NPP1_YEAST
ID NPP1_YEAST Reviewed; 742 AA.
AC P25353; D6VR36; Q8NIL9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 1;
DE Short=E-NPP 1;
DE Includes:
DE RecName: Full=Alkaline phosphodiesterase 1;
DE EC=3.1.4.1 {ECO:0000305};
DE Includes:
DE RecName: Full=Nucleotide pyrophosphatase;
DE Short=NPPase;
DE EC=3.6.1.9 {ECO:0000305};
DE AltName: Full=Nucleotide diphosphatase {ECO:0000305};
GN Name=NPP1; OrderedLocusNames=YCR026C; ORFNames=YCR246, YCR26C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-742.
RX PubMed=1574926; DOI=10.1002/yea.320080306;
RA Bolle P.-A., Gilliquet V., Berben G., Dumont J., Hilger F.;
RT "The complete sequence of K3B, a 7.9 kb fragment between PGK1 and CRY1 on
RT chromosome III, reveals the presence of seven open reading frames.";
RL Yeast 8:205-213(1992).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, NPP ACTIVITY, INDUCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=16278456; DOI=10.1128/ec.4.11.1892-1901.2005;
RA Kennedy E.J., Pillus L., Ghosh G.;
RT "Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases
RT regulate extracellular nucleotide phosphate metabolism in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 4:1892-1901(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Mediates extracellular nucleotide derived phosphate
CC hydrolysis along with NPP2 and PHO5. {ECO:0000269|PubMed:16278456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated during phosphate starvation.
CC {ECO:0000269|PubMed:16278456}.
CC -!- PTM: Autophosphorylated as part of the catalytic cycle of
CC phosphodiesterase/pyrophosphatase activity.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 3420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; X59720; CAC42978.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07505.1; -; Genomic_DNA.
DR PIR; S19437; S19437.
DR PIR; S27380; S27380.
DR RefSeq; NP_009955.2; NM_001178741.1.
DR AlphaFoldDB; P25353; -.
DR SMR; P25353; -.
DR BioGRID; 31008; 71.
DR STRING; 4932.YCR026C; -.
DR iPTMnet; P25353; -.
DR MaxQB; P25353; -.
DR PaxDb; P25353; -.
DR PRIDE; P25353; -.
DR EnsemblFungi; YCR026C_mRNA; YCR026C; YCR026C.
DR GeneID; 850391; -.
DR KEGG; sce:YCR026C; -.
DR SGD; S000000621; NPP1.
DR VEuPathDB; FungiDB:YCR026C; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000167607; -.
DR HOGENOM; CLU_017594_3_1_1; -.
DR InParanoid; P25353; -.
DR OMA; NINEVYH; -.
DR BioCyc; YEAST:G3O-29341-MON; -.
DR Reactome; R-SCE-1660662; Glycosphingolipid metabolism.
DR Reactome; R-SCE-196843; Vitamin B2 (riboflavin) metabolism.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6814848; Glycerophospholipid catabolism.
DR PRO; PR:P25353; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25353; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IMP:SGD.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:SGD.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:SGD.
DR GO; GO:0009141; P:nucleoside triphosphate metabolic process; IMP:SGD.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Membrane; Multifunctional enzyme; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..742
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase 1"
FT /id="PRO_0000202566"
FT TOPO_DOM 1..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 168..545
FT /note="Phosphodiesterase"
FT REGION 640..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 742 AA; 84734 MW; 83BD5F00D69B09C5 CRC64;
MELQNDLESL DNELNDFSED PFRDDFITDE DAVRSGWRSA WTRMKYWFYK NRLKWTNNPI
VIGDAKDSRD GSNFRRGIPL YELDANGQPI DTELVDENEL SFGTGFHSKV PFKIIFRTLF
GSLVFAIFLI LMINIAKPHH STRVLSHFGS PEFDPYVKYF NGTHEFFPLT IVISLDGFHP
SLISKRNTPF LHDLYELKYD GGMNITSTPF MVPSFPTETF PNHWTLVTGQ YPIHHGIVSN
VFWDPDLNEE FHPGVLDPRI WNNNDTEPIW QTVQSAFDGD IPFKAATHMW PGSDVNYTKY
NEEKLQPEHK NPIARERTPF YFDEFNAKEP LSQKLSKIIE YVDMSTLNER PQLILGYVPN
VDAFGHKHGY PSESEYYYED FTETLGEVDT FLKQLVESLQ ERNLTSFTNL VIVSDHGMSD
IVVPSNVIIW EDLLDEKLRK DYVSHAYLEG PMMAISLKDS GNINEVYHNL KTSIDEDKYT
VYVNGNFPKE WNFNDGKNHH MASIWIVPEP GYAVMKKEQL KKVAKGDHKD KNEDNVFTIG
SHGYDNNAID MRSVFIGMGP YFPQGYIEPF QNTEIYNLLC DICGVAEKDR NSNDGTGMLM
NQLREPQSSE EVEIEDDFDY LVSKFGEFST YNIIWGGYPE ETEQDNVDND NDDNDDGNTD
EIAAMPSSSL TIKLEMTTSI PSATETLLGE TSPSSRSSSS SSIQASATAS TVGDWLQDII
NDAKDLIDDI IDSIDDLVDS DT
