ID G1QNK4_NOMLE Unreviewed; 818 AA.
AC G1QNK4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D {ECO:0000256|ARBA:ARBA00015988};
DE EC=3.1.4.50 {ECO:0000256|ARBA:ARBA00012284};
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D {ECO:0000256|ARBA:ARBA00029753};
GN Name=GPLD1 {ECO:0000313|Ensembl:ENSNLEP00000002520.3};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000002520.3, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000002520.3, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000002520.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00034002};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the GPLD1 family.
CC {ECO:0000256|ARBA:ARBA00008652}.
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DR EMBL; ADFV01016251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01016257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QNK4; -.
DR Ensembl; ENSNLET00000002652.3; ENSNLEP00000002520.3; ENSNLEG00000001930.3.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00390000013522; -.
DR HOGENOM; CLU_011756_0_0_1; -.
DR TreeFam; TF335726; -.
DR Proteomes; UP000001073; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; ISS: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; 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; 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; 3.
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; 6.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..818
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014143767"
FT DOMAIN 28..200
FT /note="Phospholipase C/D"
FT /evidence="ECO:0000259|Pfam:PF00882"
FT REPEAT 347..408
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 416..477
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 479..539
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 543..603
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 613..673
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 684..750
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 818 AA; 90149 MW; 61927F0D096B086A CRC64;
MSAFRLWPGL LIVLGSLCRR GSSCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY
QAGTVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF
GITSHMVADV SWHSLGIEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR
RWYVPVKDLL GIYEKLYGRK VITENVILYP TYSTKSPFLV EQFQEYFLGG LDDMAFWSTN
IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ KNDFHRNLTT SLTESVDRNI
NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL SQKHISSPLA SYFLSFPYVR
LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHVGRVYLIY GNDLGLPPVD LDLDKEAHRI
LEGFQPSGRF GSALAVLDFN MDGVPDLAVG APSVGSEQLT YKGAVYVYFG SKQGRVSSSP
NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG GKQKGIVAAF YSGPSLSDKE
KLNVEAANWM VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP TWKNASRLGH LLHIRDEKKS
LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG TLTQVLLVGA PTHDDVSKMA
FLTVTLHQGG ATRMYTLTSD VQPLLLSTFS GDRRFSRFGG VLHLSDLDDD GLDEIIMAAP
LRIADVTSGL IGGEDGRVYV YNGKETTFGD MTGKCKSWIT PCPEEKVKRH VLQASSRFGS
SLITVRSKAK NQVVIAAGRS SLGARLSGAL HIYSLGSD
//
