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   02-SEP-2026, entry version 127.
DE   RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D {ECO:0000303|PubMed:2017684};
DE            Short=PI-G PLD {ECO:0000303|PubMed:2017684};
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 {ECO:0000303|PubMed:2170394};
DE            Short=GPI-PLD {ECO:0000303|PubMed:2170394};
DE            Short=GPI-specific phospholipase D;
DE   Flags: Precursor;
GN   Name=GPLD1 {ECO:0000250|UniProtKB:P80108}; 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], FUNCTION, 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, FUNCTION, GLYCOSYLATION, AND
RP   CATALYTIC 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, AND SUBCELLULAR LOCATION.
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, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-834, SUBCELLULAR LOCATION,
RP   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: Hydrolyzes the inositol phosphate linkage of
CC       glycosylphosphatidylinositol (GPI)-anchored membrane proteins, thereby
CC       releasing them from the cell surface. Cleaves on the inositol side of
CC       the anchor, leaving the phosphate group attached to the membrane
CC       (PubMed:2017684, PubMed:2170394, PubMed:9042330). This release of GPI-
CC       anchored proteins can modulate diverse biological processes, including
CC       the activation of signaling pathways (By similarity).
CC       {ECO:0000250|UniProtKB:P80108, ECO:0000269|PubMed:2017684,
CC       ECO:0000269|PubMed:2170394, ECO:0000269|PubMed:9042330}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-C-terminal carboxyl phosphoethanolamide-(1-radyl-2-
CC         octadecanoyl)-GPI(deacylinositol-H7) + H2O = [protein]-C-terminal
CC         carboxyl phosphoethanolamide-glycosylinositol (deacylinositol-H7) +
CC         1-radyl-2-octadecanoyl-sn-glycero-3-phosphate + H(+);
CC         Xref=Rhea:RHEA:86263, Rhea:RHEA-COMP:20747, Rhea:RHEA-COMP:20748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:235441,
CC         ChEBI:CHEBI:235464, ChEBI:CHEBI:235465; EC=3.1.4.50;
CC         Evidence={ECO:0000269|PubMed:2017684, ECO:0000269|PubMed:2170394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86264;
CC         Evidence={ECO:0000305|PubMed:2017684};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P80108}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9042330}.
CC       Note=Associated with the High-Density Lipoproteins (HDL).
CC       {ECO:0000269|PubMed:1606959}.
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   FunCoup; P80109; 6.
DR   STRING; 9913.ENSBTAP00000006557; -.
DR   GlyCosmos; P80109; 8 sites, No reported glycans.
DR   GlyGen; P80109; 8 sites.
DR   iPTMnet; P80109; -.
DR   PaxDb; 9913-ENSBTAP00000006557; -.
DR   GeneID; 287025; -.
DR   KEGG; bta:287025; -.
DR   CTD; 2822; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   InParanoid; P80109; -.
DR   OrthoDB; 5317514at2759; -.
DR   BRENDA; 3.1.4.50; 908.
DR   PRO; PR:P80109; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004621; F:GPI anchor 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: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: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: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:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009306; P:protein secretion; 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   FunFam; 2.130.10.130:FF:000010; Glycosylphosphatidylinositol specific phospholipase D1; 1.
DR   FunFam; 2.130.10.130:FF:000011; Glycosylphosphatidylinositol specific phospholipase D1; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 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   PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
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; Integrin alpha N-terminal domain; 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: Loss of glycosylphosphatidylinositol
FT                   phospholipase D 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
//