DS1PP_SCHPO
ID DS1PP_SCHPO Reviewed; 411 AA.
AC Q9P6N5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Dihydrosphingosine 1-phosphate phosphatase C823.11;
DE EC=3.1.3.-;
GN ORFNames=SPAC823.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Dihydrosphingosine 1-phosphate phosphatase required for
CC efficient ceramide synthesis from exogenous sphingoid bases. Involved
CC in endocytosis and calcium-mediated signaling (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB90156.1; -; Genomic_DNA.
DR RefSeq; NP_593838.1; NM_001019267.2.
DR AlphaFoldDB; Q9P6N5; -.
DR STRING; 4896.SPAC823.11.1; -.
DR MaxQB; Q9P6N5; -.
DR PaxDb; Q9P6N5; -.
DR EnsemblFungi; SPAC823.11.1; SPAC823.11.1:pep; SPAC823.11.
DR GeneID; 2543496; -.
DR KEGG; spo:SPAC823.11; -.
DR PomBase; SPAC823.11; -.
DR VEuPathDB; FungiDB:SPAC823.11; -.
DR eggNOG; KOG2822; Eukaryota.
DR HOGENOM; CLU_019266_1_0_1; -.
DR InParanoid; Q9P6N5; -.
DR OMA; HYLQDPH; -.
DR PhylomeDB; Q9P6N5; -.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q9P6N5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISO:PomBase.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:PomBase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..411
FT /note="Dihydrosphingosine 1-phosphate phosphatase C823.11"
FT /id="PRO_0000359401"
FT TOPO_DOM 1..74
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..170
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..191
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 196..216
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..233
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 234..254
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..293
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 388..408
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..411
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 115..123
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 144..147
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 191..202
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 198
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 202
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
SQ SEQUENCE 411 AA; 46847 MW; 3EFC81F484B81862 CRC64;
MVHKKKNVDI PSSQKYLGIQ HVNFYSNAFG KESLRFQLRE LILPIVRKET RLLYKIQSFF
RNPWLDVYFM YTATLGTHVF FMLALPIFFW SGCIYYTLDI TQLFAAGVYF SGCIKDYFCL
PRPRSPPMVR LTLSSDAEYE YGFPSTHTTN AMATGFYSLF LLLSMSDSMS SISYYFLLSL
VLLYIASISL GRIYCGMHGF MDVSTGTILG VTLAIFQWKY ADFFHNVWSS SSTSVPILSV
VLALFFIWFH PQPAERCICL EDSISFISVI MGIDLGTWFA SPESLSHLHD NLNSYFLLKF
FVRVLFGVCM ILIWKSFAKQ ALLAVLPPIF KSLRLSYLEP KSQSEKGIRA ATGSNHSPGN
IGTELGVITS HQSHPHPVRF DIETIARIIV YSGIGFLCTY FAPKVFLKWK I
