NPP2_YEAST
ID NPP2_YEAST Reviewed; 493 AA.
AC P39997; D3DLN4; Q6B2P3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 2;
DE Short=E-NPP 2;
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=NPP2; OrderedLocusNames=YEL016C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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).
CC -!- FUNCTION: Mediates extracellular nucleotide derived phosphate
CC hydrolysis along with NPP1 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 -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; U18530; AAB64493.1; -; Genomic_DNA.
DR EMBL; AY692687; AAT92706.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07638.1; -; Genomic_DNA.
DR PIR; S50443; S50443.
DR RefSeq; NP_010900.1; NM_001178831.1.
DR AlphaFoldDB; P39997; -.
DR SMR; P39997; -.
DR BioGRID; 36715; 48.
DR DIP; DIP-5279N; -.
DR IntAct; P39997; 3.
DR MINT; P39997; -.
DR STRING; 4932.YEL016C; -.
DR PaxDb; P39997; -.
DR PRIDE; P39997; -.
DR EnsemblFungi; YEL016C_mRNA; YEL016C; YEL016C.
DR GeneID; 856699; -.
DR KEGG; sce:YEL016C; -.
DR SGD; S000000742; NPP2.
DR VEuPathDB; FungiDB:YEL016C; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000167607; -.
DR HOGENOM; CLU_017594_3_0_1; -.
DR InParanoid; P39997; -.
DR OMA; KEAWQNG; -.
DR BioCyc; YEAST:G3O-30141-MON; -.
DR Reactome; R-SCE-1660662; Glycosphingolipid metabolism.
DR Reactome; R-SCE-196843; Vitamin B2 (riboflavin) metabolism.
DR Reactome; R-SCE-6814848; Glycerophospholipid catabolism.
DR PRO; PR:P39997; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39997; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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: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..493
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase 2"
FT /id="PRO_0000202612"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 76..438
FT /note="Phosphodiesterase"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 125
FT /note="T -> I (in Ref. 3; AAT92706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 57355 MW; 10E67A05C6DEDF09 CRC64;
MLLFEQPVDL EKNNEDDTNI KPFAISRHFL LKLLLCGIIL IELLLYSKCP KPIDNGPRTI
ANRSNTYFNG THDFKTLTIL ISIDGFHPRL IDAKYTPFLY NLHNLRSPYD MNITTAPYMI
PSFPTQTFPN HWSMVTGKYP IEHGIVSNIF WDNFTSSEFR PNNLDARIWS NTADPIWQLL
QTESQGEYKV ATHMWPGSEV VYEDHGDVPR ERMPFYFGKF NQWEKLQDKL AQIFRYIDMP
QLKDRPELVI SYIPNVDSYG HSFGYDLRDK RLQKLIGEVD GFFLDLIEGL QKRNLLKISN
VMIVSDHGMS NVNANDGEHV VVWERVFPAD AMSAFISHLY NEGPMMMVCL KNPRDKQWIC
DLIEAQLEKA YGDEISRKFH VILKEDFDPS WKYFQYDNRK HRYDDRVGDI WILADEYYAI
VKEMGDVPIG IMGTHGYNFN NCSDMASIFI GMGPMFNNEV VPPFENIEVY NMLIKASALL
GEEKTKKEKS LLQ
