Q9D020 (5NT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosolic 5'-nucleotidase 3
EC=3.1.3.5

Alternative name(s):
Cytosolic 5'-nucleotidase III
Short name=cN-III
Lupin
Pyrimidine 5'-nucleotidase 1
Short name=P5'N-1
Short name=P5N-1
Short name=PN-I

Gene names

Name:

Nt5c3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can act both as nucleotidase and as phosphotransferase By similarity.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Subunit structure	Monomer.
Subcellular location	Cytoplasm Potential.
Tissue specificity	Isoform 2 is highly expressed in the brain, heart, spleen, kidney and blood. Isoform 2 is expressed (at protein level) in the spleen, skeletal muscle and gastrointestinal epithelia.
Developmental stage	Isoform 2 is weakly expressed from E7.5 and the expression level steadily increased through gestation. At E9.5 and E10.5 is first detected colocalizing with embryonic blood cells within the region of the septum transversum and within the cardiac chambers and dorsal aorta. At E12.5 expression is found in the ventral neural tube and in the trigeminal ganglia and in the liver and dorsal root ganglia. Expression persisted in the liver, dorsal root and trigeminal ganglia at E13.5 and weaker expression becomes apparent in cardiac and skeletal muscle. At E16.5 expression is detected in liver, myocardium, tongue, bronchial epithelium, gastrointestinal epithelium, cartilage and forebrain neuroepithelium.
Sequence similarities	Belongs to the pyrimidine 5'-nucleotidase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay. Source: MGI
Molecular function	5'-nucleotidase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q9D020-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q9D020-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MDRAAVARVGAVASASVCAVVAGVVLAQYIFTLKRKTGRKTKIIE → MTNQESAVHLK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

Cytosolic 5'-nucleotidase 3

PRO_0000064388

Regions

Region

198 – 200

3

Substrate binding

Sites

Active site

83

1

Nucleophile

Active site

85

1

Proton donor

Metal binding

83

1

Magnesium

Metal binding

85

1

Magnesium; via carbonyl oxygen

Metal binding

272

1

Magnesium

Binding site

247

1

Substrate

Natural variations

Alternative sequence

1 – 45

45

MDRAA…TKIIE → MTNQESAVHLK in isoform 1.

VSP_021566

Experimental info

Sequence conflict

183

1

F → L in BAB27677. Ref.2

Sequence conflict

260

1

Q → R in BAB27901. Ref.2

Secondary structure

1

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331

Helix Strand Turn

Details...

Helix

48 – 51

4

Helix

60 – 73

14

Helix

75 – 77

3

Beta strand

78 – 82

5

Turn

85 – 87

3

Beta strand

91 – 93

3

Helix

101 – 106

6

Helix

113 – 130

18

Beta strand

133 – 135

3

Helix

137 – 158

22

Helix

162 – 164

3

Helix

165 – 171

7

Helix

180 – 190

11

Beta strand

194 – 201

8

Helix

202 – 211

10

Beta strand

219 – 224

6

Beta strand

226 – 228

3

Beta strand

232 – 237

6

Helix

247 – 252

6

Helix

255 – 260

6

Turn

261 – 263

3

Beta strand

266 – 274

9

Helix

275 – 278

4

Turn

279 – 282

4

Beta strand

287 – 295

9

Helix

299 – 309

11

Beta strand

310 – 315

6

Helix

321 – 330

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified November 14, 2006. Version 4. Checksum: 9BE4CA16863E1E0F	FASTA	331	37,252
	10 20 30 40 50 60 MDRAAVARVG AVASASVCAV VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF QKSSVRIKNP 70 80 90 100 110 120 TRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT CHNIIDNCKL VTDECRRKLL 130 140 150 160 170 180 QLKEQYYAIE VDPVLTVEEK FPYMVEWYTK SHGLLIEQGI PKAKLKEIVA DSDVMLKEGY 190 200 210 220 230 240 ENFFGKLQQH GIPVFIFSAG IGDVLEEVIR QAGVYHSNVK VVSNFMDFDE NGVLKGFKGE 250 260 270 280 290 300 LIHVFNKHDG ALKNTDYFSQ LKDNSNIILL GDSQGDLRMA DGVANVEHIL KIGYLNDRVD 310 320 330 ELLEKYMDSY DIVLVKEESL EVVNSILQKT L
	Isoform 1 [UniParc]. Checksum: 906B9D08934EEB2E	FASTA	297	33,790
	10 20 30 40 50 60 MTNQESAVHL KMMPEFQKSS VRIKNPTRVE EIICGLIKGG AAKLQIITDF DMTLSRFSYN 70 80 90 100 110 120 GKRCPTCHNI IDNCKLVTDE CRRKLLQLKE QYYAIEVDPV LTVEEKFPYM VEWYTKSHGL 130 140 150 160 170 180 LIEQGIPKAK LKEIVADSDV MLKEGYENFF GKLQQHGIPV FIFSAGIGDV LEEVIRQAGV 190 200 210 220 230 240 YHSNVKVVSN FMDFDENGVL KGFKGELIHV FNKHDGALKN TDYFSQLKDN SNIILLGDSQ 250 260 270 280 290 GDLRMADGVA NVEHILKIGY LNDRVDELLE KYMDSYDIVL VKEESLEVVN SILQKTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression analysis of murine lupin, a member of a novel gene family that is conserved through evolution and associated with Lupus inclusions." Lu M.M., Chen F., Gitler A., Li J., Jin F., Ma X.K., Epstein J.A. Dev. Genes Evol. 210:512-517(2000) [PubMed: 11180800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Embryo.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: Czech II. Tissue: Mammary gland.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 118-123, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning." Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr. J. Biol. Chem. 281:20521-20529(2006) [PubMed: 16672222] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) (ISOFORM 1) IN COMPLEXES WITH MAGNESIUM; PHOSPHATE; TRANSITION STATE ANALOG AND LEAD IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK011525 mRNA. Translation: BAB27677.2.
AK011894 mRNA. Translation: BAB27901.2.
BC038029 mRNA. Translation: AAH38029.1.

IPI

IPI00187512.
IPI00648235.

RefSeq

NP_001239303.1. NM_001252374.1.
NP_080280.3. NM_026004.3.

UniGene

Mm.158936.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BDU	X-ray	2.35	A/B	46-331	[»]
2G06	X-ray	2.25	A/B	46-331	[»]
2G07	X-ray	2.30	A/B	46-331	[»]
2G08	X-ray	2.35	A/B	46-331	[»]
2G09	X-ray	2.10	A/B	46-331	[»]
2G0A	X-ray	2.35	A/B	46-331	[»]
2Q4T	X-ray	2.35	A/B	46-331	[»]

ProteinModelPortal

Q9D020.

SMR

Q9D020. Positions 44-331.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9D020.

PTM databases

PhosphoSite

Q9D020.

Proteomic databases

PRIDE

Q9D020.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000031793; ENSMUSP00000031793; ENSMUSG00000029780.
ENSMUST00000101367; ENSMUSP00000098918; ENSMUSG00000029780.
ENSMUST00000116607; ENSMUSP00000112306; ENSMUSG00000029780.

GeneID

107569.

KEGG

mmu:107569.

UCSC

uc009cbq.2. mouse.
uc009cbr.2. mouse.

Organism-specific databases

CTD

51251.

MGI

MGI:1927186. Nt5c3.

Phylogenomic databases

eggNOG

roNOG11964.

GeneTree

ENSGT00390000012959.

HOGENOM

HBG382723.

HOVERGEN

HBG059750.

InParanoid

Q9D020.

OMA

NTEYFKQ.

OrthoDB

EOG4JWVDW.

PhylomeDB

Q9D020.

Gene expression databases

ArrayExpress

Q9D020.

Bgee

Q9D020.

CleanEx

MM_NT5C3.

Genevestigator

Q9D020.

GermOnline

ENSMUSG00000029780. Mus musculus.

Family and domain databases

InterPro

IPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]

Gene3D

G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.

KO

K01081.

PANTHER

PTHR13045. HAD-SF_hydro_IE. 1 hit.

Pfam

PF05822. UMPH-1. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01488. HAD-SF-IB. 1 hit.
TIGR01544. HAD-SF-IE. 1 hit.

ProtoNet

Search...

Other

NextBio

359058.

SOURCE

Search...

Entry information

Entry name

5NT3_MOUSE

Accession

Primary (citable) accession number: Q9D020
Secondary accession number(s): Q8CI05, Q9D0D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 86 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program