ID A0A096MFW0_POEFO Unreviewed; 430 AA.
AC A0A096MFW0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Sphingosine-1-phosphate phosphatase 1-like {ECO:0000313|Ensembl:ENSPFOP00000030301.1};
GN Name=SGPP1 {ECO:0000313|Ensembl:ENSPFOP00000030301.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000030301.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000030301.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; AYCK01011261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01011262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096MFW0; -.
DR Ensembl; ENSPFOT00000025652.1; ENSPFOP00000030301.1; ENSPFOG00000010284.2.
DR GeneTree; ENSGT00940000158836; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03388; PAP2_SPPase1; 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 PANTHER; PTHR14969:SF45; SPHINGOSINE-1-PHOSPHATE PHOSPHATASE 1; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..264
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 430 AA; 47949 MW; D83281D60323D0C4 CRC64;
ESQLNMVRVM EYLRYLQDPH LVARFQLICG IRGTLSEPVP ADISTSDSCS MGVQRRIADV
TDPRKLKHDM EDAPPNGAAL SPGGESVAVR GSTLKPLRRN SLTGEAGQEF VIENRFLFYL
FTFGTELGNE LFYIIFFPFI MWNVDAFVSR RLIMVWVWVM YVGQCTKDVI GWPRPASPPV
VKVEMFYNSE YSMPSTHAMS GTAIPFSLFF MTHGRWEYPY TLGFSLALCW CLLVCSSRIY
MGMHSVLDVI AGILYSILIL FFFLPALDMI DSFNLSSRYA PLVIVSIPLA LALFSFTLDT
WSTSRGDTAQ ILGVGAGVAL ASHVNQLLGL MPDLTADQLP LMVPTVSGGL VCSAILRLVL
GVIVLVAIRA LMKAITIPLV CWLFRVPSSD LRKARQHVEV ELPYRYIVYG TMGFSVLFLV
PLLFAYVENA
//