Reviewed, UniProtKB/Swiss-Prot Q9NPH0 (PPA6_HUMAN)

Names and origin

Protein names

Recommended name:
    Lysophosphatidic acid phosphatase type 6
    EC=3.1.3.2
Alternative name(s):
    Acid phosphatase 6, lysophosphatidic
    Acid phosphatase-like protein 1
    PACPL1

Gene names

Name:	ACP6
Synonyms:	ACPL1, LPAP
ORF Names:	UNQ205/PRO231

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	428 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	Hydrolyzes lysophosphatidic acid to monoacylglycerol. Ref.1
Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate.
Subcellular location	Secreted Probable.
Tissue specificity	Highly expressed in kidney, heart, small intestine, muscle, liver, prostate, testis, ovary and weakly expressed in thymus and colon. Ref.1 Ref.2
Induction	Induced with the differentiation from myoblast to myotube. Ref.1
Sequence similarities	Belongs to the histidine acid phosphatase family.
Caution	It is uncertain whether Met-1 or Met-8 is the initiator. Was originally (Ref.1) reported to be located in the mitochondrion, but the evidence seems to be weak and contradictory with the presence of a cleaved signal sequence.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid metabolic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Ref.1 Traceable author statement. Source: ProtInc
Molecular function	acid phosphatase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ILK	Q13418	1	EBI-717738,EBI-747644

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NPH0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NPH0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     261-271: AHNLPSCPMLK → EKMGSCRFHGS
     272-428: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Ref.9
	Chain	33 – 428	396	Lysophosphatidic acid phosphatase type 6		PRO_0000023965
Sites
	Active site	59	1	Nucleophile
	Active site	335	1	Proton donor By similarity
Natural variations
	Alternative sequence	261 – 271	11	AHNLPSCPMLK → EKMGSCRFHGS in isoform 2.		VSP_014121
	Alternative sequence	272 – 428	157	Missing in isoform 2.		VSP_014122
	Natural variant	316	1	M → V: dbSNP rs6593795. Ref.6		VAR_022678
Experimental info
	Mutagenesis	59	1	H → A: Decreased activity. Ref.1
	Sequence conflict	428	1	E → D Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3CA08CFD1BB44BFA	FASTA	428	48,886
	10 20 30 40 50 60 MITGVFSMRL WTPVGVLTSL AYCLHQRRVA LAELQEADGQ CPVDRSLLKL KMVQVVFRHG 70 80 90 100 110 120 ARSPLKPLPL EEQVEWNPQL LEVPPQTQFD YTVTNLAGGP KPYSPYDSQY HETTLKGGMF 130 140 150 160 170 180 AGQLTKVGMQ QMFALGERLR KNYVEDIPFL SPTFNPQEVF IRSTNIFRNL ESTRCLLAGL 190 200 210 220 230 240 FQCQKEGPII IHTDEADSEV LYPNYQSCWS LRQRTRGRRQ TASLQPGISE DLKKVKDRMG 250 260 270 280 290 300 IDSSDKVDFF ILLDNVAAEQ AHNLPSCPML KRFARMIEQR AVDTSLYILP KEDRESLQMA 310 320 330 340 350 360 VGPFLHILES NLLKAMDSAT APDKIRKLYL YAAHDVTFIP LLMTLGIFDH KWPPFAVDLT 370 380 390 400 410 420 MELYQHLESK EWFVQLYYHG KEQVPRGCPD GLCPLDMFLN AMSVYTLSPE KYHALCSQTQ VMEVGNEE
	Isoform 2. Checksum: FF6FF0AFF8D01144	FASTA	271	30,790
	10 20 30 40 50 60 MITGVFSMRL WTPVGVLTSL AYCLHQRRVA LAELQEADGQ CPVDRSLLKL KMVQVVFRHG 70 80 90 100 110 120 ARSPLKPLPL EEQVEWNPQL LEVPPQTQFD YTVTNLAGGP KPYSPYDSQY HETTLKGGMF 130 140 150 160 170 180 AGQLTKVGMQ QMFALGERLR KNYVEDIPFL SPTFNPQEVF IRSTNIFRNL ESTRCLLAGL 190 200 210 220 230 240 FQCQKEGPII IHTDEADSEV LYPNYQSCWS LRQRTRGRRQ TASLQPGISE DLKKVKDRMG 250 260 270 IDSSDKVDFF ILLDNVAAEQ EKMGSCRFHG S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis." Hiroyama M., Takenawa T. J. Biol. Chem. 274:29172-29180(1999) [PubMed: 10506173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 52-65; 79-97; 127-140; 186-197; 371-381 AND 398-411, FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-59, INDUCTION. Tissue: Brain.
[2]	"Novel human and mouse genes encoding an acid phosphatase family member and its downregulation in W/W(V) mouse jejunum." Takayama I., Daigo Y., Ward S.M., Sanders K.M., Walker R.L., Horowitz B., Yamanaka T., Fujino M.A. Gut 50:790-796(2002) [PubMed: 12010880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"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] (ISOFORM 1).
[4]	"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] (ISOFORM 1).
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-316.
[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] (ISOFORM 1). Tissue: Cervix and Pancreas.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-428 (ISOFORM 1).
[9]	"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 33-47.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB031478 mRNA. Translation: BAA89311.1. Different initiation. AB030039 mRNA. Translation: BAA94309.2. AY358552 mRNA. Translation: AAQ88916.1. AK000657 mRNA. Translation: BAA91310.1. AB209248 mRNA. Translation: BAD92485.1. Different initiation. AL359207 Genomic DNA. Translation: CAI15199.1. BC009965 mRNA. Translation: AAH09965.1. BC034686 mRNA. Translation: AAH34686.1. CR457101 mRNA. Translation: CAG33382.1.
IPI	IPI00099838. IPI00556344.
RefSeq	NP_057445.3.
UniGene	Hs.562154
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NPH0. 3 interactions.
STRING	Q9NPH0.
Proteomic databases
PRIDE	Q9NPH0.
Genome annotation databases
Ensembl	ENST00000369238; ENSP00000358241; ENSG00000162836; Homo sapiens. [Genome view]
GeneID	51205.
KEGG	hsa:51205.
UCSC	uc001epr.2. human.
Organism-specific databases
CTD	51205.
GeneCards	GC01M145585.
H-InvDB	HIX0000989.
HGNC	HGNC:29609. ACP6.
MIM	611471. gene.
PharmGKB	PA134930830.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06267.
HOGENOM	HBG447115.
HOVERGEN	Q9NPH0.
InParanoid	Q9NPH0.
Enzyme and pathway databases
BRENDA	3.1.3.2. 247.
Gene expression databases
ArrayExpress	Q9NPH0.
Bgee	Q9NPH0.
CleanEx	HS_ACP6.
Genevestigator	Q9NPH0.
GermOnline	ENSG00000162836. Homo sapiens.
Family and domain databases
InterPro	IPR000560. Histidine_acid_Pase. [Graphical view]
Pfam	PF00328. Acid_phosphat_A. 1 hit. [Graphical view]
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	54254.
SOURCE	Search...

Entry information

Entry name

PPA6_HUMAN

Accession

Primary (citable) accession number: Q9NPH0
Secondary accession number(s): Q59G61 , Q5T490, Q6IAQ3, Q7LG81, Q9UIG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.