SGPP1_HUMAN
ID SGPP1_HUMAN Reviewed; 441 AA.
AC Q9BX95; B2RAH0; Q9H189;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sphingosine-1-phosphate phosphatase 1 {ECO:0000305};
DE Short=SPPase1;
DE Short=Spp1;
DE Short=hSPP1;
DE Short=hSPPase1;
DE EC=3.1.3.- {ECO:0000269|PubMed:12815058, ECO:0000269|PubMed:16782891};
DE AltName: Full=Sphingosine-1-phosphatase 1;
DE AltName: Full=Sphingosine-1-phosphate phosphohydrolase 1 {ECO:0000303|PubMed:16782891};
DE Short=SPP-1 {ECO:0000303|PubMed:16782891};
GN Name=SGPP1 {ECO:0000312|HGNC:HGNC:17720};
GN Synonyms=SPP1 {ECO:0000303|PubMed:16782891};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Fetal kidney;
RX PubMed=12815058; DOI=10.1074/jbc.m301741200;
RA Johnson K.R., Johnson K.Y., Becker K.P., Bielawski J., Mao C., Obeid L.M.;
RT "Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of
RT intra- and extracellular sphingosine-1-phosphate levels and cell
RT viability.";
RL J. Biol. Chem. 278:34541-34547(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Cloning of human sphingosine-1-phosphatase.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=11756451; DOI=10.1074/jbc.m109968200;
RA Le Stunff H., Peterson C., Thornton R., Milstien S., Mandala S.M.,
RA Spiegel S.;
RT "Characterization of murine sphingosine-1-phosphate phosphohydrolase.";
RL J. Biol. Chem. 277:8920-8927(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16782891; DOI=10.1128/mcb.02107-05;
RA Giussani P., Maceyka M., Le Stunff H., Mikami A., Lepine S., Wang E.,
RA Kelly S., Merrill A.H. Jr., Milstien S., Spiegel S.;
RT "Sphingosine-1-phosphate phosphohydrolase regulates endoplasmic reticulum-
RT to-golgi trafficking of ceramide.";
RL Mol. Cell. Biol. 26:5055-5069(2006).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF HIS-208.
RX PubMed=18583713; DOI=10.1161/circresaha.108.173575;
RA Peter B.F., Lidington D., Harada A., Bolz H.J., Vogel L., Heximer S.,
RA Spiegel S., Pohl U., Bolz S.S.;
RT "Role of sphingosine-1-phosphate phosphohydrolase 1 in the regulation of
RT resistance artery tone.";
RL Circ. Res. 103:315-324(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION.
RX PubMed=20798685; DOI=10.1038/cdd.2010.104;
RA Lepine S., Allegood J.C., Park M., Dent P., Milstien S., Spiegel S.;
RT "Sphingosine-1-phosphate phosphohydrolase-1 regulates ER stress-induced
RT autophagy.";
RL Cell Death Differ. 18:350-361(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Specifically dephosphorylates sphingosine 1-phosphate (S1P),
CC dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate,
CC lysophosphatidic acid or phosphatidic acid (PubMed:16782891).
CC Sphingosine-1-phosphate phosphatase activity is needed for efficient
CC recycling of sphingosine into the sphingolipid synthesis pathway
CC (PubMed:12815058, PubMed:11756451, PubMed:16782891). Regulates the
CC intracellular levels of the bioactive sphingolipid metabolite S1P that
CC regulates diverse biological processes acting both as an extracellular
CC receptor ligand or as an intracellular second messenger
CC (PubMed:11756451, PubMed:12815058, PubMed:16782891). Involved in
CC efficient ceramide synthesis from exogenous sphingoid bases. Converts
CC S1P to sphingosine, which is readily metabolized to ceramide via
CC ceramide synthase. In concert with sphingosine kinase 2 (SphK2),
CC recycles sphingosine into ceramide through a
CC phosphorylation/dephosphorylation cycle (By similarity). Regulates
CC endoplasmic-to-Golgi trafficking of ceramides, resulting in the
CC regulation of ceramide levels in the endoplasmic reticulum,
CC preferentially long-chain ceramide species, and influences the
CC anterograde membrane transport of both ceramide and proteins from the
CC endoplasmic reticulum to the Golgi apparatus (PubMed:16782891). The
CC modulation of intracellular ceramide levels in turn regulates apoptosis
CC (By similarity). Via S1P levels, modulates resting tone, intracellular
CC Ca(2+) and myogenic vasoconstriction in resistance arteries
CC (PubMed:18583713). Also involved in unfolded protein response (UPR) and
CC ER stress-induced autophagy via regulation of intracellular S1P levels
CC (PubMed:20798685, PubMed:18583713). Involved in the regulation of
CC epidermal homeostasis and keratinocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9JI99, ECO:0000269|PubMed:11756451,
CC ECO:0000269|PubMed:12815058, ECO:0000269|PubMed:16782891,
CC ECO:0000269|PubMed:18583713, ECO:0000269|PubMed:20798685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphinganine 1-phosphate = phosphate + sphinganine;
CC Xref=Rhea:RHEA:27514, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:57939;
CC Evidence={ECO:0000269|PubMed:12815058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27515;
CC Evidence={ECO:0000269|PubMed:12815058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC Evidence={ECO:0000269|PubMed:12815058, ECO:0000269|PubMed:16782891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000269|PubMed:12815058, ECO:0000269|PubMed:16782891};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12815058}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9JI99}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the strongest level in placenta
CC and kidney. {ECO:0000269|PubMed:12815058}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AF349315; AAK26660.1; -; mRNA.
DR EMBL; AJ293294; CAC17772.1; -; mRNA.
DR EMBL; AK314188; BAG36867.1; -; mRNA.
DR EMBL; AL161670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80834.1; -; Genomic_DNA.
DR EMBL; BC063839; AAH63839.1; -; mRNA.
DR EMBL; BC070060; AAH70060.1; -; mRNA.
DR CCDS; CCDS9760.1; -.
DR RefSeq; NP_110418.1; NM_030791.3.
DR AlphaFoldDB; Q9BX95; -.
DR BioGRID; 123508; 46.
DR IntAct; Q9BX95; 26.
DR STRING; 9606.ENSP00000247225; -.
DR SwissLipids; SLP:000000158; -.
DR DEPOD; SGPP1; -.
DR iPTMnet; Q9BX95; -.
DR PhosphoSitePlus; Q9BX95; -.
DR BioMuta; SGPP1; -.
DR DMDM; 46577706; -.
DR EPD; Q9BX95; -.
DR jPOST; Q9BX95; -.
DR MassIVE; Q9BX95; -.
DR MaxQB; Q9BX95; -.
DR PaxDb; Q9BX95; -.
DR PeptideAtlas; Q9BX95; -.
DR PRIDE; Q9BX95; -.
DR ProteomicsDB; 79388; -.
DR Antibodypedia; 47291; 96 antibodies from 17 providers.
DR DNASU; 81537; -.
DR Ensembl; ENST00000247225.7; ENSP00000247225.6; ENSG00000126821.8.
DR Ensembl; ENST00000645915.2; ENSP00000496280.1; ENSG00000285281.2.
DR GeneID; 81537; -.
DR KEGG; hsa:81537; -.
DR MANE-Select; ENST00000247225.7; ENSP00000247225.6; NM_030791.4; NP_110418.1.
DR UCSC; uc001xgj.5; human.
DR CTD; 81537; -.
DR DisGeNET; 81537; -.
DR GeneCards; SGPP1; -.
DR HGNC; HGNC:17720; SGPP1.
DR HPA; ENSG00000126821; Low tissue specificity.
DR MIM; 612826; gene.
DR neXtProt; NX_Q9BX95; -.
DR OpenTargets; ENSG00000126821; -.
DR PharmGKB; PA134884424; -.
DR VEuPathDB; HostDB:ENSG00000126821; -.
DR eggNOG; KOG2822; Eukaryota.
DR GeneTree; ENSGT00940000158836; -.
DR HOGENOM; CLU_043042_1_0_1; -.
DR InParanoid; Q9BX95; -.
DR OMA; HYLQDPH; -.
DR OrthoDB; 721150at2759; -.
DR PhylomeDB; Q9BX95; -.
DR TreeFam; TF323419; -.
DR PathwayCommons; Q9BX95; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q9BX95; -.
DR BioGRID-ORCS; 81537; 103 hits in 1079 CRISPR screens.
DR ChiTaRS; SGPP1; human.
DR GeneWiki; SGPP1; -.
DR GenomeRNAi; 81537; -.
DR Pharos; Q9BX95; Tbio.
DR PRO; PR:Q9BX95; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BX95; protein.
DR Bgee; ENSG00000126821; Expressed in lymph node and 100 other tissues.
DR Genevisible; Q9BX95; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070780; F:dihydrosphingosine-1-phosphate phosphatase activity; TAS:Reactome.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:UniProtKB.
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:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0045682; P:regulation of epidermis development; ISS:UniProtKB.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006668; P:sphinganine-1-phosphate metabolic process; IEA:Ensembl.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR GO; GO:0006670; P:sphingosine metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..441
FT /note="Sphingosine-1-phosphate phosphatase 1"
FT /id="PRO_0000114477"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 25..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..186
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 205..208
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 248..259
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT COMPBIAS 32..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 259
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MUTAGEN 208
FT /note="H->A: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:18583713"
FT CONFLICT 146
FT /note="L -> P (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> A (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="D -> G (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> T (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="I -> V (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="F -> S (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="E -> G (in Ref. 1; AAK26660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49108 MW; 86A018DDDA3A3019 CRC64;
MSLRQRLAQL VGRLQDPQKV ARFQRLCGVE APPRRSADRR EDEKAEAPLA GDPRLRGRQP
GAPGGPQPPG SDRNQCPAKP DGGGAPNGVR NGLAAELGPA SPRRAGALRR NSLTGEEGQL
ARVSNWPLYC LFCFGTELGN ELFYILFFPF WIWNLDPLVG RRLVVIWVLV MYLGQCTKDI
IRWPRPASPP VVKLEVFYNS EYSMPSTHAM SGTAIPISMV LLTYGRWQYP LIYGLILIPC
WCSLVCLSRI YMGMHSILDI IAGFLYTILI LAVFYPFVDL IDNFNQTHKY APFIIIGLHL
ALGIFSFTLD TWSTSRGDTA EILGSGAGIA CGSHVTYNMG LVLDPSLDTL PLAGPPITVT
LFGKAILRIL IGMVFVLIIR DVMKKITIPL ACKIFNIPCD DIRKARQHME VELPYRYITY
GMVGFSITFF VPYIFFFIGI S
