SGPP1_RAT
ID SGPP1_RAT Reviewed; 430 AA.
AC Q99P55;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Sphingosine-1-phosphate phosphatase 1 {ECO:0000305};
DE Short=SPPase1;
DE Short=Spp1;
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9BX95};
DE AltName: Full=Sphingosine-1-phosphatase 1;
GN Name=Sgpp1 {ECO:0000312|RGD:727829};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 125-304.
RC STRAIN=Sprague-Dawley;
RA Yoshimura S., Salomone S., Waeber C.;
RT "Rattus norvegicus sphingosine-1-phosphate phosphohydrolase (Spp1) mRNA
RT sequence.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Sphingosine-1-phosphate
CC phosphatase activity is needed for efficient recycling of sphingosine
CC into the sphingolipid synthesis pathway. Regulates the intracellular
CC levels of the bioactive sphingolipid metabolite S1P that regulates
CC diverse biological processes acting both as an extracellular receptor
CC ligand or as an intracellular second messenger (By similarity).
CC Involved in efficient ceramide synthesis from exogenous sphingoid
CC bases. Converts S1P to sphingosine, which is readily metabolized to
CC ceramide via ceramide synthase. In concert with sphingosine kinase 2
CC (SphK2), 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 (By similarity). 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. Also
CC involved in unfolded protein response (UPR) and ER stress-induced
CC autophagy via regulation of intracellular S1P levels (By similarity).
CC Involved in the regulation of epidermal homeostasis and keratinocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q9BX95,
CC ECO:0000250|UniProtKB:Q9JI99}.
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:0000250|UniProtKB:Q9BX95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27515;
CC Evidence={ECO:0000250|UniProtKB:Q9BX95};
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:0000250|UniProtKB:Q9BX95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000250|UniProtKB:Q9BX95};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BX95}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9JI99}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03048654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03050704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF329638; AAK07473.1; -; mRNA.
DR AlphaFoldDB; Q99P55; -.
DR STRING; 10116.ENSRNOP00000006913; -.
DR iPTMnet; Q99P55; -.
DR PhosphoSitePlus; Q99P55; -.
DR jPOST; Q99P55; -.
DR PaxDb; Q99P55; -.
DR UCSC; RGD:727829; rat.
DR RGD; 727829; Sgpp1.
DR eggNOG; KOG2822; Eukaryota.
DR InParanoid; Q99P55; -.
DR PhylomeDB; Q99P55; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q99P55; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070780; F:dihydrosphingosine-1-phosphate phosphatase activity; IEA:RHEA.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; ISS:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISO:RGD.
DR GO; GO:0006670; P:sphingosine metabolic process; ISO:RGD.
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..430
FT /note="Sphingosine-1-phosphate phosphatase 1"
FT /id="PRO_0000114479"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 34..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..175
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 194..197
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 237..248
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT COMPBIAS 40..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 248
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:22673903"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX95"
SQ SEQUENCE 430 AA; 47649 MW; 0C95136FE9B14D4C CRC64;
MSLGQRLALL AIRLQEPQRV ASFQRLCGVE VPLGSPKAGE DAETEVRGAP GDPRRRPRQS
GADGSPAKPD CCGAPNGVRN GLAAEPGPTG PRRAGSLRRN SLTGEEGELA KVSNLPLYYL
FCFGTELGNE LFYIIFFPFW IWNLDPFVGR RLVIIWVLVM YLGQCTKDII RWPRPASPPV
IKLEIFYNSE YSMPSTHAMS GTAIPIAMIL LTYGRWQYPL IYGLILIPCW SSLVCLSRIY
MGMHSILDVI AGFLYTILIL IIFYPLVDLI DNFNQTYKYA PLIIIGLHLI LGIFSFTLDT
WSTSRGDTAE ILGSGAGIAC GSHAAYNLGI SLDPSLHTLP LAIPPLTVTL FGKAILRVVI
GMLLVLFVRD IMKKVTIPLA CKLFGIPCHD LRQARQHMEV ELPYRYITYG TVGFSITFLI
PYIFSFIGIS
