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Database: UniProt
Entry: G1M5Q1_AILME
LinkDB: G1M5Q1_AILME
Original site: G1M5Q1_AILME 
ID   G1M5Q1_AILME            Unreviewed;       286 AA.
AC   G1M5Q1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Phospholipid phosphatase 1 {ECO:0000256|ARBA:ARBA00021834};
DE            EC=3.1.3.106 {ECO:0000256|ARBA:ARBA00012497};
DE            EC=3.1.3.4 {ECO:0000256|ARBA:ARBA00012638};
DE            EC=3.6.1.75 {ECO:0000256|ARBA:ARBA00038902};
DE   AltName: Full=Lipid phosphate phosphohydrolase 1 {ECO:0000256|ARBA:ARBA00030630};
DE   AltName: Full=PAP2-alpha {ECO:0000256|ARBA:ARBA00032601};
DE   AltName: Full=Phosphatidate phosphohydrolase type 2a {ECO:0000256|ARBA:ARBA00030413};
DE   AltName: Full=Phosphatidic acid phosphatase 2a {ECO:0000256|ARBA:ARBA00031161};
GN   Name=PLPP1 {ECO:0000313|Ensembl:ENSAMEP00000014669.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000014669.1, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000014669.1, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000014669.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC         octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC         ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC         Evidence={ECO:0000256|ARBA:ARBA00000974};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC         di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:74546; Evidence={ECO:0000256|ARBA:ARBA00000980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC         Evidence={ECO:0000256|ARBA:ARBA00000980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC         dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC         ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC         Evidence={ECO:0000256|ARBA:ARBA00001611};
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:0000256|ARBA:ARBA00000235};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000256|ARBA:ARBA00000235};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC         H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC         Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC         Evidence={ECO:0000256|ARBA:ARBA00023681};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC         Evidence={ECO:0000256|ARBA:ARBA00023681};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC         octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC         ChEBI:CHEBI:145465; Evidence={ECO:0000256|ARBA:ARBA00001542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC         Evidence={ECO:0000256|ARBA:ARBA00001542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC         octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC         ChEBI:CHEBI:85376; Evidence={ECO:0000256|ARBA:ARBA00001710};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC         Evidence={ECO:0000256|ARBA:ARBA00001710};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC         phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC         Evidence={ECO:0000256|ARBA:ARBA00001476};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC         Evidence={ECO:0000256|ARBA:ARBA00001476};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC         Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC         Evidence={ECO:0000256|ARBA:ARBA00001716};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC         Evidence={ECO:0000256|ARBA:ARBA00001716};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC         glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001180};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000256|ARBA:ARBA00001180};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75;
CC         Evidence={ECO:0000256|ARBA:ARBA00035886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC         Evidence={ECO:0000256|ARBA:ARBA00035886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC         phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC         EC=3.1.3.106; Evidence={ECO:0000256|ARBA:ARBA00001472};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC         Evidence={ECO:0000256|ARBA:ARBA00001472};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC         enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC         Evidence={ECO:0000256|ARBA:ARBA00023977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC         Evidence={ECO:0000256|ARBA:ARBA00023977};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005074}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Membrane raft
CC       {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004314}. Membrane, caveola
CC       {ECO:0000256|ARBA:ARBA00004189}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004189}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   RefSeq; XP_011234182.1; XM_011235880.2.
DR   AlphaFoldDB; G1M5Q1; -.
DR   STRING; 9646.ENSAMEP00000014669; -.
DR   Ensembl; ENSAMET00000015276.2; ENSAMEP00000014669.1; ENSAMEG00000013923.2.
DR   GeneID; 100479871; -.
DR   CTD; 8611; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000156730; -.
DR   HOGENOM; CLU_021458_3_1_1; -.
DR   InParanoid; G1M5Q1; -.
DR   OMA; YLAMYLQ; -.
DR   OrthoDB; 25293at2759; -.
DR   TreeFam; TF316040; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IEA:Ensembl.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR   GO; GO:0006670; P:sphingosine metabolic process; IEA:Ensembl.
DR   CDD; cd03384; PAP2_wunen; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF26; PHOSPHOLIPID PHOSPHATASE 1; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..244
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          258..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  32138 MW;  475141D4581AC466 CRC64;
     MFDKTRLPYV ALDVLCVLLA CLPMAVLNLS QINPFQRGFF CKDNSIQYPY HDSTVTSTVL
     TIVGLGLPIS SMIIGEALSV YCNLLHSNSF IRNNYIATIY KSIGTFLFGA AASQSLTDIA
     KYSIGRLRPH FLDVCDPDWS KINCSAGYIE NYICQGNAQK VKEGRLSFYS GHSSFSMYCM
     LFVALYLQAR MKGDWARLLR PTLQFGLVAV SIYVGLSRVS DYKHHWSDVL TGLLQGALVA
     ILVAVYVSDF FKERNSPFKE RKEEDSHTTL HETPTTGNHF RNSHQP
//
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