(data stored in ACNUC14238 zone)

HOGENOM: YEASTIII_PE102

ID   YEASTIII_PE102                       STANDARD;      PRT;   742 AA.
AC   YEASTIII_PE102; P25353; D6VR36; Q8NIL9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 1;
DE   Short=E-NPP 1;Includes: RecName: Full=Alkaline phosphodiesterase 1;
DE   EC=3.1.4.1;Includes: RecName: Full=Nucleotide pyrophosphatase;
DE   Short=NPPase; EC=3.6.1 9; (YEASTIII.PE102).
GN   Name=NPP1; OrderedLocusNames=YCR026C; ORFNames=YCR26C, YCR246;
OS   SACCHAROMYCES CEREVISIAE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YEASTIII.PE102.
CC       Saccharomyces cerevisiae chromosome III EF2 full sequence 1..316617
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NPP1_YEAST
CC   -!- FUNCTION: Mediates extracellular nucleotide derived phosphate
CC       hydrolysis along with NPP2 and PHO5.
CC   -!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
CC       successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
CC       oligonucleotides.
CC   -!- CATALYTIC ACTIVITY: A dinucleotide + H(2)O = 2 mononucleotides.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Potential).
CC   -!- INDUCTION: Up-regulated during phosphate starvation.
CC   -!- PTM: Autophosphorylated as part of the catalytic cycle of
CC       phosphodiesterase/pyrophosphatase activity.
CC   -!- PTM: N-glycosylated.
CC   -!- MISCELLANEOUS: Present with 3420 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the nucleotide
CC       pyrophosphatase/phosphodiesterase family.
CC   -!- GENE_FAMILY: HBG000000000 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Saccharomyces_cerevisiae;YCR026C;YCR026C;YCR026C.
DR   EMBL; X59720; - ;
DR   UniProtKB/Swiss-Prot; P25353; D6VR36; Q8NIL9; -.
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   SMR; P25353; 152-607.
DR   STRING; P25353; -.
DR   EnsemblFungi; YCR026C; YCR026C; YCR026C.
DR   GeneID; 850391; -.
DR   KEGG; sce:YCR026C; -.
DR   NMPDR; fig|4932.3.peg.680; -.
DR   CYGD; YCR026c; -.
DR   SGD; S000000621; NPP1.
DR   eggNOG; fuNOG07343; -.
DR   GeneTree; EFGT00050000006214; -.
DR   OMA; GNFPKEW; -.
DR   OrthoDB; EOG43246W; -.
DR   PhylomeDB; P25353; -.
DR   NextBio; 965909; -.
DR   ArrayExpress; P25353; -.
DR   Genevestigator; P25353; -.
DR   GermOnline; YCR026C; Saccharomyces cerevisiae.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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; IEA:EC.
DR   GO; GO:0004528; F:phosphodiesterase I activity; IEA:EC.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEP:SGD.
DR   GO; GO:0009141; P:nucleoside triphosphate metabolic process; IMP:SGD.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 2.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; Alkaline_phosphatase_core; 1.
DR   HOGENOMDNA; YEASTIII.PE102; -.
KW   YCR026C-A100026476820036002503210000011; YCR026C-A1; NPP1_YEAST; X59720;
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane;
KW   Multifunctional enzyme; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   742 AA;  UNKNOWN MW;  UNKNOWN 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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