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Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (Cytosolic 5'-nucleotidase II)

 5NTC_HUMAN              Reviewed;         561 AA.
P49902; B7Z382; D3DR91; Q5JUV5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 176.
RecName: Full=Cytosolic purine 5'-nucleotidase;
EC=3.1.3.5;
AltName: Full=Cytosolic 5'-nucleotidase II;
Name=NT5C2; Synonyms=NT5B, NT5CP, PNT5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=7999131; DOI=10.1006/bbrc.1994.2752;
Oka J., Matsumoto A., Hosokawa Y., Inoue S.;
"Molecular cloning of human cytosolic purine 5'-nucleotidase.";
Biochem. Biophys. Res. Commun. 205:917-922(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-3.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418 AND SER-511, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
INVOLVEMENT IN SPG45.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
[10]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH
ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, AND SUBUNIT.
PubMed=17405878; DOI=10.1074/jbc.M700917200;
Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S.,
Loppnau P., Bianchi V., Nordlund P.;
"Crystal structure of human cytosolic 5'-nucleotidase II: insights
into allosteric regulation and substrate recognition.";
J. Biol. Chem. 282:17828-17836(2007).
[11]
VARIANT SPG45 PRO-460.
PubMed=28884889; DOI=10.1002/ajmg.a.38414;
Straussberg R., Onoufriadis A., Konen O., Zouabi Y., Cohen L.,
Lee J.Y.W., Hsu C.K., Simpson M.A., McGrath J.A.;
"Novel homozygous missense mutation in NT5C2 underlying hereditary
spastic paraplegia SPG45.";
Am. J. Med. Genet. A 173:3109-3113(2017).
-!- FUNCTION: May have a critical role in the maintenance of a
constant composition of intracellular purine/pyrimidine
nucleotides in cooperation with other nucleotidases.
Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other
purine nucleotides.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043;
EC=3.1.3.5;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- ACTIVITY REGULATION: Allosterically activated by various
compounds, including ATP.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17405878}.
-!- INTERACTION:
P48047:ATP5PO; NbExp=3; IntAct=EBI-742084, EBI-355815;
P51116:FXR2; NbExp=3; IntAct=EBI-742084, EBI-740459;
Q7L9L4:MOB1B; NbExp=3; IntAct=EBI-742084, EBI-2558745;
Q86TA1:MOB3B; NbExp=3; IntAct=EBI-742084, EBI-751703;
Q70IA8:MOB3C; NbExp=3; IntAct=EBI-742084, EBI-9679267;
Q9Y5B8:NME7; NbExp=4; IntAct=EBI-742084, EBI-744782;
Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-742084, EBI-740486;
O00560:SDCBP; NbExp=3; IntAct=EBI-742084, EBI-727004;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49902-1; Sequence=Displayed;
Name=2;
IsoId=P49902-2; Sequence=VSP_054235;
Note=No experimental confirmation available.;
-!- DISEASE: Spastic paraplegia 45, autosomal recessive (SPG45)
[MIM:613162]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. Some SPG45 patients manifest mental retardation,
contractures and learning disability.
{ECO:0000269|PubMed:24482476, ECO:0000269|PubMed:28884889}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
{ECO:0000305}.
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EMBL; D38524; BAA07529.1; -; mRNA.
EMBL; AK295593; BAH12118.1; -; mRNA.
EMBL; AL139817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL360001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49656.1; -; Genomic_DNA.
EMBL; CH471066; EAW49657.1; -; Genomic_DNA.
EMBL; BC001595; AAH01595.1; -; mRNA.
CCDS; CCDS7544.1; -. [P49902-1]
PIR; JC2436; JC2436.
RefSeq; NP_001127845.1; NM_001134373.2. [P49902-1]
RefSeq; NP_036361.1; NM_012229.4. [P49902-1]
RefSeq; XP_005269693.1; XM_005269636.4.
RefSeq; XP_005269696.1; XM_005269639.4.
UniGene; Hs.734531; -.
UniGene; Hs.97439; -.
PDB; 2J2C; X-ray; 2.20 A; A=1-536.
PDB; 2JC9; X-ray; 1.50 A; A=1-536.
PDB; 2JCM; X-ray; 2.15 A; A=1-536.
PDB; 2XCV; X-ray; 2.30 A; A=1-536.
PDB; 2XCW; X-ray; 1.90 A; A=1-536.
PDB; 2XCX; X-ray; 2.30 A; A=1-536.
PDB; 2XJB; X-ray; 2.30 A; A=1-536.
PDB; 2XJC; X-ray; 2.00 A; A=1-536.
PDB; 2XJD; X-ray; 2.00 A; A=1-536.
PDB; 2XJE; X-ray; 2.30 A; A=1-536.
PDB; 2XJF; X-ray; 2.10 A; A=1-536.
PDB; 4H4B; X-ray; 2.90 A; A=1-536.
PDB; 5CQZ; X-ray; 2.90 A; A/B=1-536.
PDB; 5CR7; X-ray; 2.90 A; A/B=1-536.
PDB; 5K7Y; X-ray; 1.79 A; A=1-536.
PDB; 5L4Z; X-ray; 1.84 A; A=1-536.
PDB; 5L50; X-ray; 1.64 A; A=1-536.
PDB; 5OPK; X-ray; 1.74 A; A=3-488.
PDB; 5OPL; X-ray; 1.80 A; A=1-536.
PDB; 5OPM; X-ray; 1.68 A; A=3-488.
PDB; 5OPN; X-ray; 1.77 A; A=3-488.
PDB; 5OPO; X-ray; 2.00 A; A=3-488.
PDB; 5OPP; X-ray; 1.70 A; A=3-488.
PDB; 6DD3; X-ray; 1.98 A; A=1-536.
PDB; 6DDB; X-ray; 2.80 A; A/B=1-536.
PDB; 6DDC; X-ray; 2.91 A; A/B=1-536.
PDB; 6DDH; X-ray; 2.35 A; A=1-536.
PDB; 6DDK; X-ray; 2.50 A; A/B=1-561.
PDB; 6DDL; X-ray; 2.26 A; A/B=1-523.
PDB; 6DDO; X-ray; 2.48 A; A/B=1-561.
PDB; 6DDQ; X-ray; 2.31 A; A/B=1-561.
PDB; 6DDX; X-ray; 2.90 A; A=1-536.
PDB; 6DDY; X-ray; 1.80 A; A=1-536.
PDB; 6DDZ; X-ray; 1.97 A; A=1-536.
PDB; 6DE0; X-ray; 2.05 A; A=1-523.
PDB; 6DE1; X-ray; 2.15 A; A=1-561.
PDB; 6DE2; X-ray; 2.10 A; A=1-561.
PDB; 6DE3; X-ray; 3.06 A; A=1-561.
PDBsum; 2J2C; -.
PDBsum; 2JC9; -.
PDBsum; 2JCM; -.
PDBsum; 2XCV; -.
PDBsum; 2XCW; -.
PDBsum; 2XCX; -.
PDBsum; 2XJB; -.
PDBsum; 2XJC; -.
PDBsum; 2XJD; -.
PDBsum; 2XJE; -.
PDBsum; 2XJF; -.
PDBsum; 4H4B; -.
PDBsum; 5CQZ; -.
PDBsum; 5CR7; -.
PDBsum; 5K7Y; -.
PDBsum; 5L4Z; -.
PDBsum; 5L50; -.
PDBsum; 5OPK; -.
PDBsum; 5OPL; -.
PDBsum; 5OPM; -.
PDBsum; 5OPN; -.
PDBsum; 5OPO; -.
PDBsum; 5OPP; -.
PDBsum; 6DD3; -.
PDBsum; 6DDB; -.
PDBsum; 6DDC; -.
PDBsum; 6DDH; -.
PDBsum; 6DDK; -.
PDBsum; 6DDL; -.
PDBsum; 6DDO; -.
PDBsum; 6DDQ; -.
PDBsum; 6DDX; -.
PDBsum; 6DDY; -.
PDBsum; 6DDZ; -.
PDBsum; 6DE0; -.
PDBsum; 6DE1; -.
PDBsum; 6DE2; -.
PDBsum; 6DE3; -.
ProteinModelPortal; P49902; -.
SMR; P49902; -.
BioGrid; 116627; 35.
IntAct; P49902; 14.
MINT; P49902; -.
STRING; 9606.ENSP00000339479; -.
ChEMBL; CHEMBL3708197; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00811; Ribavirin.
DEPOD; P49902; -.
iPTMnet; P49902; -.
PhosphoSitePlus; P49902; -.
BioMuta; NT5C2; -.
DMDM; 1703012; -.
EPD; P49902; -.
MaxQB; P49902; -.
PaxDb; P49902; -.
PeptideAtlas; P49902; -.
PRIDE; P49902; -.
ProteomicsDB; 56174; -.
TopDownProteomics; P49902-1; -. [P49902-1]
DNASU; 22978; -.
Ensembl; ENST00000343289; ENSP00000339479; ENSG00000076685. [P49902-1]
Ensembl; ENST00000404739; ENSP00000383960; ENSG00000076685. [P49902-1]
GeneID; 22978; -.
KEGG; hsa:22978; -.
UCSC; uc001kwq.4; human. [P49902-1]
CTD; 22978; -.
DisGeNET; 22978; -.
EuPathDB; HostDB:ENSG00000076685.18; -.
GeneCards; NT5C2; -.
HGNC; HGNC:8022; NT5C2.
HPA; HPA003751; -.
MalaCards; NT5C2; -.
MIM; 600417; gene.
MIM; 613162; phenotype.
neXtProt; NX_P49902; -.
OpenTargets; ENSG00000076685; -.
Orphanet; 320396; Autosomal recessive spastic paraplegia type 45.
PharmGKB; PA31801; -.
eggNOG; KOG2469; Eukaryota.
eggNOG; ENOG410XQAV; LUCA.
GeneTree; ENSGT00940000162369; -.
HOGENOM; HOG000246075; -.
HOVERGEN; HBG000025; -.
KO; K01081; -.
OMA; ACLYTSR; -.
OrthoDB; EOG091G074N; -.
PhylomeDB; P49902; -.
TreeFam; TF315266; -.
BioCyc; MetaCyc:HS01216-MONOMER; -.
BRENDA; 3.1.3.5; 2681.
Reactome; R-HSA-2161541; Abacavir metabolism.
Reactome; R-HSA-74259; Purine catabolism.
SABIO-RK; P49902; -.
ChiTaRS; NT5C2; human.
EvolutionaryTrace; P49902; -.
GenomeRNAi; 22978; -.
PRO; PR:P49902; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000076685; Expressed in 233 organ(s), highest expression level in ectocervix.
CleanEx; HS_NT5C2; -.
ExpressionAtlas; P49902; baseline and differential.
Genevisible; P49902; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0008253; F:5'-nucleotidase activity; EXP:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050146; F:nucleoside phosphotransferase activity; TAS:Reactome.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0046085; P:adenosine metabolic process; IBA:GO_Central.
GO; GO:0017144; P:drug metabolic process; TAS:Reactome.
GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
InterPro; IPR023214; HAD_sf.
InterPro; IPR016695; Pur_nucleotidase.
PANTHER; PTHR12103; PTHR12103; 1.
Pfam; PF05761; 5_nucleotid; 1.
PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing;
Complete proteome; Cytoplasm; Disease mutation;
Hereditary spastic paraplegia; Hydrolase; Magnesium; Metal-binding;
Neurodegeneration; Nucleotide metabolism; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 561 Cytosolic purine 5'-nucleotidase.
/FTId=PRO_0000064389.
REGION 202 210 Substrate binding. {ECO:0000255}.
COMPBIAS 549 561 Asp/Glu-rich (acidic).
ACT_SITE 52 52 Nucleophile.
ACT_SITE 54 54 Proton donor.
METAL 52 52 Magnesium.
METAL 54 54 Magnesium; via carbonyl oxygen.
METAL 351 351 Magnesium.
BINDING 127 127 Allosteric activator 1.
BINDING 154 154 Allosteric activator 2.
BINDING 354 354 Allosteric activator 2.
BINDING 436 436 Allosteric activator 1; via carbonyl
oxygen.
BINDING 453 453 Allosteric activator 2.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:Q3V1L4}.
VAR_SEQ 1 34 MSTSWSDRLQNAADMPANMDKHALKKYRREAYHR -> MSK
EG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054235.
VARIANT 3 3 T -> A (in dbSNP:rs10883841).
{ECO:0000269|Ref.4}.
/FTId=VAR_024244.
VARIANT 136 136 Q -> R (in dbSNP:rs12262171).
/FTId=VAR_030242.
VARIANT 460 460 L -> P (in SPG45; unknown pathological
significance).
{ECO:0000269|PubMed:28884889}.
/FTId=VAR_079707.
HELIX 5 13 {ECO:0000244|PDB:2JC9}.
HELIX 21 28 {ECO:0000244|PDB:2JC9}.
HELIX 31 33 {ECO:0000244|PDB:2JC9}.
STRAND 36 39 {ECO:0000244|PDB:2JC9}.
HELIX 43 45 {ECO:0000244|PDB:2JC9}.
STRAND 48 51 {ECO:0000244|PDB:2JC9}.
TURN 55 57 {ECO:0000244|PDB:2JC9}.
STRAND 58 60 {ECO:0000244|PDB:6DE1}.
HELIX 64 79 {ECO:0000244|PDB:2JC9}.
HELIX 84 88 {ECO:0000244|PDB:2JC9}.
STRAND 101 103 {ECO:0000244|PDB:2JC9}.
TURN 104 107 {ECO:0000244|PDB:2JC9}.
STRAND 108 112 {ECO:0000244|PDB:2JC9}.
STRAND 117 123 {ECO:0000244|PDB:2JC9}.
STRAND 126 128 {ECO:0000244|PDB:5OPL}.
HELIX 130 136 {ECO:0000244|PDB:2JC9}.
HELIX 138 140 {ECO:0000244|PDB:6DDL}.
TURN 147 149 {ECO:0000244|PDB:2JC9}.
STRAND 150 152 {ECO:0000244|PDB:2JC9}.
HELIX 156 158 {ECO:0000244|PDB:2JC9}.
HELIX 159 174 {ECO:0000244|PDB:2JC9}.
STRAND 178 181 {ECO:0000244|PDB:2JC9}.
STRAND 184 187 {ECO:0000244|PDB:2JC9}.
STRAND 190 193 {ECO:0000244|PDB:2JC9}.
HELIX 194 210 {ECO:0000244|PDB:2JC9}.
HELIX 214 220 {ECO:0000244|PDB:2JC9}.
HELIX 222 225 {ECO:0000244|PDB:2JC9}.
HELIX 231 242 {ECO:0000244|PDB:2JC9}.
STRAND 243 248 {ECO:0000244|PDB:2JC9}.
HELIX 253 263 {ECO:0000244|PDB:2JC9}.
STRAND 266 271 {ECO:0000244|PDB:2JC9}.
HELIX 279 282 {ECO:0000244|PDB:2JC9}.
STRAND 284 289 {ECO:0000244|PDB:2JC9}.
HELIX 294 296 {ECO:0000244|PDB:2JC9}.
STRAND 302 306 {ECO:0000244|PDB:2JC9}.
TURN 307 310 {ECO:0000244|PDB:2JC9}.
STRAND 312 315 {ECO:0000244|PDB:6DDQ}.
HELIX 320 323 {ECO:0000244|PDB:6DDQ}.
STRAND 327 329 {ECO:0000244|PDB:2JC9}.
HELIX 332 339 {ECO:0000244|PDB:2JC9}.
HELIX 343 345 {ECO:0000244|PDB:2JC9}.
STRAND 346 351 {ECO:0000244|PDB:2JC9}.
HELIX 353 357 {ECO:0000244|PDB:2JC9}.
HELIX 358 364 {ECO:0000244|PDB:2JC9}.
STRAND 367 371 {ECO:0000244|PDB:2JC9}.
HELIX 375 384 {ECO:0000244|PDB:2JC9}.
HELIX 386 398 {ECO:0000244|PDB:2JC9}.
TURN 403 405 {ECO:0000244|PDB:6DDL}.
TURN 417 420 {ECO:0000244|PDB:5OPO}.
HELIX 421 432 {ECO:0000244|PDB:2JC9}.
STRAND 440 443 {ECO:0000244|PDB:2JC9}.
STRAND 446 448 {ECO:0000244|PDB:5OPN}.
HELIX 449 457 {ECO:0000244|PDB:2JC9}.
STRAND 459 463 {ECO:0000244|PDB:2JC9}.
HELIX 465 470 {ECO:0000244|PDB:2JC9}.
HELIX 485 487 {ECO:0000244|PDB:2JC9}.
HELIX 503 506 {ECO:0000244|PDB:6DDL}.
TURN 548 550 {ECO:0000244|PDB:6DDQ}.
SEQUENCE 561 AA; 64970 MW; 4C27D762575E0EA2 CRC64;
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA
PQEITHCHDE DDDEEEEEEE E


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