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Dihydrosphingosine 1-phosphate phosphatase YSR3 (EC 3.1.3.-) (Long-chain base protein 2) (Sphingolipid resistance protein 3)

 DS1P2_YEAST             Reviewed;         404 AA.
P23501; D6VXB4;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
12-SEP-2018, entry version 136.
RecName: Full=Dihydrosphingosine 1-phosphate phosphatase YSR3;
EC=3.1.3.-;
AltName: Full=Long-chain base protein 2;
AltName: Full=Sphingolipid resistance protein 3;
Name=YSR3; Synonyms=LBP2; OrderedLocusNames=YKR053C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 197-404.
STRAIN=M1301;
PubMed=1703236; DOI=10.1016/0022-2836(91)90608-9;
Wiesenberger G., Link T.A., von Ahsen U., Waldherr M., Schweyen R.J.;
"MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast,
are new members of the mitochondrial carrier family.";
J. Mol. Biol. 217:23-37(1991).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9353337; DOI=10.1074/jbc.272.45.28690;
Mao C., Wadleigh M., Jenkins G.M., Hannun Y.A., Obeid L.M.;
"Identification and characterization of Saccharomyces cerevisiae
dihydrosphingosine-1-phosphate phosphatase.";
J. Biol. Chem. 272:28690-28694(1997).
[5]
FUNCTION.
PubMed=9419344; DOI=10.1073/pnas.95.1.150;
Mandala S.M., Thornton R., Tu Z., Kurtz M.B., Nickels J., Broach J.,
Menzeleev R., Spiegel S.;
"Sphingoid base 1-phosphate phosphatase: a key regulator of
sphingolipid metabolism and stress response.";
Proc. Natl. Acad. Sci. U.S.A. 95:150-155(1998).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10477278; DOI=10.1042/bj3420667;
Mao C., Saba J.D., Obeid L.M.;
"The dihydrosphingosine-1-phosphate phosphatases of Saccharomyces
cerevisiae are important regulators of cell proliferation and heat
stress responses.";
Biochem. J. 342:667-675(1999).
[7]
FUNCTION.
PubMed=10856228; DOI=10.1093/emboj/19.12.2824;
Zanolari B., Friant S., Funato K., Suetterlin C., Stevenson B.J.,
Riezman H.;
"Sphingoid base synthesis requirement for endocytosis in Saccharomyces
cerevisiae.";
EMBO J. 19:2824-2833(2000).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10563329; DOI=10.1016/S0076-6879(00)11085-7;
Mao C., Obeid L.M.;
"Yeast sphingosine-1-phosphate phosphatases: assay, expression,
deletion, purification, and cellular localization by GFP tagging.";
Methods Enzymol. 311:223-232(2000).
-!- FUNCTION: Dihydrosphingosine 1-phosphate phosphatase required for
efficient ceramide synthesis from exogenous sphingoid bases.
Involved in endocytosis and calcium-mediated signaling.
{ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329,
ECO:0000269|PubMed:10856228, ECO:0000269|PubMed:9353337,
ECO:0000269|PubMed:9419344}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329,
ECO:0000269|PubMed:9353337}; Multi-pass membrane protein
{ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329,
ECO:0000269|PubMed:9353337}.
-!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Z28278; CAA82131.1; -; Genomic_DNA.
EMBL; X56444; CAA39827.1; -; Genomic_DNA.
EMBL; BK006944; DAA09204.1; -; Genomic_DNA.
PIR; S38127; S38127.
RefSeq; NP_012979.3; NM_001179843.3.
ProteinModelPortal; P23501; -.
BioGrid; 34184; 138.
DIP; DIP-5258N; -.
IntAct; P23501; 1.
STRING; 4932.YKR053C; -.
SwissLipids; SLP:000000933; -.
PaxDb; P23501; -.
PRIDE; P23501; -.
EnsemblFungi; YKR053C; YKR053C; YKR053C.
GeneID; 853927; -.
KEGG; sce:YKR053C; -.
EuPathDB; FungiDB:YKR053C; -.
SGD; S000001761; YSR3.
GeneTree; ENSGT00390000017322; -.
HOGENOM; HOG000066080; -.
InParanoid; P23501; -.
KO; K04717; -.
OMA; YKFVTYS; -.
OrthoDB; EOG092C3MDD; -.
BioCyc; MetaCyc:YKR053C-MONOMER; -.
BioCyc; YEAST:YKR053C-MONOMER; -.
Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
PRO; PR:P23501; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:SGD.
GO; GO:0046839; P:phospholipid dephosphorylation; IDA:SGD.
GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
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.
3: Inferred from homology;
Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Lipid metabolism; Membrane; Reference proteome;
Sphingolipid metabolism; Transmembrane; Transmembrane helix.
CHAIN 1 404 Dihydrosphingosine 1-phosphate
phosphatase YSR3.
/FTId=PRO_0000203216.
TOPO_DOM 1 86 Lumenal. {ECO:0000250|UniProtKB:P47013}.
TRANSMEM 87 107 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 108 113 Cytoplasmic.
{ECO:0000250|UniProtKB:P47013}.
TRANSMEM 114 134 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 135 154 Lumenal. {ECO:0000250|UniProtKB:P47013}.
TRANSMEM 155 176 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 177 182 Cytoplasmic.
{ECO:0000250|UniProtKB:P47013}.
TRANSMEM 183 203 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 204 215 Lumenal. {ECO:0000250|UniProtKB:P47013}.
TRANSMEM 216 236 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 237 241 Cytoplasmic.
{ECO:0000250|UniProtKB:P47013}.
TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 263 319 Lumenal. {ECO:0000250|UniProtKB:P47013}.
TRANSMEM 320 340 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 341 379 Cytoplasmic.
{ECO:0000250|UniProtKB:P47013}.
TRANSMEM 380 400 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 401 404 Lumenal. {ECO:0000250|UniProtKB:P47013}.
REGION 129 137 Phosphatase sequence motif I.
{ECO:0000305}.
REGION 158 161 Phosphatase sequence motif II.
{ECO:0000305}.
REGION 204 215 Phosphatase sequence motif III.
{ECO:0000305}.
ACT_SITE 161 161 Proton donor.
{ECO:0000250|UniProtKB:P0A924}.
ACT_SITE 211 211 Nucleophile.
{ECO:0000250|UniProtKB:P0A924}.
SITE 215 215 Stabilizes the active site histidine for
nucleophilic attack.
{ECO:0000250|UniProtKB:P0A924}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 404 AA; 46488 MW; 0CDB272FBF868BF8 CRC64;
MTIIQTVTEL GVTEDTIKVQ MAPSGGKHLL ADPGNHPAEH FESQMSWLRF QTRQYLTRFT
DNQSDFVHSL QKKHRTPFRD VYFKYTSLMG SHMFYVIVLP MPVWLGYRDL TRDMIYVLGY
SIYLSGYLKD YWCLPRPKSP PVDRITLSEY TTKEYGAPSS HSANATAVSL LFFWRICLSD
TLVWPTKLLL LSLVIFYYLT LVFGRVYCGM HGMLDLFSGA AVGAICFFIR IWVVHALRNF
QIGEHLWFPL LSVAWGLFIL FNHVRPIDEC PCFEDSVAFI GVVSGLDCSD WLTERYGWNL
VCSRYASCGS KVFLRPLVGV ASVIVWKDVI SKTAVYTLLI KLLRFHDDRS EKVHFHNETS
EEEECLLYSG VSKVEIVGRF LIYAGIPTTV FLLCPVFFTW TNLR


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