5NT3A_MOUSE
ID 5NT3A_MOUSE Reviewed; 331 AA.
AC Q9D020; Q8CI05; Q9D0D9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytosolic 5'-nucleotidase 3A {ECO:0000305|PubMed:16672222};
DE EC=3.1.3.5 {ECO:0000269|PubMed:16672222};
DE AltName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000250|UniProtKB:Q9H0P0};
DE Short=7-methylguanosine nucleotidase;
DE EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9H0P0};
DE AltName: Full=Cytosolic 5'-nucleotidase 3;
DE AltName: Full=Cytosolic 5'-nucleotidase III;
DE Short=cN-III;
DE AltName: Full=Lupin;
DE AltName: Full=Pyrimidine 5'-nucleotidase 1;
DE Short=P5'N-1;
DE Short=P5N-1;
DE Short=PN-I;
GN Name=Nt5c3a; Synonyms=Nt5c3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11180800; DOI=10.1007/s004270050340;
RA Lu M.M., Chen F., Gitler A., Li J., Jin F., Ma X.K., Epstein J.A.;
RT "Cloning and expression analysis of murine lupin, a member of a novel gene
RT family that is conserved through evolution and associated with Lupus
RT inclusions.";
RL Dev. Genes Evol. 210:512-517(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 118-123, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) (ISOFORM 1) IN COMPLEXES WITH
RP MAGNESIUM; PHOSPHATE; TRANSITION STATE ANALOG AND LEAD IONS, CATALYTIC
RP ACTIVITY, ACTIVE SITE, AND METAL BINDING.
RX PubMed=16672222; DOI=10.1074/jbc.m602000200;
RA Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr.;
RT "Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of
RT action and inhibition during lead poisoning.";
RL J. Biol. Chem. 281:20521-20529(2006).
CC -!- FUNCTION: Nucleotidase which shows specific activity towards cytidine
CC monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP
CC seems to be the preferred substrate. {ECO:0000250|UniProtKB:Q9H0P0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(7)-methyl-GMP = N(7)-methylguanosine + phosphate;
CC Xref=Rhea:RHEA:37107, ChEBI:CHEBI:15377, ChEBI:CHEBI:20794,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58285; EC=3.1.3.91;
CC Evidence={ECO:0000250|UniProtKB:Q9H0P0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000269|PubMed:16672222};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9D020-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9D020-1; Sequence=VSP_021566;
CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in the brain, heart,
CC spleen, kidney and blood. Isoform 2 is expressed (at protein level) in
CC the spleen, skeletal muscle and gastrointestinal epithelia.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is weakly expressed from 7.5 dpc and the
CC expression level steadily increases through gestation. At 9.5 dpc and
CC 10.5 dpc is first detected colocalizing with embryonic blood cells
CC within the region of the septum transversum and within the cardiac
CC chambers and dorsal aorta. At 12.5 dpc expression is found in the
CC ventral neural tube and in the trigeminal ganglia and in the liver and
CC dorsal root ganglia. Expression persists in the liver, dorsal root and
CC trigeminal ganglia at 13.5 dpc and weaker expression becomes apparent
CC in cardiac and skeletal muscle. At 16.5 dpc expression is detected in
CC liver, myocardium, tongue, bronchial epithelium, gastrointestinal
CC epithelium, cartilage and forebrain neuroepithelium.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AK011525; BAB27677.2; -; mRNA.
DR EMBL; AK011894; BAB27901.2; -; mRNA.
DR EMBL; BC038029; AAH38029.1; -; mRNA.
DR CCDS; CCDS20171.1; -. [Q9D020-3]
DR CCDS; CCDS57424.1; -. [Q9D020-1]
DR RefSeq; NP_001239303.1; NM_001252374.1. [Q9D020-1]
DR RefSeq; NP_080280.3; NM_026004.3. [Q9D020-3]
DR RefSeq; XP_006505335.1; XM_006505272.1.
DR RefSeq; XP_006505336.1; XM_006505273.1. [Q9D020-1]
DR RefSeq; XP_011239413.1; XM_011241111.1. [Q9D020-1]
DR PDB; 2BDU; X-ray; 2.35 A; A/B=46-331.
DR PDB; 2G06; X-ray; 2.25 A; A/B=46-331.
DR PDB; 2G07; X-ray; 2.30 A; A/B=46-331.
DR PDB; 2G08; X-ray; 2.35 A; A/B=46-331.
DR PDB; 2G09; X-ray; 2.10 A; A/B=46-331.
DR PDB; 2G0A; X-ray; 2.35 A; A/B=46-331.
DR PDB; 2Q4T; X-ray; 2.35 A; A/B=46-331.
DR PDB; 4FE3; X-ray; 1.74 A; A=46-331.
DR PDB; 4KX3; X-ray; 2.10 A; A=46-331.
DR PDB; 4KX5; X-ray; 1.90 A; A=46-331.
DR PDBsum; 2BDU; -.
DR PDBsum; 2G06; -.
DR PDBsum; 2G07; -.
DR PDBsum; 2G08; -.
DR PDBsum; 2G09; -.
DR PDBsum; 2G0A; -.
DR PDBsum; 2Q4T; -.
DR PDBsum; 4FE3; -.
DR PDBsum; 4KX3; -.
DR PDBsum; 4KX5; -.
DR AlphaFoldDB; Q9D020; -.
DR SMR; Q9D020; -.
DR BioGRID; 223400; 1.
DR STRING; 10090.ENSMUSP00000031793; -.
DR iPTMnet; Q9D020; -.
DR PhosphoSitePlus; Q9D020; -.
DR jPOST; Q9D020; -.
DR MaxQB; Q9D020; -.
DR PaxDb; Q9D020; -.
DR PeptideAtlas; Q9D020; -.
DR PRIDE; Q9D020; -.
DR ProteomicsDB; 285574; -. [Q9D020-3]
DR ProteomicsDB; 285575; -. [Q9D020-1]
DR Antibodypedia; 26385; 187 antibodies from 27 providers.
DR DNASU; 107569; -.
DR Ensembl; ENSMUST00000031793; ENSMUSP00000031793; ENSMUSG00000029780. [Q9D020-3]
DR Ensembl; ENSMUST00000101367; ENSMUSP00000098918; ENSMUSG00000029780. [Q9D020-1]
DR GeneID; 107569; -.
DR KEGG; mmu:107569; -.
DR UCSC; uc009cbq.3; mouse. [Q9D020-1]
DR UCSC; uc009cbr.3; mouse. [Q9D020-3]
DR CTD; 107569; -.
DR MGI; MGI:1927186; Nt5c3.
DR VEuPathDB; HostDB:ENSMUSG00000029780; -.
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR HOGENOM; CLU_048584_0_2_1; -.
DR InParanoid; Q9D020; -.
DR OMA; GPERMQI; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q9D020; -.
DR TreeFam; TF314663; -.
DR BRENDA; 3.1.3.5; 3474.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR BioGRID-ORCS; 107569; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Nt5c3; mouse.
DR EvolutionaryTrace; Q9D020; -.
DR PRO; PR:Q9D020; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D020; protein.
DR Bgee; ENSMUSG00000029780; Expressed in blood and 269 other tissues.
DR ExpressionAtlas; Q9D020; baseline and differential.
DR Genevisible; Q9D020; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046085; P:adenosine metabolic process; ISO:MGI.
DR GO; GO:0006248; P:CMP catabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0046074; P:dTMP catabolic process; ISO:MGI.
DR GO; GO:0046079; P:dUMP catabolic process; ISO:MGI.
DR GO; GO:0046050; P:UMP catabolic process; ISO:MGI.
DR CDD; cd07504; HAD_5NT; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR Pfam; PF05822; UMPH-1; 1.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Cytosolic 5'-nucleotidase 3A"
FT /id="PRO_0000064388"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16672222"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16672222"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16672222"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16672222"
FT BINDING 130
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 130
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 151
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16672222"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16672222"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16672222"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..45
FT /note="MDRAAVARVGAVASASVCAVVAGVVLAQYIFTLKRKTGRKTKIIE -> MTN
FT QESAVHLK (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021566"
FT CONFLICT 183
FT /note="F -> L (in Ref. 2; BAB27677)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="Q -> R (in Ref. 2; BAB27901)"
FT /evidence="ECO:0000305"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4KX5"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2Q4T"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4FE3"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 113..131
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 137..157
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:4FE3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:4FE3"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:4FE3"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:4FE3"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:4FE3"
SQ SEQUENCE 331 AA; 37252 MW; 9BE4CA16863E1E0F CRC64;
MDRAAVARVG AVASASVCAV VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF QKSSVRIKNP
TRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT CHNIIDNCKL VTDECRRKLL
QLKEQYYAIE VDPVLTVEEK FPYMVEWYTK SHGLLIEQGI PKAKLKEIVA DSDVMLKEGY
ENFFGKLQQH GIPVFIFSAG IGDVLEEVIR QAGVYHSNVK VVSNFMDFDE NGVLKGFKGE
LIHVFNKHDG ALKNTDYFSQ LKDNSNIILL GDSQGDLRMA DGVANVEHIL KIGYLNDRVD
ELLEKYMDSY DIVLVKEESL EVVNSILQKT L
