Q5RA22 (5NTC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosolic purine 5'-nucleotidase
EC=3.1.3.5

Alternative name(s):
Cytosolic 5'-nucleotidase II

Gene names

Name:

NT5C2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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 By similarity.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	Allosterically activated by various compounds, including ATP By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the 5'(3')-deoxyribonucleotidase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 561	561	Cytosolic purine 5'-nucleotidase		PRO_0000310265
Regions
	Region	202 – 210	9	Substrate binding Potential
	Compositional bias	549 – 561	13	Asp/Glu-rich (acidic)
Sites
	Active site	52	1	Nucleophile By similarity
	Active site	54	1	Proton donor By similarity
	Metal binding	52	1	Magnesium By similarity
	Metal binding	54	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	351	1	Magnesium By similarity
	Binding site	127	1	Allosteric activator 1 By similarity
	Binding site	154	1	Allosteric activator 2 By similarity
	Binding site	354	1	Allosteric activator 2 By similarity
	Binding site	436	1	Allosteric activator 1; via carbonyl oxygen By similarity
	Binding site	453	1	Allosteric activator 2 By similarity
Amino acid modifications
	Modified residue	502	1	Phosphoserine By similarity
	Modified residue	527	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RA22 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 4C27D762575E0EA2	FASTA	561	64,970
	10 20 30 40 50 60 MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 70 80 90 100 110 120 KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV 130 140 150 160 170 180 CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS 190 200 210 220 230 240 CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK 250 260 270 280 290 300 EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 310 320 330 340 350 360 VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS 370 380 390 400 410 420 KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ 430 440 450 460 470 480 RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA 490 500 510 520 530 540 HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA 550 560 PQEITHCHDE DDDEEEEEEE E

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR859201 mRNA. Translation: CAH91388.1.
RefSeq	NP_001125821.1. NM_001132349.1.
UniGene	Pab.19052.
3D structure databases
HSSP	HSSP built from PDB template 2BDE based on UniProtKB Q5ZZB6.
ProteinModelPortal	Q5RA22.
SMR	Q5RA22. Positions 3-488.
ModBase	Search...
Proteomic databases
PRIDE	Q5RA22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPPYT00000003149; ENSPPYP00000003045; ENSPPYG00000002616.
GeneID	100172749.
KEGG	pon:100172749.
Organism-specific databases
CTD	22978.
Phylogenomic databases
HOVERGEN	HBG000025.
InParanoid	Q5RA22.
OMA	WERVFRA.
Family and domain databases
InterPro	IPR023214. HAD-like_dom. IPR008380. HAD-SF_hydro_IG_5-nucl. IPR016695. Pur_nucleotidase. [Graphical view]
KO	K01081.
PANTHER	PTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.
Pfam	PF05761. 5_nucleotid. 1 hit. [Graphical view]
PIRSF	PIRSF017434. Purine_5'-nucleotidase. 1 hit.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNet	Search...

Entry information

Entry name

5NTC_PONAB

Accession

Primary (citable) accession number: Q5RA22

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	December 21, 2004
Last modified:	November 16, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program