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Database: UniProt
Entry: G3P9U1_GASAC
LinkDB: G3P9U1_GASAC
Original site: G3P9U1_GASAC 
ID   G3P9U1_GASAC            Unreviewed;       386 AA.
AC   G3P9U1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Sphingosine-1-phosphate phosphatase 1 {ECO:0000313|Ensembl:ENSGACP00000014365.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000014365.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000014365.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000014365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3P9U1; -.
DR   STRING; 69293.ENSGACP00000014365; -.
DR   Ensembl; ENSGACT00000014390.1; ENSGACP00000014365.1; ENSGACG00000010855.1.
DR   eggNOG; KOG2822; Eukaryota.
DR   GeneTree; ENSGT00940000158836; -.
DR   InParanoid; G3P9U1; -.
DR   OMA; CDYIGNC; -.
DR   TreeFam; TF323419; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000010855; Expressed in intestinal epithelial cell and 10 other cell types or tissues.
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:UP000007635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..234
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          35..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  43158 MW;  6CA4285BE7ED7444 CRC64;
     MGKSNRLLNL YHYLQDPHLV ARFQHFCGVR ETFSNGRSSC PPDLTGATES EEPGNEKAPG
     SSGTVKPLRK NSLTGDAGQE FLIQNRFLYY AFTLGTELGN ELFYITFFPF VTWNVDAFVS
     RRLIMVWVWV MYLGQCTKDL LGWSRPASPP VIKVEMFYNS EYSMPSTHAM SGTAIPFSLF
     FMTYGRWEYP FPLGFSLALC WCLLVCVRIY MGMHSVLDVI AGVLYSVLIL LFFLPALDLI
     DGFNLSCRYA PLIIVCLHLG LGLFSFTLDT WSTSRGDTAQ ILGTGAGVAL ASHVNHRLGL
     MPDPTPDQLP LLRLALGVLV LMATRALMKA VTIPAVCRVF GVPSGDVRKA RQRMEVELPY
     RYIVYGAVGF NVLFLVPLLF SYTRLS
//
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