PHLD_RAT
ID PHLD_RAT Reviewed; 843 AA.
AC Q8R2H5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
DE Short=PI-G PLD;
DE EC=3.1.4.50;
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11855934; DOI=10.1006/mgme.2001.3287;
RA Schofield J.N., Stephens J.W., Hurel S.J., Bell K.M., deSouza J.B.,
RA Rademacher T.W.;
RT "Insulin reduces serum glycosylphosphatidylinositol phospholipase D levels
RT in human type I diabetic patients and streptozotocin diabetic rats.";
RL Mol. Genet. Metab. 75:154-161(2002).
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 -!- 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 -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Associated with the High-Density
CC Lipoproteins (HDL). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
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DR EMBL; AJ308109; CAC87069.1; -; mRNA.
DR RefSeq; NP_001093982.1; NM_001100512.1.
DR AlphaFoldDB; Q8R2H5; -.
DR STRING; 10116.ENSRNOP00000024196; -.
DR GlyGen; Q8R2H5; 10 sites.
DR PaxDb; Q8R2H5; -.
DR PRIDE; Q8R2H5; -.
DR GeneID; 291132; -.
DR KEGG; rno:291132; -.
DR UCSC; RGD:631371; rat.
DR CTD; 2822; -.
DR RGD; 631371; Gpld1.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; Q8R2H5; -.
DR PhylomeDB; Q8R2H5; -.
DR BRENDA; 3.1.4.50; 5301.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q8R2H5; -.
DR Proteomes; UP000002494; 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; ISO:RGD.
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:0004630; F:phospholipase D activity; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071282; P:cellular response to iron(II) ion; IDA: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; 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:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; 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: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; -; 3.
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; 3.
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 2: Evidence at transcript level;
KW Glycoprotein; HDL; Hydrolase; Lipid metabolism; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..843
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /id="PRO_0000278285"
FT REPEAT 368..429
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 435..498
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 500..560
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 564..625
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 635..695
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 707..773
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 791..843
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 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 843 AA; 93782 MW; 99964E1C35AB84D6 CRC64;
MSVGRLWSGL LLLLLFFCSR SSSCGLSTHV EIGHRALQFL QLQDGRINYK ELLLEHQDAY
QAGTVFPDAF YPSICKQGKF HEVSESTHWT PFLNASIHYI RENYPLPWEK DTEKLVAFLF
GVTSHMVADV SWHSLGIEQG FLRTMGAIDF YDSYSEAHSA GDFGGDVLSQ FEFNFNYLSR
RWYVPIQDLL RIYDNLYGRK VITKNVIVDC TYLQFLEMHG EMLAVSKLYS TYSTKSPFLV
EQFQDYFLGG LDDMAFWSTN IYRLTSFMLE NGTSDCNLPE NPLFISCDGR KNHTLSSSKV
QKNDFHRNLT MFISKDIRKN LNYTERGVFY STGSWAPESV TFMYQTLERN LRMMFTGNSQ
TALKHVSSPS ASYTLSVPYA RLGWVMASAD LNQDGHGDLV VGAPGYSHPG RFQIGRVYII
YGNDLGLPPI DLDLDKEAHG VLEGFQPSGR FGSALAVLDF NKDGLPDLAV GAPSVGSGQL
TYNGSVYVYY GSQQGRLSSS PNITISCKDT YCNLGWALLA ADADGDGQHD LVISSPFAPG
GGKQRGIVAA FYSHPRRNDK ESLTLDEADW KVNGEEDFSW FGYSLHGVTV ANRSLLLIGS
PTWKNISRMA RSSHQKNQEK KSLGRVYGYF PPNRQREITI SGDKAMGKLG TSLSSGYVRV
NGTLTQVLLV GAPTHDDVSK MAFLTMTLHH GGATRMYELA PEKTQPALFS TFSGDRRFSR
FGSVLHLTDL DDDGLDEIIM AAPLRITDVT SGLLGEEDGR VYIYNGMHTT LGDVTGKCKS
WMTPCPEEKA QYVLISPEAS SRFGSSLVSV RSKERNQVVV AAGRSSWGAR LSGALHVYSF
SSD
