PPA6_BOVIN
ID PPA6_BOVIN Reviewed; 429 AA.
AC A6H757;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Lysophosphatidic acid phosphatase type 6;
DE EC=3.1.3.2 {ECO:0000269|PubMed:10506173};
DE Flags: Precursor;
GN Name=ACP6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 52-65; 80-98; 128-141; 187-198; 372-382 AND 399-412,
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=10506173; DOI=10.1074/jbc.274.41.29172;
RA Hiroyama M., Takenawa T.;
RT "Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that
RT is involved in the regulation of mitochondrial lipid biosynthesis.";
RL J. Biol. Chem. 274:29172-29180(1999).
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:0000269|PubMed:10506173}.
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:0000269|PubMed:10506173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000305|PubMed:10506173};
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:0000250|UniProtKB:Q9NPH0}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:10506173}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
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DR EMBL; DAAA02007328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146121; AAI46122.1; -; mRNA.
DR RefSeq; NP_001092843.1; NM_001099373.2.
DR AlphaFoldDB; A6H757; -.
DR SMR; A6H757; -.
DR STRING; 9913.ENSBTAP00000022675; -.
DR PaxDb; A6H757; -.
DR PRIDE; A6H757; -.
DR Ensembl; ENSBTAT00000022675; ENSBTAP00000022675; ENSBTAG00000017051.
DR GeneID; 515738; -.
DR KEGG; bta:515738; -.
DR CTD; 51205; -.
DR VEuPathDB; HostDB:ENSBTAG00000017051; -.
DR VGNC; VGNC:52602; ACP6.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000158408; -.
DR HOGENOM; CLU_030431_5_0_1; -.
DR InParanoid; A6H757; -.
DR OMA; SWPPFTS; -.
DR OrthoDB; 1221585at2759; -.
DR TreeFam; TF318821; -.
DR BRENDA; 3.1.3.106; 908.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000017051; Expressed in cortex of kidney and 106 other tissues.
DR ExpressionAtlas; A6H757; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
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; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid metabolism; Mitochondrion;
KW Phospholipid metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 33..429
FT /note="Lysophosphatidic acid phosphatase type 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000424239"
FT REGION 58..169
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 48945 MW; BB1C199EE3661CA0 CRC64;
MISRVFKLRM WAPVGVLTSL TYCLHQRRVA LAEPGGADQQ NPVDRNLLEL KMVQVVFRHG
ARSPLKPLPQ EDQQVEWKSQ LLEVPPQTQL EYTVTNLAGG PKPHSPFDSQ YHETTLKGGM
FAGQLTKVGM EQMFALGERL RKNYVEDIPF LSPTFNPLEV FIRSTNIYRN LESTRCLLAG
LFQRQKEGPI VIHTDEASSE VLYPNYQYCW NLQKRTRGRR QAASLQPGIS EDLKKVKEGM
GIASSDEVDF LVLLDNMAAE QVHSLPSCPT LKRFAWMIEQ RAVDTALYIL QWEDREGLQM
AVGPFLHILE SNLLKVVDPA TPPSKTRKLY LYAAHDVTLM PLLMTLGIFD HKWPPFAVDL
TMELYQHRES KEWFVQLYYR GKEQVPKGCP DGLCPLDKFL NTISVYTLSP EKYHMLCSEA
QMMGLGNGE
