PPA6_MOUSE
ID PPA6_MOUSE Reviewed; 418 AA.
AC Q8BP40; Q3TNE2; Q8BN33; Q9JMG5; Q9QXG5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Lysophosphatidic acid phosphatase type 6;
DE EC=3.1.3.2 {ECO:0000250|UniProtKB:Q9NPH0};
DE AltName: Full=Acid phosphatase 6, lysophosphatidic;
DE AltName: Full=Acid phosphatase-like protein 1;
DE AltName: Full=PACPL1;
DE Flags: Precursor;
GN Name=Acp6; Synonyms=Acpl1, Lpap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=12010880; DOI=10.1136/gut.50.6.790;
RA Takayama I., Daigo Y., Ward S.M., Sanders K.M., Walker R.L., Horowitz B.,
RA Yamanaka T., Fujino M.A.;
RT "Novel human and mouse genes encoding an acid phosphatase family member and
RT its downregulation in W/W(V) mouse jejunum.";
RL Gut 50:790-796(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Pituitary, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-418 (ISOFORM 1).
RX PubMed=12837850; DOI=10.1194/jlr.m300188-jlr200;
RA Luquain C., Singh A., Wang L., Natarajan V., Morris A.J.;
RT "Role of phospholipase D in agonist-stimulated lysophosphatidic acid
RT synthesis by ovarian cancer cells.";
RL J. Lipid Res. 44:1963-1975(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolyzes lysophosphatidic acid (LPA) containing a medium
CC length fatty acid chain to the corresponding monoacylglycerol. Has
CC highest activity with lysophosphatidic acid containing myristate
CC (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower
CC activity with C18:0 and C6:0 lysophosphatidic acid.
CC {ECO:0000250|UniProtKB:Q9NPH0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000250|UniProtKB:Q9NPH0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000250|UniProtKB:Q9NPH0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q9NPH0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000250|UniProtKB:Q9NPH0};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NPH0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12010880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BP40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BP40-2; Sequence=VSP_014123, VSP_014124;
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF20010.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA94308.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB030038; BAA94308.1; ALT_FRAME; mRNA.
DR EMBL; AK077729; BAC36983.1; -; mRNA.
DR EMBL; AK089736; BAC40949.1; -; mRNA.
DR EMBL; AK160271; BAE35722.1; -; mRNA.
DR EMBL; AK165356; BAE38147.1; -; mRNA.
DR EMBL; AK171757; BAE42654.1; -; mRNA.
DR EMBL; BC047276; AAH47276.1; -; mRNA.
DR EMBL; AF216223; AAF20010.1; ALT_FRAME; mRNA.
DR CCDS; CCDS17653.1; -. [Q8BP40-1]
DR RefSeq; NP_062774.2; NM_019800.4. [Q8BP40-1]
DR AlphaFoldDB; Q8BP40; -.
DR SMR; Q8BP40; -.
DR BioGRID; 211627; 1.
DR IntAct; Q8BP40; 1.
DR MINT; Q8BP40; -.
DR STRING; 10090.ENSMUSP00000088263; -.
DR iPTMnet; Q8BP40; -.
DR PhosphoSitePlus; Q8BP40; -.
DR EPD; Q8BP40; -.
DR jPOST; Q8BP40; -.
DR MaxQB; Q8BP40; -.
DR PaxDb; Q8BP40; -.
DR PeptideAtlas; Q8BP40; -.
DR PRIDE; Q8BP40; -.
DR ProteomicsDB; 289728; -. [Q8BP40-1]
DR ProteomicsDB; 289729; -. [Q8BP40-2]
DR Antibodypedia; 33980; 181 antibodies from 22 providers.
DR DNASU; 66659; -.
DR Ensembl; ENSMUST00000090759; ENSMUSP00000088263; ENSMUSG00000028093. [Q8BP40-1]
DR GeneID; 66659; -.
DR KEGG; mmu:66659; -.
DR UCSC; uc008qoq.2; mouse. [Q8BP40-1]
DR CTD; 51205; -.
DR MGI; MGI:1931010; Acp6.
DR VEuPathDB; HostDB:ENSMUSG00000028093; -.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000158408; -.
DR HOGENOM; CLU_030431_5_0_1; -.
DR InParanoid; Q8BP40; -.
DR OMA; SWPPFTS; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; Q8BP40; -.
DR TreeFam; TF318821; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 66659; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Acp6; mouse.
DR PRO; PR:Q8BP40; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BP40; protein.
DR Bgee; ENSMUSG00000028093; Expressed in skin of snout and 222 other tissues.
DR Genevisible; Q8BP40; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 2.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid metabolism; Mitochondrion;
KW Phospholipid metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..418
FT /note="Lysophosphatidic acid phosphatase type 6"
FT /id="PRO_0000023966"
FT REGION 51..161
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT VAR_SEQ 68..159
FT /note="EWNPKLLEIPPQTRFDYTVTNLAGGPKPHSHYDTEYRKTTLRGGVLAGQLTK
FT VGMQQMFALGEKLRKNYVEDIPFLSPVYNPQEVFIRSTNM -> RGGPQRGSWGHTLAS
FT PVGARAGSRPEGNNSRLALRLWPGVIIPCSSQTTGVVCKPSWLGQPLPPKLSVAWCSET
FT FERCIRMSQATVLIKCRF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014123"
FT VAR_SEQ 160..418
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014124"
FT CONFLICT 130..131
FT /note="EK -> KR (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="V -> L (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="F -> L (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="I -> L (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="G -> E (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> N (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Y -> F (in Ref. 4; AAF20010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47625 MW; C4124CE0D5CC0966 CRC64;
MRVWVPVGVL TSLAYCFHQR RVALAEQRAP NGQRPVDRNL LELKMVQVVF RHGARSPLKP
LPLEEQVEWN PKLLEIPPQT RFDYTVTNLA GGPKPHSHYD TEYRKTTLRG GVLAGQLTKV
GMQQMFALGE KLRKNYVEDI PFLSPVYNPQ EVFIRSTNMF RNLESTRCLL AGLFQHQKGS
AVIHTDEASS EVLYPNYQSC WVLKEKTRGR KKAAISQPGI SEDLEKVKTG VGINNGDDVD
FFVLLDNVAA EQVHSLLNCP ALERFAQLIE QRAVDMALYV VEQEDRESIQ MAVGPFLHIL
EGNLLKTVDP TTAPSKTRKM YLYATHDVTL LPMLLALGIF DQKWPPFAVD LTMELYQHQE
SKEWFVQLFY NGKEQVPRGC PDKLCPLDKF LNTMSVYSVS PEKYRTLCSK TRIVELGE
