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P80108 (PHLD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol-glycan-specific phospholipase D

Short name=PI-G PLD
EC=3.1.4.50
Alternative name(s):
Glycoprotein phospholipase D
Glycosyl-phosphatidylinositol-specific phospholipase D
Short name=GPI-PLD
Short name=GPI-specific phospholipase D
Gene names
Name:GPLD1
Synonyms:PIGPLD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length840 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.

Catalytic activity

6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + phosphatidate.

Subunit structure

Monomer Potential.

Subcellular location

Secreted.

Sequence similarities

Belongs to the GPLD1 family.

Contains 7 FG-GAP repeats.

Sequence caution

The sequence AAA36444.1 differs from that shown. Reason: This sequence has numerous of conflicts with the human genome.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGPI anchor release

Inferred from direct assay PubMed 15907827PubMed 19135435PubMed 2760042. Source: UniProtKB

cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 17720976. Source: UniProtKB

cellular response to calcium ion

Inferred from direct assay PubMed 2760042. Source: UniProtKB

cellular response to cholesterol

Inferred from mutant phenotype PubMed 17761367. Source: UniProtKB

cellular response to drug

Inferred from direct assay PubMed 17761367. Source: UniProtKB

cellular response to insulin stimulus

Inferred from direct assay PubMed 15907827. Source: UniProtKB

cellular response to pH

Inferred from direct assay PubMed 17761367. Source: UniProtKB

cellular response to triglyceride

Inferred from mutant phenotype PubMed 17761367. Source: UniProtKB

chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

complement receptor mediated signaling pathway

Inferred from direct assay PubMed 15907827PubMed 19135435. Source: UniProtKB

hematopoietic stem cell migration

Traceable author statement PubMed 17368745. Source: UniProtKB

hematopoietic stem cell migration to bone marrow

Traceable author statement PubMed 17368745. Source: UniProtKB

insulin receptor signaling pathway

Inferred from direct assay PubMed 18328347. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 19135435. Source: UniProtKB

negative regulation of triglyceride catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylcholine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of alkaline phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 19135435. Source: UniProtKB

positive regulation of cytolysis

Inferred from direct assay PubMed 15907827PubMed 19135435. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from mutant phenotype PubMed 17720976. Source: UniProtKB

positive regulation of glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of high-density lipoprotein particle clearance

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 17720976. Source: UniProtKB

positive regulation of secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular response to insulin stimulus

Inferred from direct assay PubMed 18328347. Source: UniProtKB

response to glucose

Inferred from direct assay PubMed 15907827. Source: UniProtKB

transepithelial transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19135435. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 15907827PubMed 17720976PubMed 17761367PubMed 1833386PubMed 2760042. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 15907827. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 1833386. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglycosylphosphatidylinositol phospholipase D activity

Inferred from direct assay PubMed 15907827PubMed 17720976PubMed 1833386PubMed 19135435PubMed 2760042. Source: UniProtKB

phospholipase D activity

Inferred from direct assay PubMed 2760042. Source: UniProtKB

sodium channel regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P80108-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P80108-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-176: GDVLSQFEFNFN → TVYLHLLNFLVV
     177-840: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 840817Phosphatidylinositol-glycan-specific phospholipase D
PRO_0000022047

Regions

Repeat367 – 42862FG-GAP 1
Repeat436 – 49762FG-GAP 2
Repeat499 – 55961FG-GAP 3
Repeat563 – 62361FG-GAP 4
Repeat633 – 69361FG-GAP 5
Repeat704 – 77067FG-GAP 6
Repeat788 – 84053FG-GAP 7

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Ref.7
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation6041N-linked (GlcNAc...) Potential
Glycosylation6591N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence165 – 17612GDVLS…EFNFN → TVYLHLLNFLVV in isoform 2.
VSP_023261
Alternative sequence177 – 840664Missing in isoform 2.
VSP_023262
Natural variant171L → V. Ref.5
Corresponds to variant rs2235501 [ dbSNP | Ensembl ].
VAR_030743
Natural variant301V → I. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1126617 [ dbSNP | Ensembl ].
VAR_030744
Natural variant2751D → E.
Corresponds to variant rs17300770 [ dbSNP | Ensembl ].
VAR_030745
Natural variant3501I → V. Ref.1
Corresponds to variant rs1062496 [ dbSNP | Ensembl ].
VAR_051278
Natural variant3961G → S.
Corresponds to variant rs6924628 [ dbSNP | Ensembl ].
VAR_030746
Natural variant4611V → M. Ref.1
Corresponds to variant rs1062505 [ dbSNP | Ensembl ].
VAR_030747
Natural variant6941M → V. Ref.2
Corresponds to variant rs1042303 [ dbSNP | Ensembl ].
VAR_030748
Natural variant6981T → I. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs1772256 [ dbSNP | Ensembl ].
VAR_030749

Experimental info

Sequence conflict531 – 5344VIGS → MLGT AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 20, 2007. Version 3.
Checksum: 11369BAFEC3D6D38

FASTA84092,336
        10         20         30         40         50         60 
MSAFRLWPGL LIMLGSLCHR GSPCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY 

        70         80         90        100        110        120 
QAGIVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF 

       130        140        150        160        170        180 
GITSHMAADV SWHSLGLEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR 

       190        200        210        220        230        240 
RWYVPVKDLL GIYEKLYGRK VITENVIVDC SHIQFLEMYG EMLAVSKLYP TYSTKSPFLV 

       250        260        270        280        290        300 
EQFQEYFLGG LDDMAFWSTN IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ 

       310        320        330        340        350        360 
KNDFHRNLTT SLTESVDRNI NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL 

       370        380        390        400        410        420 
SQKHVSSPLA SYFLSFPYAR LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHIGRVYLIY 

       430        440        450        460        470        480 
GNDLGLPPVD LDLDKEAHRI LEGFQPSGRF GSALAVLDFN VDGVPDLAVG APSVGSEQLT 

       490        500        510        520        530        540 
YKGAVYVYFG SKQGGMSSSP NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG 

       550        560        570        580        590        600 
GKQKGIVAAF YSGPSLSDKE KLNVEAANWT VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP 

       610        620        630        640        650        660 
TWKNASRLGH LLHIRDEKKS LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG 

       670        680        690        700        710        720 
TLKQVLLVGA PTYDDVSKVA FLTVTLHQGG ATRMYALTSD AQPLLLSTFS GDRRFSRFGG 

       730        740        750        760        770        780 
VLHLSDLDDD GLDEIIMAAP LRIADVTSGL IGGEDGRVYV YNGKETTLGD MTGKCKSWIT 

       790        800        810        820        830        840 
PCPEEKAQYV LISPEASSRF GSSLITVRSK AKNQVVIAAG RSSLGARLSG ALHVYSLGSD 

« Hide

Isoform 2 [UniParc].

Checksum: B71070D7DD58234B
Show »

FASTA17619,865

References

« Hide 'large scale' references
[1]"Isolation and expression of two human glycosylphosphatidylinositol phospholipase D (GPI-PLD) cDNAs."
Tsang T.C., Fung W.-J.C., Levine J., Metz C.N., Davitz M.A., Burns D.K., Huang K.-S., Kochan J.P.
FASEB J. 6:A1922-A1922(1992)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-30; VAL-350; MET-461 AND ILE-698.
Tissue: Liver and Pancreas.
[2]"Structure and expression of the human glycosylphosphatidylinositol phospholipase D1 (GPLD1) gene."
Schofield J.N., Rademacher T.W.
Biochim. Biophys. Acta 1494:189-194(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 384-840, VARIANTS ILE-30; VAL-694 AND ILE-698.
Tissue: Liver.
[3]"Preliminary study of the gene structure of human glycosylphosphatidylinositol specific phospholipase D."
Tang J.H., Gu S.L., Zhang X.J.
Hunan Yi Ke Da Xue Xue Bao 26:96-97(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-698.
Tissue: Bone marrow.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 266-840 (ISOFORM 1), VARIANTS VAL-17; ILE-30 AND ILE-698.
Tissue: Eye and Liver.
[6]"Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high-density lipoproteins."
Hoener M.C., Brodbeck U.
Eur. J. Biochem. 206:747-757(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Serum.
[7]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94.
Tissue: Plasma.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11701 mRNA. Translation: AAA36444.1. Sequence problems.
L11702 mRNA. Translation: AAA36445.1.
AJ308108 mRNA. Translation: CAC87068.1.
AJ400872 expand/collapse EMBL AC list , AJ400873, AJ400874, AJ400875, AJ400876 Genomic DNA. Translation: CAC14844.1.
AY007546 mRNA. Translation: AAG16627.2.
AL359713, AL031230 Genomic DNA. Translation: CAI17103.1.
AL031230, AL359713 Genomic DNA. Translation: CAI22602.1.
AL031230 Genomic DNA. Translation: CAD92520.1.
BC007614 mRNA. Translation: AAH07614.1.
BC020748 mRNA. Translation: AAH20748.1.
BC093645 mRNA. Translation: AAH93645.1.
BC112001 mRNA. Translation: AAI12002.1.
CCDSCCDS4553.1. [P80108-1]
RefSeqNP_001494.2. NM_001503.3. [P80108-1]
UniGeneHs.533291.

3D structure databases

ProteinModelPortalP80108.
SMRP80108. Positions 369-768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109083. 2 interactions.

PTM databases

PhosphoSiteP80108.

Polymorphism databases

DMDM126302583.

Proteomic databases

PaxDbP80108.
PeptideAtlasP80108.
PRIDEP80108.

Protocols and materials databases

DNASU2822.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230036; ENSP00000230036; ENSG00000112293. [P80108-1]
GeneID2822.
KEGGhsa:2822.
UCSCuc003ned.2. human. [P80108-1]
uc003nee.4. human. [P80108-2]

Organism-specific databases

CTD2822.
GeneCardsGC06M024377.
H-InvDBHIX0032817.
HGNCHGNC:4459. GPLD1.
HPACAB008625.
HPA012500.
MIM602515. gene.
neXtProtNX_P80108.
PharmGKBPA28842.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146018.
HOVERGENHBG008185.
InParanoidP80108.
KOK01127.
OMASYSEAHS.
OrthoDBEOG7MD4PC.
PhylomeDBP80108.
TreeFamTF335726.

Enzyme and pathway databases

BRENDA3.1.4.50. 2681.
SignaLinkP80108.

Gene expression databases

BgeeP80108.
GenevestigatorP80108.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR001028. Gprt_PLipase_D.
IPR013519. Int_alpha_beta-p.
IPR029002. PLPC/GPLD1.
[Graphical view]
PfamPF01839. FG-GAP. 3 hits.
PF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSPR00718. PHPHLIPASED.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGPLD1.
GenomeRNAi2822.
NextBio11121.
PROP80108.
SOURCESearch...

Entry information

Entry namePHLD_HUMAN
AccessionPrimary (citable) accession number: P80108
Secondary accession number(s): Q15127 expand/collapse secondary AC list , Q15128, Q2M2F2, Q5T3Y0, Q7Z6T8, Q8TCV0, Q8WW82, Q96ID6, Q9H167, Q9H4M1, Q9UJC9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM