Reviewed, UniProtKB/Swiss-Prot O17405 (PLDL_CAEEL)

Names and origin

Protein names

Recommended name:
    Probable phospholipase D F09G2.8
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase F09G2.8
    Phosphatidylcholine-hydrolyzing phospholipase D F09G2.8

Gene names

ORF Names:

F09G2.8

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Sequence similarities	Belongs to the phospholipase D family. Contains 2 PLD phosphodiesterase domains.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Membrane
Domain	Repeat Signal-anchor Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phospholipase D activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 516	516	Probable phospholipase D F09G2.8		PRO_0000250583
Regions
	Topological domain	1 – 85	85	Cytoplasmic Potential
	Transmembrane	86 – 106	21	Signal-anchor for type II membrane protein Potential
	Topological domain	107 – 516	410	Extracellular Potential
	Domain	234 – 261	28	PLD phosphodiesterase 1
	Domain	454 – 480	27	PLD phosphodiesterase 2
Sites
	Active site	239	1	Potential
	Active site	241	1	Potential
	Active site	246	1	Potential
Amino acid modifications
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Ref.2 Ref.3
	Glycosylation	312	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	430	1	N-linked (GlcNAc...) Potential
	Glycosylation	475	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O17405-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 62747B31104FAE57	FASTA	516	58,573
	10 20 30 40 50 60 MVSGRTYLTP HEKEENGERK NTRMETHDGR ADMTNFEMDL FDTRIEVPTS KNSGGDGMHS 70 80 90 100 110 120 PYYDEESSKK RCCKCGNSRN RIIKPACVPI SIVSLFIIAL VFLPLFNEED LASPIKLTTG 130 140 150 160 170 180 CSVDCKTFLV ESIPIGLPFK TNNHTAEAWI NIIDNSKQYL DISVMYWNLN TSDYKSSVYG 190 200 210 220 230 240 RRVYEAIIRA GKRGVKIRIA QDGASNLSDN KESAYLVQEG LAEVREINVT RLIGSGIIHT 250 260 270 280 290 300 KFILSDIATL YIGSANMDWK SLSEVKEVGV VFQECPCVAS DLYKIFAAYW KLGENDSVIP 310 320 330 340 350 360 EKWPISYRTP FNFSSMAKLT MDGEPAEYFI SSSPGPFNPK GREHDLAAIQ KIMKDARKSV 370 380 390 400 410 420 CISVMDYIPS TLYMKKSNRF WPEIDDSIRD AAYRGVNVRM LISHWDHSRK EMIPFLKSLQ 430 440 450 460 470 480 TITDGLPRYN RTEHGQVQVR IFTVPPNGKE KIPFTRVNHA KYMVTEDIAY IGTSNWSGDY 490 500 510 FISTAGVAMV VRQPSATKRL QNVFDRDWNS EYSKDL

References

[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295, MASS SPECTROMETRY.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295 AND ASN-312, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF026215 Genomic DNA. Translation: AAB71325.1.
PIR	T32489.
RefSeq	NP_504824.1.
UniGene	Cel.8908
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O17405.
Genome annotation databases
Ensembl	F09G2.8.1; F09G2.8.1; F09G2.8; Caenorhabditis elegans. [Genome view] F09G2.8.2; F09G2.8.2; F09G2.8; Caenorhabditis elegans. [Genome view] F09G2.8b; F09G2.8b; F09G2.8; Caenorhabditis elegans. [Genome view]
GeneID	179105.
UCSC	F09G2.8b. c. elegans.
Organism-specific databases
CTD	179105.
WormBase	WBGene00017316. F09G2.8.
WormPep	F09G2.8. CE09303. [WorfDB]
Phylogenomic databases
OMA	VFERDWN.
Enzyme and pathway databases
BRENDA	3.1.4.4. 672.
Gene expression databases
ArrayExpress	O17405.
Family and domain databases
InterPro	IPR013582. PLD_envelope. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
Pfam	PF08371. PLD_envelope. 1 hit. PF00614. PLDc. 2 hits. [Graphical view]
SMART	SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	903946.

Entry information

Entry name

PLDL_CAEEL

Accession

Primary (citable) accession number: O17405

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project