(data stored in ACNUC14238 zone)

SWISSPROT: 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   05-JUL-2017, entry version 143.
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;
OC   Saccharomycetes; 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.,
RA   Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA   Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA   Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA   Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA   de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA   Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA   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.,
RA   Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA   Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA   Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA   Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA   Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA   van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA   Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA   Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
RT   on chromosome III, reveals the presence of seven open reading
RT   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.,
RA   Dephoure N., 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/
RT   phosphodiesterases regulate extracellular nucleotide phosphate
RT   metabolism in Saccharomyces 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
RT   reveals 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.
CC       {ECO:0000269|PubMed:16278456}.
CC   -!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
CC       successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
CC       oligonucleotides. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate. {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
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the nucleotide
CC       pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
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   ProteinModelPortal; P25353; -.
DR   BioGrid; 31008; 63.
DR   STRING; 4932.YCR026C; -.
DR   iPTMnet; P25353; -.
DR   MaxQB; P25353; -.
DR   PRIDE; P25353; -.
DR   EnsemblFungi; CAC42978; CAC42978; CAC42978.
DR   EnsemblFungi; YCR026C; YCR026C; YCR026C.
DR   GeneID; 850391; -.
DR   KEGG; sce:YCR026C; -.
DR   EuPathDB; FungiDB:YCR026C; -.
DR   SGD; S000000621; NPP1.
DR   GeneTree; ENSGT00760000119157; -.
DR   InParanoid; P25353; -.
DR   OMA; DGWPLFG; -.
DR   OrthoDB; EOG092C1GZ6; -.
DR   BioCyc; YEAST:G3O-29341-MONOMER; -.
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   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004551; F:nucleotide diphosphatase activity; ISS:SGD.
DR   GO; GO:0004528; F:phosphodiesterase I activity; ISS:SGD.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IMP:SGD.
DR   GO; GO:0009141; P:nucleoside triphosphate metabolic process; IMP:SGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:SGD.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P25353.
DR   SWISS-2DPAGE; P25353.
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane;
KW   Multifunctional enzyme; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    742       Ectonucleotide
FT                                pyrophosphatase/phosphodiesterase 1.
FT                                /FTId=PRO_0000202566.
FT   TOPO_DOM      1    113       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    114    134       Helical. {ECO:0000255}.
FT   TOPO_DOM    135    742       Extracellular. {ECO:0000255}.
FT   REGION      168    545       Phosphodiesterase.
FT   COMPBIAS    692    702       Poly-Ser.
FT   ACT_SITE    219    219       Nucleophile. {ECO:0000250}.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    264    264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    403    403       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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