GPLD1
Phosphatidylinositol-glycan-specific phospholipase D
Also known as: PHLD_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P80108
- Gene
- GPLD1
- Ensembl
- ENSG00000112293
- Chromosome
- 6
- Canonical length
- 840 aa
- Protein class
- Enzymes, Metabolic proteins, Plasma proteins, Predicted secreted proteins
- Secretome location
- Secreted to blood
OverviewNCBI Gene
Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by this gene is a GPI degrading enzyme. Glycosylphosphatidylinositol specific phospholipase D1 hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
840 residues, UniProt reviewed canonical sequence.
>P80108|GPLD1
1 MSAFRLWPGL LIMLGSLCHR GSPCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY
61 QAGIVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF
121 GITSHMAADV SWHSLGLEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR
181 RWYVPVKDLL GIYEKLYGRK VITENVIVDC SHIQFLEMYG EMLAVSKLYP TYSTKSPFLV
241 EQFQEYFLGG LDDMAFWSTN IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ
301 KNDFHRNLTT SLTESVDRNI NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL
361 SQKHVSSPLA SYFLSFPYAR LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHIGRVYLIY
421 GNDLGLPPVD LDLDKEAHRI LEGFQPSGRF GSALAVLDFN VDGVPDLAVG APSVGSEQLT
481 YKGAVYVYFG SKQGGMSSSP NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG
541 GKQKGIVAAF YSGPSLSDKE KLNVEAANWT VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP
601 TWKNASRLGH LLHIRDEKKS LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG
661 TLKQVLLVGA PTYDDVSKVA FLTVTLHQGG ATRMYALTSD AQPLLLSTFS GDRRFSRFGG
721 VLHLSDLDDD GLDEIIMAAP LRIADVTSGL IGGEDGRVYV YNGKETTLGD MTGKCKSWIT
781 PCPEEKAQYV LISPEASSRF GSSLITVRSK AKNQVVIAAG RSSLGARLSG ALHVYSLGSDLocalizationUniProt · AlphaFold · HPA
Whether an antibody against GPLD1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.21
- Highest tissue expression
- 43 nTPM
Expression across tissuesHPA
Tissue
- liver: 43 nTPM
- cerebellum: 11 nTPM
- skin: 8.1 nTPM
- retina: 5.6 nTPM
- thymus: 4.8 nTPM
- seminal vesicle: 4.5 nTPM
Single-cell type
- hepatocytes: 214 nCPM
- cone photoreceptor cells: 106 nCPM
- cardiomyocytes: 83 nCPM
- brain excitatory neurons: 71 nCPM
- brain inhibitory neurons: 71 nCPM
- other brain neurons: 69 nCPM
Immune cell
- naive B-cell: 0.2 nTPM
- naive CD8 T-cell: 0.2 nTPM
- plasmacytoid DC: 0.2 nTPM
- basophil: 0.1 nTPM
- gdT-cell: 0.1 nTPM
- MAIT T-cell: 0.1 nTPM
Brain region
- cerebellum: 23 nTPM
- cerebral cortex: 17 nTPM
- hypothalamus: 13 nTPM
- midbrain: 12 nTPM
- basal ganglia: 12 nTPM
- pons: 12 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.83
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.3
- DepMap mean gene effect
- -0.06
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell migration involved in sprouting angiogenesis
- cellular response to cholesterol
- cellular response to insulin stimulus
- cellular response to pH
- cellular response to triglyceride
- cellular response to xenobiotic stimulus
- chondrocyte differentiation
- complement receptor mediated signaling pathway
- hematopoietic stem cell migration
- hematopoietic stem cell migration to bone marrow
- insulin receptor signaling pathway
- negative regulation of cell population proliferation
- negative regulation of triglyceride catabolic process
- ossification
- phosphatidylcholine metabolic process
- positive regulation of apoptotic process
- positive regulation of endothelial cell migration
- positive regulation of glucose metabolic process
- positive regulation of high-density lipoprotein particle clearance
- positive regulation of insulin secretion involved in cellular response to glucose stimulus
- positive regulation of membrane protein ectodomain proteolysis
- positive regulation of triglyceride biosynthetic process
- protein secretion
- regulation of cellular response to insulin stimulus
- response to glucose
- transepithelial transport
- positive regulation of alkaline phosphatase activity
Molecular functions
- phospholipase D activity
- sodium channel regulator activity
- glycosylphosphatidylinositol phospholipase D activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- FG-GAP repeat
- Integrin alpha beta-propellor
- Integrin alpha, N-terminal
- FG-GAP repeat
- Glycoprotein phospholipase D
- Phospholipase C/D
- Zinc dependent phospholipase C
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads GPLD1 as an antibody target. Whether an autoantibody or antibody against GPLD1 could matter depends on whether native GPLD1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
GPLD1 is annotated as secreted, so native GPLD1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label GPLD1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...