DS1P2_YEAST
ID DS1P2_YEAST Reviewed; 404 AA.
AC P23501; D6VXB4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dihydrosphingosine 1-phosphate phosphatase YSR3 {ECO:0000303|PubMed:9353337};
DE EC=3.1.3.- {ECO:0000269|PubMed:25345524};
DE AltName: Full=Long-chain base protein 2 {ECO:0000303|PubMed:9419344};
DE AltName: Full=Sphingolipid resistance protein 3 {ECO:0000303|PubMed:9353337};
GN Name=YSR3 {ECO:0000303|PubMed:9353337};
GN Synonyms=LBP2 {ECO:0000303|PubMed:9419344}; OrderedLocusNames=YKR053C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 197-404.
RC STRAIN=M1301;
RX PubMed=1703236; DOI=10.1016/0022-2836(91)90608-9;
RA Wiesenberger G., Link T.A., von Ahsen U., Waldherr M., Schweyen R.J.;
RT "MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast, are new
RT members of the mitochondrial carrier family.";
RL J. Mol. Biol. 217:23-37(1991).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9353337; DOI=10.1074/jbc.272.45.28690;
RA Mao C., Wadleigh M., Jenkins G.M., Hannun Y.A., Obeid L.M.;
RT "Identification and characterization of Saccharomyces cerevisiae
RT dihydrosphingosine-1-phosphate phosphatase.";
RL J. Biol. Chem. 272:28690-28694(1997).
RN [5]
RP FUNCTION.
RX PubMed=9419344; DOI=10.1073/pnas.95.1.150;
RA Mandala S.M., Thornton R., Tu Z., Kurtz M.B., Nickels J., Broach J.,
RA Menzeleev R., Spiegel S.;
RT "Sphingoid base 1-phosphate phosphatase: a key regulator of sphingolipid
RT metabolism and stress response.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:150-155(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10477278; DOI=10.1042/bj3420667;
RA Mao C., Saba J.D., Obeid L.M.;
RT "The dihydrosphingosine-1-phosphate phosphatases of Saccharomyces
RT cerevisiae are important regulators of cell proliferation and heat stress
RT responses.";
RL Biochem. J. 342:667-675(1999).
RN [7]
RP FUNCTION.
RX PubMed=10856228; DOI=10.1093/emboj/19.12.2824;
RA Zanolari B., Friant S., Funato K., Suetterlin C., Stevenson B.J.,
RA Riezman H.;
RT "Sphingoid base synthesis requirement for endocytosis in Saccharomyces
RT cerevisiae.";
RL EMBO J. 19:2824-2833(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10563329; DOI=10.1016/s0076-6879(00)11085-7;
RA Mao C., Obeid L.M.;
RT "Yeast sphingosine-1-phosphate phosphatases: assay, expression, deletion,
RT purification, and cellular localization by GFP tagging.";
RL Methods Enzymol. 311:223-232(2000).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25345524; DOI=10.1038/ncomms6338;
RA Kondo N., Ohno Y., Yamagata M., Obara T., Seki N., Kitamura T.,
RA Naganuma T., Kihara A.;
RT "Identification of the phytosphingosine metabolic pathway leading to odd-
RT numbered fatty acids.";
RL Nat. Commun. 5:5338-5338(2014).
CC -!- FUNCTION: Dihydrosphingosine 1-phosphate phosphatase required for
CC efficient ceramide synthesis from exogenous sphingoid bases
CC (PubMed:10477278, PubMed:10563329, PubMed:10856228, PubMed:9353337,
CC PubMed:9419344). Involved in endocytosis and calcium-mediated signaling
CC (PubMed:10856228). {ECO:0000269|PubMed:10477278,
CC ECO:0000269|PubMed:10563329, ECO:0000269|PubMed:10856228,
CC ECO:0000269|PubMed:9353337, ECO:0000269|PubMed:9419344}.
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:25345524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27515;
CC Evidence={ECO:0000269|PubMed:25345524};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329,
CC ECO:0000269|PubMed:9353337}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329,
CC ECO:0000269|PubMed:9353337}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000305}.
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DR EMBL; Z28278; CAA82131.1; -; Genomic_DNA.
DR EMBL; X56444; CAA39827.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09204.1; -; Genomic_DNA.
DR PIR; S38127; S38127.
DR RefSeq; NP_012979.3; NM_001179843.3.
DR AlphaFoldDB; P23501; -.
DR BioGRID; 34184; 138.
DR DIP; DIP-5258N; -.
DR IntAct; P23501; 1.
DR STRING; 4932.YKR053C; -.
DR SwissLipids; SLP:000000933; -.
DR PaxDb; P23501; -.
DR PRIDE; P23501; -.
DR EnsemblFungi; YKR053C_mRNA; YKR053C; YKR053C.
DR GeneID; 853927; -.
DR KEGG; sce:YKR053C; -.
DR SGD; S000001761; YSR3.
DR VEuPathDB; FungiDB:YKR053C; -.
DR eggNOG; KOG2822; Eukaryota.
DR GeneTree; ENSGT00660000096503; -.
DR HOGENOM; CLU_019266_1_1_1; -.
DR InParanoid; P23501; -.
DR OMA; WVLVMYV; -.
DR BioCyc; MetaCyc:YKR053C-MON; -.
DR BioCyc; YEAST:YKR053C-MON; -.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:P23501; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P23501; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
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:0070780; F:dihydrosphingosine-1-phosphate phosphatase activity; IEA:RHEA.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:SGD.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="Dihydrosphingosine 1-phosphate phosphatase YSR3"
FT /id="PRO_0000203216"
FT TOPO_DOM 1..86
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 87..107
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 114..134
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..154
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 155..176
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 183..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..215
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..319
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 320..340
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT TRANSMEM 380..400
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..404
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P47013"
FT REGION 129..137
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 158..161
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 204..215
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 215
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
