Q8NCC3 (PAG15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Group XV phospholipase A2
EC=2.3.1.-

Alternative name(s):
1-O-acylceramide synthase
Short name=ACS
LCAT-like lysophospholipase
Short name=LLPL
Lysophospholipase 3
Lysosomal phospholipase A2
Short name=LPLA2

Gene names

Name:	PLA2G15
Synonyms:	LYPLA3
ORF Names:	UNQ341/PRO540

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid By similarity. May have weak lysophospholipase activity.
Subcellular location	Lysosome By similarity. Secreted Ref.1.
Tissue specificity	Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Ref.1
Post-translational modification	N-glycosylated. Ref.10
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.
Sequence caution	The sequence CAB53675.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Lysosome Secreted
Domain	Signal
Molecular function	Acyltransferase Hydrolase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid catabolic process Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Non-traceable author statement Ref.10. Source: UniProtKB
Molecular function	O-acyltransferase activity Inferred from electronic annotation. Source: InterPro lysophospholipase activity Traceable author statement. Source: ProtInc phospholipid binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 33	33	Ref.1 Ref.8
	Chain	34 – 412	379	Group XV phospholipase A2		PRO_0000017808
Sites
	Active site	198	1	Acyl-ester intermediate Potential
	Active site	360	1	Charge relay system By similarity
	Active site	392	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	273	1	N-linked (GlcNAc...) Potential
	Glycosylation	289	1	N-linked (GlcNAc...) Potential
	Glycosylation	398	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	94	1	I → T in BAD96510. Ref.4
	Sequence conflict	370	1	Q → R in BAC11233. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8NCC3 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 1FEA8A5783AF050A	FASTA	412	46,658
	10 20 30 40 50 60 MGLHLRPYRV GLLPDGLLFL LLLLMLLADP ALPAGRHPPV VLVPGDLGNQ LEAKLDKPTV 70 80 90 100 110 120 VHYLCSKKTE SYFTIWLNLE LLLPVIIDCW IDNIRLVYNK TSRATQFPDG VDVRVPGFGK 130 140 150 160 170 180 TFSLEFLDPS KSSVGSYFHT MVESLVGWGY TRGEDVRGAP YDWRRAPNEN GPYFLALREM 190 200 210 220 230 240 IEEMYQLYGG PVVLVAHSMG NMYTLYFLQR QPQAWKDKYI RAFVSLGAPW GGVAKTLRVL 250 260 270 280 290 300 ASGDNNRIPV IGPLKIREQQ RSAVSTSWLL PYNYTWSPEK VFVQTPTINY TLRDYRKFFQ 310 320 330 340 350 360 DIGFEDGWLM RQDTEGLVEA TMPPGVQLHC LYGTGVPTPD SFYYESFPDR DPKICFGDGD 370 380 390 400 410 GTVNLKSALQ CQAWQSRQEH QVLLQELPGS EHIEMLANAT TLAYLKRVLL GP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase." Taniyama Y., Shibata S., Kita S., Horikoshi K., Shirafuji H., Sumino Y., Fujino M. Biochem. Biophys. Res. Commun. 257:50-56(1999) [PubMed: 10092508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-43, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Heart and Kidney.
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 and Colon.
[8]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-48.
[9]	The European IMAGE consortium Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-412.
[10]	"Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase." Hiraoka M., Abe A., Shayman J.A. J. Biol. Chem. 277:10090-10099(2002) [PubMed: 11790796] [Abstract] Cited for: GLYCOSYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB017494 mRNA. Translation: BAA76877.1. AY358425 mRNA. Translation: AAQ88791.1. AK001705 mRNA. Translation: BAG50965.1. AK074828 mRNA. Translation: BAC11233.1. AK222790 mRNA. Translation: BAD96510.1. AL110209 mRNA. Translation: CAB53675.1. Different initiation. CH471092 Genomic DNA. Translation: EAW83217.1. BC011640 mRNA. Translation: AAH11640.2. BC062605 mRNA. Translation: AAH62605.1. AL389957 mRNA. Translation: CAB97531.1.
IPI	IPI00301459.
PIR	T14755.
RefSeq	NP_036452.1. NM_012320.3.
UniGene	Hs.632199.
3D structure databases
ProteinModelPortal	Q8NCC3.
SMR	Q8NCC3. Positions 153-234.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NCC3. 2 interactions.
MINT	MINT-1403291.
STRING	Q8NCC3.
Polymorphism databases
DMDM	44888104.
Proteomic databases
PeptideAtlas	Q8NCC3.
PRIDE	Q8NCC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219345; ENSP00000219345; ENSG00000103066.
GeneID	23659.
KEGG	hsa:23659.
UCSC	uc002evr.1. human.
Organism-specific databases
CTD	23659.
GeneCards	GC16P068279.
H-InvDB	HIX0013171.
HGNC	HGNC:17163. PLA2G15.
HPA	HPA041702. HPA041727.
MIM	609362. gene.
neXtProt	NX_Q8NCC3.
PharmGKB	PA164724567.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000004902.
HOGENOM	HBG604424.
InParanoid	Q8NCC3.
OMA	NYTLRDY.
OrthoDB	EOG4TTGHZ.
PhylomeDB	Q8NCC3.
Gene expression databases
ArrayExpress	Q8NCC3.
Bgee	Q8NCC3.
CleanEx	HS_PLA2G15.
Genevestigator	Q8NCC3.
GermOnline	ENSG00000103066. Homo sapiens.
Family and domain databases
InterPro	IPR003386. LACT/PDAT_acylTrfase. [Graphical view]
KO	K06129.
PANTHER	PTHR11440. LACT. 1 hit.
Pfam	PF02450. LACT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	46505.
SOURCE	Search...

Entry information

Entry name

PAG15_HUMAN

Accession

Primary (citable) accession number: Q8NCC3
Secondary accession number(s): B3KMF3 , Q53GZ1, Q9NPQ6, Q9UG04, Q9Y2B3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2004
Last modified:	January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.