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Reviewed, UniProtKB/Swiss-Prot Q8IV08 (PLD3_HUMAN)

Last modified November 3, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Phospholipase D3
      Short name=PLD 3
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 3
    Phosphatidylcholine-hydrolyzing phospholipase D3
    HindIII K4L homolog
    Hu-K4
Gene names
Name: PLD3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein. Ref.3

Tissue specificity

Widely expressed. Expressec at higher level in brain. Expresse at low level in corpus callosum, suggsting that it is highly expressed in neurons. Ref.3

Post-translational modification

Glycosylated. Ref.3 Ref.5

Sequence similarities

Belongs to the phospholipase D family.

Contains 2 PLD phosphodiesterase domains.

Sequence caution

The sequence AAB16799.1 differs from that shown. Reason: Frameshift at position 52.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Signal-anchor
Transmembrane
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: EC

phospholipase D activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Phospholipase D3
PRO_0000280326

Regions

Topological domain1 – 3838Cytoplasmic Potential
Transmembrane39 – 5921Signal-anchor for type II membrane protein Potential
Topological domain60 – 490431Lumenal Potential
Domain196 – 22328PLD phosphodiesterase 1
Domain411 – 43727PLD phosphodiesterase 2

Sites

Active site2011 Potential
Active site2031 Potential
Active site2081 Potential

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Ref.5
Glycosylation1321N-linked (GlcNAc...) Ref.5

Experimental info

Sequence conflict4731S → I in AAB16799. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8IV08-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 444EC4D02F5610F1

FASTA49054,705
        10         20         30         40         50         60 
MKPKLMYQEL KVPAEEPANE LPMNEIEAWK AAEKKARWVL LVLILAVVGF GALMTQLFLW 

        70         80         90        100        110        120 
EYGDLHLFGP NQRPAPCYDP CEAVLVESIP EGLDFPNAST GNPSTSQAWL GLLAGAHSSL 

       130        140        150        160        170        180 
DIASFYWTLT NNDTHTQEPS AQQGEEVLRQ LQTLAPKGVN VRIAVSKPSG PQPQADLQAL 

       190        200        210        220        230        240 
LQSGAQVRMV DMQKLTHGVL HTKFWVVDQT HFYLGSANMD WRSLTQVKEL GVVMYNCSCL 

       250        260        270        280        290        300 
ARDLTKIFEA YWFLGQAGSS IPSTWPRFYD TRYNQETPME ICLNGTPALA YLASAPPPLC 

       310        320        330        340        350        360 
PSGRTPDLKA LLNVVDNARS FIYVAVMNYL PTLEFSHPHR FWPAIDDGLR RATYERGVKV 

       370        380        390        400        410        420 
RLLISCWGHS EPSMRAFLLS LAALRDNHTH SDIQVKLFVV PADEAQARIP YARVNHNKYM 

       430        440        450        460        470        480 
VTERATYIGT SNWSGNYFTE TAGTSLLVTQ NGRGGLRSQL EAIFLRDWDS PYSHDLDTSA 

       490 
DSVGNACRLL 

« Hide

References

« Hide 'large scale' references
[1]"A human homolog of the vaccinia virus HindIII K4L gene is a member of the phospholipase D superfamily."
Cao J.X., Koop B.F., Upton C.
Virus Res. 48:11-18(1997) [PubMed: 9140189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Colon and Lung.
[3]"Hu-K4 is a ubiquitously expressed type 2 transmembrane protein associated with the endoplasmic reticulum."
Munck A., Boehm C., Seibel N.M., Hashemol Hosseini Z., Hampe W.
FEBS J. 272:1718-1726(2005) [PubMed: 15794758] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, GLYCOSYLATION.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97 AND ASN-132, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

U60644 mRNA. Translation: AAB16799.1. Frameshift.
BC000553 mRNA. Translation: AAH00553.2.
BC036327 mRNA. Translation: AAH36327.1.
BC096820 mRNA. Translation: AAH96820.1.
IPIIPI00328243.
RefSeqNP_001026866.1.
NP_036400.2.
UniGeneHs.257008

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8IV08.

Proteomic databases

PRIDEQ8IV08.

Genome annotation databases

EnsemblENST00000356508; ENSP00000348901; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000359274; ENSP00000352220; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000392032; ENSP00000375886; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000409281; ENSP00000387022; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000409419; ENSP00000386293; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000409587; ENSP00000387050; ENSG00000105223; Homo sapiens. [Genome view]
ENST00000409735; ENSP00000386938; ENSG00000105223; Homo sapiens. [Genome view]
GeneID23646.
KEGGhsa:23646.
UCSCuc002onj.2. human.

Organism-specific databases

CTD23646.
GeneCardsGC19P045557.
HGNCHGNC:17158. PLD3.
HPACAB020812.
HPA012800.
PharmGKBPA134887482.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8IV08.
OMAVFERDWN.

Enzyme and pathway databases

BRENDA3.1.4.4. 247.

Gene expression databases

ArrayExpressQ8IV08.
BgeeQ8IV08.
CleanExHS_PLD3.
GenevestigatorQ8IV08.

Family and domain databases

InterProIPR013582. PLD_envelope.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamPF08371. PLD_envelope. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
SMARTSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio46461.

Entry information

Entry namePLD3_HUMAN
AccessionPrimary (citable) accession number: Q8IV08
Secondary accession number(s): Q92853, Q9BW87
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

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