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Reviewed, UniProtKB/Swiss-Prot Q9NPH0 (PPA6_HUMAN)

Last modified January 19, 2010. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processlipid metabolic process Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionacid 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

ILKQ134181EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.9
Chain33 – 428396Lysophosphatidic acid phosphatase type 6
PRO_0000023965

Sites

Active site591Nucleophile
Active site3351Proton donor By similarity

Natural variations

Alternative sequence261 – 27111AHNLPSCPMLK → EKMGSCRFHGS in isoform 2.
VSP_014121
Alternative sequence272 – 428157Missing in isoform 2.
VSP_014122
Natural variant3161M → V: dbSNP rs6593795. Ref.6
VAR_022678

Experimental info

Mutagenesis591H → A: Decreased activity. Ref.1
Sequence conflict4281E → D Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3CA08CFD1BB44BFA

FASTA42848,886
        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 

« Hide

Isoform 2.

Checksum: FF6FF0AFF8D01144
Show »

FASTA27130,790

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
IPIIPI00099838.
IPI00556344.
RefSeqNP_057445.3.
UniGeneHs.562154

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NPH0. 3 interactions.
STRINGQ9NPH0.

Proteomic databases

PRIDEQ9NPH0.

Genome annotation databases

EnsemblENST00000369238; ENSP00000358241; ENSG00000162836; Homo sapiens. [Genome view]
GeneID51205.
KEGGhsa:51205.
UCSCuc001epr.2. human.

Organism-specific databases

CTD51205.
GeneCardsGC01M145585.
H-InvDBHIX0000989.
HGNCHGNC:29609. ACP6.
MIM611471. gene.
PharmGKBPA134930830.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06267.
HOGENOMHBG447115.
HOVERGENQ9NPH0.
InParanoidQ9NPH0.

Enzyme and pathway databases

BRENDA3.1.3.2. 247.

Gene expression databases

ArrayExpressQ9NPH0.
BgeeQ9NPH0.
CleanExHS_ACP6.
GenevestigatorQ9NPH0.
GermOnlineENSG00000162836. Homo sapiens.

Family and domain databases

InterProIPR000560. Histidine_acid_Pase.
[Graphical view]
PfamPF00328. Acid_phosphat_A. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio54254.
SOURCESearch...

Entry information

Entry namePPA6_HUMAN
AccessionPrimary (citable) accession number: Q9NPH0
Secondary accession number(s): Q59G61 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents