGFHKNVTA ALTKNIGKHI NYTKRGVFFS VDSWTMDSLS FMYKSLERSI REMFIGSSQP
LTHVSSPAAS YYLSFPYTRL GWAMTSADLN QDGYGDLVVG APGYSHPGRI HVGRVYLIYG
NDLGLPRIDL DLDKEAHGIL EGFQPSGRFG SAVAVLDFNV DGVPDLAVGA PSVGSEKLTY
TGAVYVYFGS KQGQLSSSPN VTISCQDTYC NLGWTLLAAD VNGDSEPDLV IGSPFAPGGG
KQKGIVAAFY SGSSYSSREK LNVEAANWMV KGEEDFAWLG YSLHGVNVNN RTLLLAGSPT
WKDTSSQGHL FRTRDEKQSP GRVYGYFPPI CQSWFTISGD KAMGKLGTSL SSGHVMVNGT
RTQVLLVGAP TQDVVSKVSF LTMTLHQGGS TRMYELTPDS QPSLLSTFSG NRRFSRFGGV
LHLSDLDNDG LDEIIVAAPL RITDATAGLM GEEDGRVYVF NGKQITVGDV TGKCKSWVTP
CPEEKAQYVL ISPEAGSRFG SSVITVRSKE KNQVIIAAGR SSLGARLSGV LHIYRLGQD
