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Purine nucleoside phosphorylase (PNP) (EC 2.4.2.1) (Inosine phosphorylase) (Inosine-guanosine phosphorylase)

 PNPH_MOUSE              Reviewed;         289 AA.
P23492; Q4FJT6;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Purine nucleoside phosphorylase;
Short=PNP;
EC=2.4.2.1;
AltName: Full=Inosine phosphorylase;
AltName: Full=Inosine-guanosine phosphorylase;
Name=Pnp; Synonyms=Np, Pnp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=1902950; DOI=10.1093/nar/19.7.1708;
Jenuth J.P., Snyder F.F.;
"Nucleotide sequence of murine purine nucleoside phosphorylase cDNA.";
Nucleic Acids Res. 19:1708-1708(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=1374046; DOI=10.1016/0378-1119(92)90398-9;
Nelson D.M., Foresman M.D., Ronnei B.J., McIvor R.S.;
"Isolation and expression of a murine purine nucleoside phosphorylase-
encoding cDNA and sequence similarity with the human message.";
Gene 113:215-221(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HEHA, MOLF/EiJ, and SPRET-1; TISSUE=Liver;
PubMed=7903568; DOI=10.1007/BF00361392;
Jenuth J.P., Mangat R.K., Snyder F.F.;
"cDNA sequence of four purine nucleoside phosphorylase (Np) alleles in
the mouse.";
Mamm. Genome 4:598-603(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland, and Mesenchymal cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 134-148, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: The purine nucleoside phosphorylases catalyze the
phosphorolytic breakdown of the N-glycosidic bond in the beta-
(deoxy)ribonucleoside molecules, with the formation of the
corresponding free purine bases and pentose-1-phosphate.
{ECO:0000269|PubMed:1902950}.
-!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine +
alpha-D-ribose 1-phosphate.
-!- PATHWAY: Purine metabolism; purine nucleoside salvage.
-!- SUBUNIT: Homotrimer.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
-!- POLYMORPHISM: Four electrophoretic alleles of NP are known; NPA
(shown here), NPB, NPC and NPD.
-!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
{ECO:0000305}.
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EMBL; X56548; CAA39888.1; -; mRNA.
EMBL; M84563; AAA39835.1; -; mRNA.
EMBL; L11290; AAC37634.1; -; mRNA.
EMBL; L11291; AAC37635.1; -; mRNA.
EMBL; L11292; AAC37706.1; -; mRNA.
EMBL; U35374; AAB60510.1; -; mRNA.
EMBL; CT010316; CAJ18524.1; -; mRNA.
EMBL; BC003788; AAH03788.1; -; mRNA.
EMBL; BC052679; AAH52679.1; -; mRNA.
CCDS; CCDS27029.1; -.
PIR; I57010; I57010.
PIR; I76672; I76672.
RefSeq; NP_038660.1; NM_013632.4.
UniGene; Mm.17932; -.
ProteinModelPortal; P23492; -.
SMR; P23492; -.
IntAct; P23492; 3.
MINT; MINT-1869537; -.
STRING; 10090.ENSMUSP00000043926; -.
BindingDB; P23492; -.
ChEMBL; CHEMBL2215; -.
iPTMnet; P23492; -.
PhosphoSitePlus; P23492; -.
SwissPalm; P23492; -.
EPD; P23492; -.
MaxQB; P23492; -.
PaxDb; P23492; -.
PeptideAtlas; P23492; -.
PRIDE; P23492; -.
DNASU; 18950; -.
GeneID; 18950; -.
KEGG; mmu:18950; -.
CTD; 4860; -.
MGI; MGI:97365; Pnp.
eggNOG; KOG3984; Eukaryota.
eggNOG; COG0005; LUCA.
HOGENOM; HOG000045183; -.
HOVERGEN; HBG002460; -.
InParanoid; P23492; -.
KO; K03783; -.
PhylomeDB; P23492; -.
UniPathway; UPA00606; -.
PRO; PR:P23492; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PNP1; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0001882; F:nucleoside binding; ISO:MGI.
GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
GO; GO:0002060; F:purine nucleobase binding; ISO:MGI.
GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:MGI.
GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:MGI.
GO; GO:0006161; P:deoxyguanosine catabolic process; IMP:MGI.
GO; GO:0006149; P:deoxyinosine catabolic process; IMP:MGI.
GO; GO:0046070; P:dGTP metabolic process; IMP:MGI.
GO; GO:0006183; P:GTP biosynthetic process; IMP:MGI.
GO; GO:0046115; P:guanosine catabolic process; IMP:MGI.
GO; GO:0006148; P:inosine catabolic process; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:MGI.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:MGI.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
GO; GO:0042278; P:purine nucleoside metabolic process; IDA:MGI.
GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
GO; GO:0034418; P:urate biosynthetic process; IMP:MGI.
InterPro; IPR000845; Nucleoside_phosphorylase_d.
InterPro; IPR035994; Nucleoside_phosphorylase_sf.
InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
InterPro; IPR011268; Purine_phosphorylase.
InterPro; IPR018099; Purine_phosphorylase-2_CS.
PANTHER; PTHR11904; PTHR11904; 1.
Pfam; PF01048; PNP_UDP_1; 1.
PIRSF; PIRSF000477; PurNPase; 1.
SUPFAM; SSF53167; SSF53167; 1.
TIGRFAMs; TIGR01700; PNPH; 1.
TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
PROSITE; PS01240; PNP_MTAP_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Glycosyltransferase; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 289 Purine nucleoside phosphorylase.
/FTId=PRO_0000184537.
REGION 84 86 Phosphate binding.
{ECO:0000250|UniProtKB:P55859}.
BINDING 33 33 Phosphate.
{ECO:0000250|UniProtKB:P55859}.
BINDING 64 64 Phosphate.
{ECO:0000250|UniProtKB:P55859}.
BINDING 116 116 Phosphate; via amide nitrogen.
{ECO:0000250|UniProtKB:P55859}.
BINDING 201 201 Purine nucleoside.
{ECO:0000250|UniProtKB:P55859}.
BINDING 220 220 Phosphate.
{ECO:0000250|UniProtKB:P55859}.
BINDING 243 243 Purine nucleoside.
{ECO:0000250|UniProtKB:P55859}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P00491}.
VARIANT 22 22 E -> K (in haplotype NPD).
VARIANT 39 39 T -> A (in haplotype NPD).
VARIANT 152 152 D -> E (in haplotype NPD).
VARIANT 176 176 T -> S (in haplotype NPB).
VARIANT 258 258 M -> K (in haplotype NPC).
SEQUENCE 289 AA; 32277 MW; DE7C1C2B004A1113 CRC64;
MENEFTYEDY ETTAKWLLQH TEYRPQVAVI CGSGLGGLTA HLKEAQIFDY NEIPNFPQST
VQGHAGRLVF GLLNGRCCVM MQGRFHMYEG YSLSKVTFPV RVFHLLGVET LVVTNAAGGL
NPNFEVGDIM LIRDHINLPG FCGQNPLRGP NDERFGVRFP AMSDAYDRDM RQKAFTAWKQ
MGEQRKLQEG TYVMLAGPNF ETVAESRLLK MLGADAVGMS TVPEVIVARH CGLRVFGFSL
ITNKVVMDYE NLEKANHMEV LDAGKAAAQT LERFVSILME SIPLPDRGS


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