ID   PPA6_PONAB              Reviewed;         428 AA.
AC   Q5R8C0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   22-FEB-2023, entry version 67.
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   Flags: Precursor;
GN   Name=ACP6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9NPH0}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; CR859833; CAH91990.1; -; mRNA.
DR   RefSeq; NP_001127492.1; NM_001134020.1.
DR   AlphaFoldDB; Q5R8C0; -.
DR   SMR; Q5R8C0; -.
DR   STRING; 9601.ENSPPYP00000001102; -.
DR   GeneID; 100174567; -.
DR   KEGG; pon:100174567; -.
DR   CTD; 51205; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   InParanoid; Q5R8C0; -.
DR   OrthoDB; 5477542at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11567:SF202; LYSOPHOSPHATIDIC ACID PHOSPHATASE TYPE 6; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipid metabolism; Mitochondrion; Phospholipid metabolism;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..428
FT                   /note="Lysophosphatidic acid phosphatase type 6"
FT                   /id="PRO_0000023967"
FT   REGION          58..168
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        59
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        335
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  48771 MW;  76F75BB45A6C46B0 CRC64;
     MITGVFSMRL WTPVGVLTSL AYCLHQRRVA LAELQEADGR RPVDRSLLKS KMVQVVFRHG
     ARSPRKPLPL EEQVEWNPQL LEVPPQTQFD YTVTNLAGGP KPYSPYDAQY CETTLKGGMF
     AGQLTKVGMQ QMFALGERLR KNYVEDIPFL SPTFSPQEVF IRSTNIFRNL ESTRCLLAGL
     FQCQKEGPII IHTDEADSEV LYPNYQSCWS LRQRTRGRRQ TASLQPGISE DLKKVKDRMG
     IDSSDKVDFF ILLDNMAAEQ AHNLPSCPML KRFAQMIEQR AVDTSLYILP KEDRESLQMA
     VGPLLHILES NLLKAMDSAT APDKIRKLYL YAAHDVTLIP LLMTLGIFDH KWPPFAVDLT
     MELYQHLESK EWFVQLYYHG KEQVPRGCPD GLCPLDMFLN AMSVYTLSPE KYHALCSQTQ
     VMEVGNGE
//