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O35405 (PLD3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Schwannoma-associated protein 9
Short name=SAM-9
Gene names
Name:Pld3
Synonyms:Sam9
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Expressed at higher level in brain than in non-nervous tissue. Probably highly expressed in neurons. Expressed in mature neurons of the forebrain and appears to be turned on at late stages of neurogenesis. Expressed during late neuronal development in the forebrain. Ref.1

Post-translational modification

Glycosylated By similarity.

Sequence similarities

Belongs to the phospholipase D family.

Contains 2 PLD phosphodiesterase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Phospholipase D3
PRO_0000280328

Regions

Topological domain1 – 3838Cytoplasmic Potential
Transmembrane39 – 5921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain60 – 488429Lumenal Potential
Domain194 – 22128PLD phosphodiesterase 1
Domain409 – 43527PLD phosphodiesterase 2

Sites

Active site1991 Potential
Active site2011 Potential
Active site2061 Potential

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict181A → G in BAE32053. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O35405 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C7F0184EB09D7573

FASTA48854,389
        10         20         30         40         50         60 
MKPKLMYQEL KVPVEEPAGE LPLNEIEAWK AAEKKARWVL LVLILAVVGF GALMTQLFLW 

        70         80         90        100        110        120 
EYGDLHLFGP NQRPAPCYDP CEAVLVESIP EGLEFPNATT SNPSTSQAWL GLLAGAHSSL 

       130        140        150        160        170        180 
DIASFYWTLT NNDTHTQEPS AQQGEEVLQQ LQALAPRGVK VRIAVSKPNG PLADLQSLLQ 

       190        200        210        220        230        240 
SGAQVRMVDM QKLTHGVLHT KFWVVDQTHF YLGSANMDWR SLTQVKELGV VMYNCSCLAR 

       250        260        270        280        290        300 
DLTKIFEAYW FLGQAGSSIP STWPRSFDTR YNQETPMEIC LNGTPALAYL ASAPPPLCPS 

       310        320        330        340        350        360 
GRTPDLKALL NVVDSARSFI YIAVMNYLPT MEFSHPRRFW PAIDDGLRRA AYERGVKVRL 

       370        380        390        400        410        420 
LISCWGHSDP SMRSFLLSLA ALHDNHTHSD IQVKLFVVPT DESQARIPYA RVNHNKYMVT 

       430        440        450        460        470        480 
ERASYIGTSN WSGSYFTETA GTSLLVTQNG HGGLRSQLEA VFLRDWESPY SHDLDTSANS 


VGNACRLL 

« Hide

References

« Hide 'large scale' references
[1]"Expression of a novel murine phospholipase D homolog coincides with late neuronal development in the forebrain."
Pedersen K.M., Finsen B., Celis J.E., Jensen N.A.
J. Biol. Chem. 273:31494-31504(1998) [PubMed: 9813063] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6 X DBA/2.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[3]"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].
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026124 mRNA. Translation: AAC73069.1.
AK153508 mRNA. Translation: BAE32053.1.
BC076586 mRNA. Translation: AAH76586.1.
IPIIPI00130624.
RefSeqNP_035246.1. NM_011116.1.
UniGeneMm.6483.

3D structure databases

ProteinModelPortalO35405.
ModBaseSearch...

Protein-protein interaction databases

STRINGO35405.

PTM databases

PhosphoSiteO35405.

Proteomic databases

PRIDEO35405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117095; ENSMUSP00000113820; ENSMUSG00000003363.
ENSMUST00000117611; ENSMUSP00000112942; ENSMUSG00000003363.
GeneID18807.
KEGGmmu:18807.
UCSCuc009fwm.1. mouse.

Organism-specific databases

CTD23646.
MGIMGI:1333782. Pld3.

Phylogenomic databases

eggNOGroNOG08898.
HOGENOMHBG444645.
HOVERGENHBG052880.
InParanoidO35405.
OMAIDIASFY.
OrthoDBEOG4M65HG.
PhylomeDBO35405.

Gene expression databases

ArrayExpressO35405.
BgeeO35405.
CleanExMM_PLD3.
GenevestigatorO35405.

Family and domain databases

InterProIPR001736. PLipase_D/transphosphatidylase.
IPR013582. PLipase_D_envelope.
[Graphical view]
PfamPF08371. PLD_envelope. 1 hit.
PF00614. PLDc. 1 hit.
[Graphical view]
SMARTSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio295120.
SOURCESearch...

Entry information

Entry namePLD3_MOUSE
AccessionPrimary (citable) accession number: O35405
Secondary accession number(s): Q3U5M5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: January 1, 1998
Last modified: October 19, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families