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Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (EC 3 1 3 -) (Sphingosine-1-phosphatase 1)

 SGPP1_RAT               Reviewed;         430 AA.
Q99P55;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
10-OCT-2003, sequence version 2.
22-APR-2020, entry version 99.
RecName: Full=Sphingosine-1-phosphate phosphatase 1 {ECO:0000305};
Short=SPPase1;
Short=Spp1;
EC=3.1.3.- {ECO:0000250|UniProtKB:Q9BX95};
AltName: Full=Sphingosine-1-phosphatase 1;
Name=Sgpp1 {ECO:0000312|RGD:727829};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
Mockrin S., Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into mammalian
evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE OF 125-304.
STRAIN=Sprague-Dawley;
Yoshimura S., Salomone S., Waeber C.;
"Rattus norvegicus sphingosine-1-phosphate phosphohydrolase (Spp1) mRNA
sequence.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Specifically dephosphorylates sphingosine 1-phosphate (S1P),
dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate,
lysophosphatidic acid or phosphatidic acid. Sphingosine-1-phosphate
phosphatase activity is needed for efficient recycling of sphingosine
into the sphingolipid synthesis pathway. Regulates the intracellular
levels of the bioactive sphingolipid metabolite S1P that regulates
diverse biological processes acting both as an extracellular receptor
ligand or as an intracellular second messenger (By similarity).
Involved in efficient ceramide synthesis from exogenous sphingoid
bases. Converts S1P to sphingosine, which is readily metabolized to
ceramide via ceramide synthase. In concert with sphingosine kinase 2
(SphK2), recycles sphingosine into ceramide through a
phosphorylation/dephosphorylation cycle (By similarity). Regulates
endoplasmic-to-Golgi trafficking of ceramides, resulting in the
regulation of ceramide levels in the endoplasmic reticulum,
preferentially long-chain ceramide species, and influences the
anterograde membrane transport of both ceramide and proteins from the
endoplasmic retiulum to the Golgi apparatus (By similarity). The
modulation of intracellular ceramide levels in turn regulates apoptosis
(By similarity). Via S1P levels, modulates resting tone, intracellular
Ca(2+) and myogenic vasoconstriction in resistance arteries. Also
involved in unfolded protein response (UPR) and ER stress-induced
autophagy via regulation of intracellular S1P levels (By similarity).
Involved in the regulation of epidermal homeostasis and keratinocyte
differentiation (By similarity). {ECO:0000250|UniProtKB:Q9BX95,
ECO:0000250|UniProtKB:Q9JI99}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + sphinganine 1-phosphate = phosphate + sphinganine;
Xref=Rhea:RHEA:27514, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57817, ChEBI:CHEBI:57939;
Evidence={ECO:0000250|UniProtKB:Q9BX95};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27515;
Evidence={ECO:0000250|UniProtKB:Q9BX95};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
Evidence={ECO:0000250|UniProtKB:Q9BX95};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
Evidence={ECO:0000250|UniProtKB:Q9BX95};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9BX95}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9JI99}; Multi-pass
membrane protein {ECO:0000255}.
-!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
{ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AABR03048654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03050704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF329638; AAK07473.1; -; mRNA.
STRING; 10116.ENSRNOP00000006913; -.
iPTMnet; Q99P55; -.
PhosphoSitePlus; Q99P55; -.
jPOST; Q99P55; -.
PaxDb; Q99P55; -.
PRIDE; Q99P55; -.
UCSC; RGD:727829; rat.
RGD; 727829; Sgpp1.
eggNOG; ENOG410IQK8; Eukaryota.
eggNOG; ENOG410Z1GR; LUCA.
InParanoid; Q99P55; -.
PhylomeDB; Q99P55; -.
Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
PRO; PR:Q99P55; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
GO; GO:0035621; P:ER to Golgi ceramide transport; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0045682; P:regulation of epidermis development; ISS:UniProtKB.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0006668; P:sphinganine-1-phosphate metabolic process; ISO:RGD.
GO; GO:0006665; P:sphingolipid metabolic process; ISO:RGD.
GO; GO:0006670; P:sphingosine metabolic process; ISO:RGD.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Cell membrane; Endoplasmic reticulum; Hydrolase; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1..430
/note="Sphingosine-1-phosphate phosphatase 1"
/id="PRO_0000114479"
TRANSMEM 121..141
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 152..172
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 193..213
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 216..236
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 246..266
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 279..299
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 311..331
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 348..368
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 409..429
/note="Helical"
/evidence="ECO:0000255"
REGION 167..175
/note="Phosphatase sequence motif I"
/evidence="ECO:0000305"
REGION 194..197
/note="Phosphatase sequence motif II"
/evidence="ECO:0000305"
REGION 237..248
/note="Phosphatase sequence motif III"
/evidence="ECO:0000305"
ACT_SITE 197
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:P0A924"
ACT_SITE 244
/note="Nucleophile"
/evidence="ECO:0000250|UniProtKB:P0A924"
SITE 248
/note="Stabilizes the active site histidine for
nucleophilic attack"
/evidence="ECO:0000250|UniProtKB:P0A924"
MOD_RES 101
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 103
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q9BX95"
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


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Pathways :
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2353: vitamin B9 (folate) biosynthesis pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP76: TCA Cycle
WP1709: Thiamine metabolism
WP1652: Fructose and mannose metabolism
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP1696: Riboflavin metabolism
WP1028: Pentose Phosphate Pathway
WP2212: Methylerythritol phosphate pathway
WP1370: TGF Beta Signaling Pathway
WP560: TGF Beta Signaling Pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP63: Pentose Phosphate Pathway
WP1067: Toll-like receptor signaling pathway
WP1164: TGF Beta Signaling Pathway
WP829: Toll-like receptor signaling pathway
WP122: Pentose Phosphate Pathway
WP282: Pentose Phosphate Pathway
WP1664: Inositol phosphate metabolism
WP930: TGF Beta Signaling Pathway
WP1271: Toll-like receptor signaling pathway
WP369: Pentose Phosphate Pathway
WP134: Pentose Phosphate Pathway

Related Genes :
[Sgpp1 Spp1 Spph1] Sphingosine-1-phosphate phosphatase 1 (SPP) (SPPase1) (mSPP1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1)
[SGPP1 SPP1] Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (hSPP1) (hSPPase1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1) (Sphingosine-1-phosphate phosphohydrolase 1) (SPP-1)
[Sgpp1] Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1)
[sglA DDB_G0282819] Sphingosine-1-phosphate lyase (S1P lyase) (S1PL) (SP-lyase) (SPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase)
[SPHK1 SK1 SPHK SPK] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91) (Acetyltransferase SPHK1) (EC 2.3.1.-)
[Sphk1 Sk1] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91) (Acetyltransferase SPHK1) (EC 2.3.1.-)
[Sphk1] Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91) (Acetyltransferase SPHK1) (EC 2.3.1.-)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[SGPL1 KIAA1252] Sphingosine-1-phosphate lyase 1 (S1PL) (SP-lyase 1) (SPL 1) (hSPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase)
[Sgpl1 Spl] Sphingosine-1-phosphate lyase 1 (S1PL) (SP-lyase 1) (SPL 1) (mSPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[Plpp1 Hpic53 Lpp1 Ppap2a] Phospholipid phosphatase 1 (EC 3.1.3.-) (EC 3.1.3.106) (EC 3.1.3.4) (EC 3.1.3.81) (35 kDa PAP) (mPAP) (Hydrogen peroxide-inducible protein 53) (Hic53) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a)
[PLPP3 LPP3 PPAP2B] Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b) (Vascular endothelial growth factor and type I collagen-inducible protein) (VCIP)
[Plpp3 Lpp3 Ppap2b] Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b)
[s1pr1 edg1] Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1)
[Plpp3 Lpp3 Ppap2b] Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Differentially expressed in rat intestine 42) (Dri42) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b)
[PLPP3 PPAP2B] Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b)
[S1PR2 EDG5] Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Endothelial differentiation G-protein coupled receptor 5) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5)
[SAC1 RSD1 YKL212W] Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Recessive suppressor of secretory defect)
[CERS3 LASS3] Ceramide synthase 3 (CerS3) (EC 2.3.1.-) (Dihydroceramide synthase 3) (LAG1 longevity assurance homolog 3) (Sphingosine N-acyltransferase CERS3) (EC 2.3.1.24)
[fbp TK2164] Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase)
[Cers5 Lass5 Trh4] Ceramide synthase 5 (CerS5) (EC 2.3.1.-) (LAG1 longevity assurance homolog 5) (Sphingosine N-acyltransferase CERS5) (EC 2.3.1.24) (Translocating chain-associating membrane protein homolog 4) (TRAM homolog 4)
[TPS2 PFK3 YDR074W YD8554.07] Trehalose-phosphatase (EC 3.1.3.12) (Trehalose synthase complex catalytic subunit TPS2) (Trehalose-6-phosphate phosphatase) (TPP)
[Ppp1cc] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[suhB MJ0109] Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (FBPase/IMPase) (EC 3.1.3.11) (EC 3.1.3.25) (Inositol-1-phosphatase) (I-1-Pase)
[MJ0917] Bifunctional NADP phosphatase/NAD kinase [Includes: NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK); NADP phosphatase (NADPase) (pNPPase) (EC 3.1.3.-)]
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[ligD PA2138] Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase); DNA ligase D (LigD) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]); DNA repair polymerase (Pol) (Polymerase/primase)]
[arsC slr0946] Glutaredoxin arsenate reductase (EC 1.20.4.1) (Low molecular weight protein-tyrosine-phosphatase) (EC 3.1.3.48) (Protein ArsC) (SynArsC) (rSynArsC)

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