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Protein

Cytosolic 5'-nucleotidase 3A

Gene

Nt5c3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m7GMP). CMP seems to be the preferred substrate.By similarity

Catalytic activityi

N(7)-methyl-GMP + H2O = N(7)-methyl-guanosine + phosphate.By similarity
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei83 – 831Nucleophile1 Publication
Metal bindingi83 – 831Magnesium1 Publication
Active sitei85 – 851Proton donor1 Publication
Metal bindingi85 – 851Magnesium; via carbonyl oxygen1 Publication
Binding sitei130 – 1301CMPBy similarity
Binding sitei130 – 1301N(7)-methyl-GMPBy similarity
Binding sitei151 – 1511N(7)-methyl-GMPBy similarity
Binding sitei247 – 2471Substrate1 Publication
Metal bindingi272 – 2721Magnesium1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-73621. Pyrimidine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic 5'-nucleotidase 3A1 Publication (EC:3.1.3.51 Publication)
Alternative name(s):
7-methylguanosine phosphate-specific 5'-nucleotidaseBy similarity (EC:3.1.3.91By similarity)
Short name:
7-methylguanosine nucleotidase
Cytosolic 5'-nucleotidase 3
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 namesi
Name:Nt5c3a
Synonyms:Nt5c3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1927186. Nt5c3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Cytosolic 5'-nucleotidase 3APRO_0000064388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D020.
MaxQBiQ9D020.
PaxDbiQ9D020.
PRIDEiQ9D020.

PTM databases

iPTMnetiQ9D020.
PhosphoSiteiQ9D020.

Expressioni

Tissue specificityi

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 stagei

Isoform 2 is weakly expressed from E7.5 and the expression level steadily increases 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 persists 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.

Gene expression databases

BgeeiQ9D020.
CleanExiMM_NT5C3.
ExpressionAtlasiQ9D020. baseline and differential.
GenevisibleiQ9D020. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiQ9D020. 1 interaction.
MINTiMINT-4126326.
STRINGi10090.ENSMUSP00000031793.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503Combined sources
Beta strandi55 – 584Combined sources
Helixi60 – 7718Combined sources
Beta strandi78 – 825Combined sources
Turni85 – 873Combined sources
Beta strandi91 – 933Combined sources
Helixi101 – 1066Combined sources
Helixi113 – 13119Combined sources
Beta strandi133 – 1353Combined sources
Helixi137 – 15721Combined sources
Helixi162 – 1643Combined sources
Helixi165 – 1706Combined sources
Helixi180 – 18910Combined sources
Beta strandi194 – 2018Combined sources
Helixi202 – 21110Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi232 – 2376Combined sources
Helixi247 – 2526Combined sources
Helixi255 – 2606Combined sources
Turni261 – 2633Combined sources
Beta strandi266 – 2738Combined sources
Helixi274 – 2785Combined sources
Turni279 – 2824Combined sources
Beta strandi287 – 2959Combined sources
Helixi299 – 30911Combined sources
Beta strandi310 – 3167Combined sources
Helixi321 – 33010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDUX-ray2.35A/B46-331[»]
2G06X-ray2.25A/B46-331[»]
2G07X-ray2.30A/B46-331[»]
2G08X-ray2.35A/B46-331[»]
2G09X-ray2.10A/B46-331[»]
2G0AX-ray2.35A/B46-331[»]
2Q4TX-ray2.35A/B46-331[»]
4FE3X-ray1.74A46-331[»]
4KX3X-ray2.10A46-331[»]
4KX5X-ray1.90A46-331[»]
ProteinModelPortaliQ9D020.
SMRiQ9D020. Positions 44-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D020.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2003Substrate binding1 Publication

Sequence similaritiesi

Belongs to the pyrimidine 5'-nucleotidase family.Curated

Phylogenomic databases

eggNOGiKOG3128. Eukaryota.
ENOG410ZQJ8. LUCA.
GeneTreeiENSGT00390000012959.
HOGENOMiHOG000244931.
HOVERGENiHBG059750.
InParanoidiQ9D020.
KOiK01081.
OMAiAGVYHSN.
OrthoDBiEOG7XSTHV.
PhylomeDBiQ9D020.
TreeFamiTF314663.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.
TIGR01544. HAD-SF-IE. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q9D020-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDRAAVARVG AVASASVCAV VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF
60 70 80 90 100
QKSSVRIKNP TRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT
110 120 130 140 150
CHNIIDNCKL VTDECRRKLL QLKEQYYAIE VDPVLTVEEK FPYMVEWYTK
160 170 180 190 200
SHGLLIEQGI PKAKLKEIVA DSDVMLKEGY ENFFGKLQQH GIPVFIFSAG
210 220 230 240 250
IGDVLEEVIR QAGVYHSNVK VVSNFMDFDE NGVLKGFKGE LIHVFNKHDG
260 270 280 290 300
ALKNTDYFSQ LKDNSNIILL GDSQGDLRMA DGVANVEHIL KIGYLNDRVD
310 320 330
ELLEKYMDSY DIVLVKEESL EVVNSILQKT L
Length:331
Mass (Da):37,252
Last modified:November 14, 2006 - v4
Checksum:i9BE4CA16863E1E0F
GO
Isoform 1 (identifier: Q9D020-1) [UniParc]FASTAAdd to basket

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

Show »
Length:297
Mass (Da):33,790
Checksum:i906B9D08934EEB2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831F → L in BAB27677 (PubMed:16141072).Curated
Sequence conflicti260 – 2601Q → R in BAB27901 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545MDRAA…TKIIE → MTNQESAVHLK in isoform 1. 1 PublicationVSP_021566Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011525 mRNA. Translation: BAB27677.2.
AK011894 mRNA. Translation: BAB27901.2.
BC038029 mRNA. Translation: AAH38029.1.
CCDSiCCDS20171.1. [Q9D020-3]
CCDS57424.1. [Q9D020-1]
RefSeqiNP_001239303.1. NM_001252374.1. [Q9D020-1]
NP_080280.3. NM_026004.3. [Q9D020-3]
XP_006505335.1. XM_006505272.1. [Q9D020-1]
XP_006505336.1. XM_006505273.1. [Q9D020-1]
XP_011239413.1. XM_011241111.1. [Q9D020-1]
UniGeneiMm.158936.
Mm.487949.

Genome annotation databases

EnsembliENSMUST00000031793; ENSMUSP00000031793; ENSMUSG00000029780. [Q9D020-3]
ENSMUST00000101367; ENSMUSP00000098918; ENSMUSG00000029780. [Q9D020-1]
GeneIDi107569.
KEGGimmu:107569.
UCSCiuc009cbq.3. mouse. [Q9D020-1]
uc009cbr.3. mouse. [Q9D020-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011525 mRNA. Translation: BAB27677.2.
AK011894 mRNA. Translation: BAB27901.2.
BC038029 mRNA. Translation: AAH38029.1.
CCDSiCCDS20171.1. [Q9D020-3]
CCDS57424.1. [Q9D020-1]
RefSeqiNP_001239303.1. NM_001252374.1. [Q9D020-1]
NP_080280.3. NM_026004.3. [Q9D020-3]
XP_006505335.1. XM_006505272.1. [Q9D020-1]
XP_006505336.1. XM_006505273.1. [Q9D020-1]
XP_011239413.1. XM_011241111.1. [Q9D020-1]
UniGeneiMm.158936.
Mm.487949.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDUX-ray2.35A/B46-331[»]
2G06X-ray2.25A/B46-331[»]
2G07X-ray2.30A/B46-331[»]
2G08X-ray2.35A/B46-331[»]
2G09X-ray2.10A/B46-331[»]
2G0AX-ray2.35A/B46-331[»]
2Q4TX-ray2.35A/B46-331[»]
4FE3X-ray1.74A46-331[»]
4KX3X-ray2.10A46-331[»]
4KX5X-ray1.90A46-331[»]
ProteinModelPortaliQ9D020.
SMRiQ9D020. Positions 44-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D020. 1 interaction.
MINTiMINT-4126326.
STRINGi10090.ENSMUSP00000031793.

PTM databases

iPTMnetiQ9D020.
PhosphoSiteiQ9D020.

Proteomic databases

EPDiQ9D020.
MaxQBiQ9D020.
PaxDbiQ9D020.
PRIDEiQ9D020.

Protocols and materials databases

DNASUi107569.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031793; ENSMUSP00000031793; ENSMUSG00000029780. [Q9D020-3]
ENSMUST00000101367; ENSMUSP00000098918; ENSMUSG00000029780. [Q9D020-1]
GeneIDi107569.
KEGGimmu:107569.
UCSCiuc009cbq.3. mouse. [Q9D020-1]
uc009cbr.3. mouse. [Q9D020-3]

Organism-specific databases

CTDi107569.
MGIiMGI:1927186. Nt5c3.

Phylogenomic databases

eggNOGiKOG3128. Eukaryota.
ENOG410ZQJ8. LUCA.
GeneTreeiENSGT00390000012959.
HOGENOMiHOG000244931.
HOVERGENiHBG059750.
InParanoidiQ9D020.
KOiK01081.
OMAiAGVYHSN.
OrthoDBiEOG7XSTHV.
PhylomeDBiQ9D020.
TreeFamiTF314663.

Enzyme and pathway databases

ReactomeiR-MMU-73621. Pyrimidine catabolism.

Miscellaneous databases

EvolutionaryTraceiQ9D020.
NextBioi359058.
PROiQ9D020.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D020.
CleanExiMM_NT5C3.
ExpressionAtlasiQ9D020. baseline and differential.
GenevisibleiQ9D020. MM.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.
TIGR01544. HAD-SF-IE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) (ISOFORM 1) IN COMPLEXES WITH MAGNESIUM; PHOSPHATE; TRANSITION STATE ANALOG AND LEAD IONS, CATALYTIC ACTIVITY, ACTIVE SITE, METAL BINDING.

Entry informationi

Entry namei5NT3A_MOUSE
AccessioniPrimary (citable) accession number: Q9D020
Secondary accession number(s): Q8CI05, Q9D0D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: November 14, 2006
Last modified: March 16, 2016
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.