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Q0V8L6 (PLD2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase D2
Short name=PLD 2
EC=3.1.4.4
Alternative name(s):
Choline phosphatase 2
Phosphatidylcholine-hydrolyzing phospholipase D2
Gene names
Name:PLD2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May have a role in signal-induced cytoskeletal regulation and/or endocytosis By similarity.

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulation

Stimulated by phosphatidylinositol 4,5-bisphosphate and activated by the ADP-ribosylation factor-1 (ARF-1) By similarity.

Subunit structure

Interacts with EGFR and PIP5K1B By similarity.

Subcellular location

Membrane; Peripheral membrane protein By similarity.

Post-translational modification

Phosphorylated by FGR By similarity.

Sequence similarities

Belongs to the phospholipase D family.

Contains 1 PH domain.

Contains 2 PLD phosphodiesterase domains.

Contains 1 PX (phox homology) domain.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentMembrane
   DomainRepeat
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell communication

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: EC

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

phospholipase D activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Phospholipase D2
PRO_0000253038

Regions

Domain65 – 195131PX
Domain203 – 311109PH
Domain437 – 46428PLD phosphodiesterase 1
Domain751 – 77828PLD phosphodiesterase 2
Region441 – 788348Catalytic

Sequences

Sequence LengthMass (Da)Tools
Q0V8L6 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 8B5C417338397455

FASTA933105,766
        10         20         30         40         50         60 
MAATPQSLFP SGDDLDSSQL QMEPDEVDTL KEGEDPADRM HPFLAIYHLQ PLKLHPLVFA 

        70         80         90        100        110        120 
PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLLRHKVF 

       130        140        150        160        170        180 
MSLLPLARFA VASSPAPEGD SREIPSLPRA GPEGSSRRTA SKQKYLENYL NRLLTMSFYR 

       190        200        210        220        230        240 
NYHAMTEFLE VSQLSFIPDL GCKGLEGVIR KRSGGHRVPG LTCCGRDQVC YRWSKRWLVV 

       250        260        270        280        290        300 
KDSFLLYMCL ETGAISFVQL FDPGFKVQVG KRSTEARYGV RVDTSHRSLI LKCSSYRQAR 

       310        320        330        340        350        360 
WWAQEITELA QGPGRDFIQL HRHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF 

       370        380        390        400        410        420 
ITDWWLSPEI YLKRPAHSDD WRLDIMLKKK AEEGVHVSVL LFKEVELALA INSGYSKKAL 

       430        440        450        460        470        480 
MLLHPNIKVM RHPDQVTLWA HHEKLLVVDQ VVAFLGGLDL AYGRWDDLHY RLTDLGDSSE 

       490        500        510        520        530        540 
SAAPQPPTSC SDLPATPDLT HNQLFWLGKD YSNLITKDWV QLDRPFDDFI DRETMPRMPW 

       550        560        570        580        590        600 
RDIGVVVHGS PARDLARHFI QRWNFTKTTK TKYKIPIYPY LLPKSTSTAN QLPFTLSGGQ 

       610        620        630        640        650        660 
CATVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE 

       670        680        690        700        710        720 
IVDRILKAHK QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR 

       730        740        750        760        770        780 
LKAAMGTEWR NYISVCGLRT HGELGGHPVS ELIYIHSKML IADDRTVIIG SANINDRSLL 

       790        800        810        820        830        840 
GKRDSELAVL IEDTEMEPSL MNGVEYQAGR FALSLRKHCF SVILGAAARP HLDLRDPVCD 

       850        860        870        880        890        900 
AFFQLWQDTA ESNANIYEQI FRCLPSNATR SLRALREYVV VEPLATVSPP LARSELNQVQ 

       910        920        930 
GHLVHFPLKF LEDEYLLPSL GSKEGVMPLE VWT

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BT026202 mRNA. Translation: ABG67041.1.
BC123547 mRNA. Translation: AAI23548.1.
IPIIPI00704116.
RefSeqNP_001069295.1. NM_001075827.1.
UniGeneBt.1009.

3D structure databases

ProteinModelPortalQ0V8L6.
ModBaseSearch...

Proteomic databases

PRIDEQ0V8L6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID522159.
KEGGbta:522159.

Organism-specific databases

CTD5338.

Phylogenomic databases

eggNOGmaNOG13101.
HOVERGENHBG006650.

Family and domain databases

InterProIPR011993. PH_type.
IPR001683. Phox.
IPR001849. Pleckstrin_homology.
IPR015679. PLipase_D.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.1520.10. PX. 1 hit.
KOK01115.
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00614. PLDc. 2 hits.
PF00787. PX. 1 hit.
[Graphical view]
PIRSFPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. PX. 1 hit.
PROSITEPS50003. PH_DOMAIN. False negative.
PS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLD2_BOVIN
AccessionPrimary (citable) accession number: Q0V8L6
Secondary accession number(s): Q08DV7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: September 5, 2006
Last modified: November 16, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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