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Reviewed, UniProtKB/Swiss-Prot P80109 (PHLD_BOVIN)

Last modified September 1, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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-specific phospholipase D
      Short name=GPI-PLD
Gene names
Name: GPLD1
Synonyms: PIGPLD
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length839 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. Ref.4

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. Note: Associated with the High-Density Lipoproteins (HDL). Ref.4

Post-translational modification

Glycosylated. Ref.4 Ref.2

Sequence similarities

Belongs to the GPLD1 family.

Contains 4 FG-GAP repeats.

Ontologies

Keywords
   Cellular componentHDL
Secreted
   DomainRepeat
Signal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componenthigh-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglycosylphosphatidylinositol phospholipase D activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.3
Chain24 – 839816Phosphatidylinositol-glycan-specific phospholipase D
PRO_0000022053

Regions

Repeat380 – 41839FG-GAP 1
Repeat449 – 48739FG-GAP 2
Repeat512 – 54938FG-GAP 3
Repeat717 – 74933FG-GAP 4

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis8341Y → A: Severe loss of enzymatic activity. Ref.4
Sequence conflict1811H → F AA sequence Ref.2
Sequence conflict1841V → L AA sequence Ref.2
Sequence conflict2351K → R AA sequence Ref.2
Sequence conflict6341W → P AA sequence Ref.2
Sequence conflict7771W → N AA sequence Ref.2
Sequence conflict7801P → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P80109-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: F9BFF8A00226BF40

FASTA83992,602
        10         20         30         40         50         60 
MSAFRFWSGL LMLLGFLCPR SSPCGISTHI EIGHRALEFL HLQDGSINYK ELLLRHQDAY 

        70         80         90        100        110        120 
QAGSVFPDSF YPSICERGQF HDVSESTHWT PFLNASVHYI RKNYPLPWDE DTEKLVAFLF 

       130        140        150        160        170        180 
GITSHMVADV NWHSLGIEQG FLRTMAAIDF HNSYPEAHPA GDFGGDVLSQ FEFKFNYLSR 

       190        200        210        220        230        240 
HWYVPAEDLL GIYRELYGRI VITKKAIVDC SYLQFLEMYA EMLAISKLYP TYSVKSPFLV 

       250        260        270        280        290        300 
EQFQEYFLGG LEDMAFWSTN IYHLTSYMLK NGTSNCNLPE NPLFITCGGQ QNNTHGSKVQ 

       310        320        330        340        350        360 
KNGFHKNVTA ALTKNIGKHI NYTKRGVFFS VDSWTMDSLS FMYKSLERSI REMFIGSSQP 

       370        380        390        400        410        420 
LTHVSSPAAS YYLSFPYTRL GWAMTSADLN QDGYGDLVVG APGYSHPGRI HVGRVYLIYG 

       430        440        450        460        470        480 
NDLGLPRIDL DLDKEAHGIL EGFQPSGRFG SAVAVLDFNV DGVPDLAVGA PSVGSEKLTY 

       490        500        510        520        530        540 
TGAVYVYFGS KQGQLSSSPN VTISCQDTYC NLGWTLLAAD VNGDSEPDLV IGSPFAPGGG 

       550        560        570        580        590        600 
KQKGIVAAFY SGSSYSSREK LNVEAANWMV KGEEDFAWLG YSLHGVNVNN RTLLLAGSPT 

       610        620        630        640        650        660 
WKDTSSQGHL FRTRDEKQSP GRVYGYFPPI CQSWFTISGD KAMGKLGTSL SSGHVMVNGT 

       670        680        690        700        710        720 
RTQVLLVGAP TQDVVSKVSF LTMTLHQGGS TRMYELTPDS QPSLLSTFSG NRRFSRFGGV 

       730        740        750        760        770        780 
LHLSDLDNDG LDEIIVAAPL RITDATAGLM GEEDGRVYVF NGKQITVGDV TGKCKSWVTP 

       790        800        810        820        830 
CPEEKAQYVL ISPEAGSRFG SSVITVRSKE KNQVIIAAGR SSLGARLSGV LHIYRLGQD 

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References

[1]"Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D."
Scallon B.J., Fung W.-J.C., Tsang T.C., Li S., Kado-Fong H., Huang K.-S., Kochan J.P.
Science 252:446-448(1991) [PubMed: 2017684] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification and characterization of glycosyl-phosphatidylinositol-specific phospholipase D."
Huang K.S., Li S., Fung W.J., Hulmes J.D., Reik L., Pan Y.C., Low M.G.
J. Biol. Chem. 265:17738-17745(1990) [PubMed: 2170394] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-50; 56-77; 126-138; 181-185; 235-261; 380-408; 449-477; 623-636; 678-692 AND 776-807, GLYCOSYLATION.
Tissue: Serum.
[3]"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: 1606959] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-50; 126-138; 145-164; 353-367; 569-579; 693-708 AND 750-773.
Tissue: Serum.
[4]"The C-terminus of glycosylphosphatidylinositol-specific phospholipase D is essential for biological activity."
Stadelmann B., Buetikofer P., Koenig A., Brodbeck U.
Biochim. Biophys. Acta 1355:107-113(1997) [PubMed: 9042330] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-834, SUBCELLULAR LOCATION, GLYCOSYLATION.

Cross-references

Sequence databases

M60804 mRNA. Translation: AAA30721.1.
IPIIPI00701859.
PIRA56337.
RefSeqNP_777241.1.
UniGeneBt.452

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP80109.

Genome annotation databases

EnsemblENSBTAT00000006557; ENSBTAP00000006557; ENSBTAG00000004982; Bos taurus. [Genome view]
GeneID287025.
KEGGbta:287025.

Organism-specific databases

CTD287025.

Phylogenomic databases

HOVERGENP80109.

Enzyme and pathway databases

BRENDA3.1.4.50. 251.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR001028. Gprt_PlipaseD.
IPR013519. Int_alpha_beta-p.
[Graphical view]
PANTHERPTHR23221:SF2. Gprt_PlipaseD. 1 hit.
PfamPF01839. FG-GAP. 4 hits.
[Graphical view]
PRINTSPR00718. PHPHLIPASED.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHLD_BOVIN
AccessionPrimary (citable) accession number: P80109
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 1, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents