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Database: UniProt
Entry: I3MGQ7_ICTTR
LinkDB: I3MGQ7_ICTTR
Original site: I3MGQ7_ICTTR 
ID   I3MGQ7_ICTTR            Unreviewed;       428 AA.
AC   I3MGQ7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Sphingosine-1-phosphate phosphatase 1 {ECO:0000313|Ensembl:ENSSTOP00000009979.3};
GN   Name=SGPP1 {ECO:0000313|Ensembl:ENSSTOP00000009979.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000009979.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000009979.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AGTP01026955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MGQ7; -.
DR   STRING; 43179.ENSSTOP00000009979; -.
DR   Ensembl; ENSSTOT00000011125.3; ENSSTOP00000009979.3; ENSSTOG00000011129.3.
DR   eggNOG; KOG2822; Eukaryota.
DR   GeneTree; ENSGT00940000158836; -.
DR   HOGENOM; CLU_043042_1_0_1; -.
DR   InParanoid; I3MGQ7; -.
DR   TreeFam; TF323419; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IEA:Ensembl.
DR   GO; GO:0035621; P:ER to Golgi ceramide transport; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0006668; P:sphinganine-1-phosphate metabolic process; IEA:Ensembl.
DR   GO; GO:0006670; P:sphingosine metabolic process; IEA:Ensembl.
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:UP000005215};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        115..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..262
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          30..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  48044 MW;  4445B52741B1EEA2 CRC64;
     MSLRQHLAQL AACLQEPQKV ARFQRLCGVE APPNRSADRR EDEKLEAPLA GDPRRRGRQS
     GATEVKPDGS GAPNGVRNGL AAELGPTSSQ RAGSLRRNSL TGEEGELARL SNWPLYYLFC
     FGTELGNELF YIMFFPFWIW NLDPLVGRRL VIIWVLVMYL GQCTKDIIRW PRPSSPPVVK
     LEVFYNSEYS MPSTHAMSGT AIPIAMVLLT YGRWQYPPIY GLILIPCWCS LVCLSRIYMG
     MHSILDIIAG FLYTILILAV FYPFVDLIDN FNQTHKYAPL IIIGLHLSLG IFSFTLDTWS
     TSRGDTAEIL GSGAGIACGS HVAYSVGLLL DPSLEILPFT RPPITVTLFG KAILRILIGM
     IFVLIVRDIM KKITIPLACK IFNIPCDDIR KARQHMEVEL PYRYITYGMV GFSITFLVPY
     IFFFIGIS
//
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