ID M3YZ11_MUSPF Unreviewed; 326 AA.
AC M3YZ11;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Sphingosine-1-phosphate phosphatase 2 {ECO:0000313|Ensembl:ENSMPUP00000016571.1};
GN Name=SGPP2 {ECO:0000313|Ensembl:ENSMPUP00000016571.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000016571.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000016571.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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DR EMBL; AEYP01056913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YZ11; -.
DR STRING; 9669.ENSMPUP00000016571; -.
DR Ensembl; ENSMPUT00000016817.1; ENSMPUP00000016571.1; ENSMPUG00000016674.1.
DR eggNOG; KOG2822; Eukaryota.
DR GeneTree; ENSGT00940000159500; -.
DR HOGENOM; CLU_043042_1_0_1; -.
DR InParanoid; M3YZ11; -.
DR OMA; YWVNEQL; -.
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:0061469; P:regulation of type B pancreatic cell proliferation; 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:SF14; SPHINGOSINE-1-PHOSPHATE PHOSPHATASE 2; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..160
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 326 AA; 36899 MW; 0AFE8F9155D154AA CRC64;
AYVQKYIVKN YFYYYLFRFS AALGQEVFYI TFLPFTHWNI DPYLSRRLII IWVLVMYIGQ
VAKDILKWPR PLSPPVVKLE KRVIDEYGMP STHAMAATVI SFTLLLSTMD RYQYPFALGL
LMAVVFSTLV CLSRLYTGMH TVLDVLGGIL VTAVLIVLTY PAWTLIDRLD SASPLFPVCV
IVVPFFLCYN YPVSDCYSPT RADTTTILAA GAGVTLGFWI NHFFQLASAP TEALPVVQNI
PPLTANMLVL GLTKFAVGIV LILLVRQLVQ NLSLQVLYSC FKVVTRNKEA RRRLEIEVPY
KFVTYTSVGL CATTFVPMLH RFLGLL
//
