Primary Information |
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| BoMiProt ID | Bomi5009 |
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| Protein Name | Cytosolic purine 5'-nucleotidase/Cytosolic 5'-nucleotidase II/Cytosolic IMP/GMP-specific 5'-nucleotidase |
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| Organism | Bos taurus |
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| Uniprot ID | O46411 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776830.1 |
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| Aminoacid Length | 560 |
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| Molecular Weight | 64841 |
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| FASTA Sequence |
Download |
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| Gene Name | NT5C2 |
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| Gene ID | 281951 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | purine nucleotide degradation.dephosphorylation of the 5′-nucleoside monophosphates. |
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| Biochemical Properties | timulated by nucleoside triphosphates, among them ATP and GTP, and inhibited by Pi.Binds 1 Mg2+ ion per subunit |
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| PTMs | phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|O46411|5NTC_BOVIN Cytosolic purine 5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5C2 PE=1 SV=1
MTTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTVCDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISS*418IQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMES*502PLATRNRTS*511VDFKDTDYKRHQLTRS*527ISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEE
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| Predicted Disorder Regions | 544-560 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1.Allegrini S, Pesi R, Tozzi MG, Fiol CJ, Johnson RB, Eriksson S. Bovine cytosolic IMP/GMP-specific 5'-nucleotidase: cloning and expression of active enzyme in Escherichia coli. Biochem J. 1997 Dec 1;328 ( Pt 2)(Pt 2):483-7. doi: 10.1042/bj3280483. PMID: 9371705; PMCID: PMC1218945. 2.Van den Berghe G, Bontemps F, Vincent MF. Cytosolic purine 5'-nucleotidases of rat liver and human red blood cells: regulatory properties and role in AMP dephosphorylation. Adv Enzyme Regul. 1988;27:297-311. doi: 10.1016/0065-2571(88)90023-4. PMID: 2854949. |