5NT3B_MOUSE
ID 5NT3B_MOUSE Reviewed; 300 AA.
AC Q3UFY7; A2A4I2; A2A4I3; Q3TLP3; Q8BHU9; Q91WE8; Q9D9F9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000250|UniProtKB:Q9W197};
DE Short=7-methylguanosine nucleotidase;
DE EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9W197};
DE AltName: Full=Cytosolic 5'-nucleotidase 3B;
DE AltName: Full=Cytosolic 5'-nucleotidase III-like protein {ECO:0000250|UniProtKB:Q9W197};
DE Short=cN-III-like protein;
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9W197};
DE AltName: Full=N(7)-methylguanylate 5'-phosphatase;
GN Name=Nt5c3b; Synonyms=Nt5c3l;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-300 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate
CC (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific
CC activity for m(7)GMP may protect cells against undesired salvage of
CC m(7)GMP and its incorporation into nucleic acids. Also has weak
CC activity for CMP. UMP and purine nucleotides are poor substrates (By
CC similarity). {ECO:0000250}.
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:Q9W197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:29367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60377; EC=3.1.3.91;
CC Evidence={ECO:0000250|UniProtKB:Q9W197};
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:0000250|UniProtKB:Q9W197};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UFY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UFY7-2; Sequence=VSP_032853, VSP_032854;
CC Name=3;
CC IsoId=Q3UFY7-3; Sequence=VSP_032851, VSP_032852;
CC Name=4;
CC IsoId=Q3UFY7-4; Sequence=VSP_046298;
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24814.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC38632.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE37053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM23034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM23036.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK006972; BAB24814.1; ALT_FRAME; mRNA.
DR EMBL; AK082816; BAC38632.1; ALT_INIT; mRNA.
DR EMBL; AK148222; BAE28422.1; -; mRNA.
DR EMBL; AK162770; BAE37053.1; ALT_INIT; mRNA.
DR EMBL; AK166393; BAE38749.1; -; mRNA.
DR EMBL; AL590968; CAM23034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL590968; CAM23035.1; -; Genomic_DNA.
DR EMBL; AL590968; CAM23036.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC015307; AAH15307.1; ALT_INIT; mRNA.
DR CCDS; CCDS48930.1; -. [Q3UFY7-2]
DR CCDS; CCDS48931.1; -. [Q3UFY7-1]
DR CCDS; CCDS88254.1; -. [Q3UFY7-4]
DR RefSeq; NP_001096120.1; NM_001102650.1. [Q3UFY7-1]
DR RefSeq; NP_080837.3; NM_026561.4. [Q3UFY7-2]
DR RefSeq; XP_006534106.1; XM_006534043.3.
DR AlphaFoldDB; Q3UFY7; -.
DR SMR; Q3UFY7; -.
DR BioGRID; 212658; 8.
DR STRING; 10090.ENSMUSP00000090360; -.
DR PhosphoSitePlus; Q3UFY7; -.
DR EPD; Q3UFY7; -.
DR jPOST; Q3UFY7; -.
DR MaxQB; Q3UFY7; -.
DR PaxDb; Q3UFY7; -.
DR PeptideAtlas; Q3UFY7; -.
DR PRIDE; Q3UFY7; -.
DR ProteomicsDB; 296454; -. [Q3UFY7-1]
DR ProteomicsDB; 296455; -. [Q3UFY7-2]
DR ProteomicsDB; 296456; -. [Q3UFY7-3]
DR ProteomicsDB; 296457; -. [Q3UFY7-4]
DR Antibodypedia; 28986; 79 antibodies from 17 providers.
DR DNASU; 68106; -.
DR Ensembl; ENSMUST00000092688; ENSMUSP00000090360; ENSMUSG00000017176. [Q3UFY7-1]
DR Ensembl; ENSMUST00000107397; ENSMUSP00000103020; ENSMUSG00000017176. [Q3UFY7-4]
DR Ensembl; ENSMUST00000107398; ENSMUSP00000103021; ENSMUSG00000017176. [Q3UFY7-2]
DR Ensembl; ENSMUST00000107399; ENSMUSP00000103022; ENSMUSG00000017176. [Q3UFY7-2]
DR GeneID; 68106; -.
DR KEGG; mmu:68106; -.
DR UCSC; uc007llc.1; mouse. [Q3UFY7-2]
DR UCSC; uc007lld.2; mouse. [Q3UFY7-1]
DR UCSC; uc007llg.1; mouse. [Q3UFY7-3]
DR CTD; 115024; -.
DR MGI; MGI:1915356; Nt5c3b.
DR VEuPathDB; HostDB:ENSMUSG00000017176; -.
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR HOGENOM; CLU_048584_0_2_1; -.
DR InParanoid; Q3UFY7; -.
DR OMA; EIDPYRT; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q3UFY7; -.
DR TreeFam; TF314663; -.
DR Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
DR BioGRID-ORCS; 68106; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Nt5c3b; mouse.
DR PRO; PR:Q3UFY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UFY7; protein.
DR Bgee; ENSMUSG00000017176; Expressed in embryonic brain and 248 other tissues.
DR ExpressionAtlas; Q3UFY7; baseline and differential.
DR Genevisible; Q3UFY7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
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 Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..300
FT /note="7-methylguanosine phosphate-specific 5'-
FT nucleotidase"
FT /id="PRO_0000328949"
FT ACT_SITE 41
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT ACT_SITE 43
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 88
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 88
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 156..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q969T7"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046298"
FT VAR_SEQ 77..85
FT /note="LTELFHHYY -> CGETCNPRG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032851"
FT VAR_SEQ 86..300
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032852"
FT VAR_SEQ 257..261
FT /note="VEERR -> LPEAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032853"
FT VAR_SEQ 262..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032854"
FT CONFLICT 158
FT /note="G -> R (in Ref. 1; BAB24814)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="D -> H (in Ref. 1; BAB24814)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> H (in Ref. 1; BAB24814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 34425 MW; 9208C1438FBFD2A2 CRC64;
MAEEVSSLMK ATVLMRQPGR VQEIVGALRR GGGDRLQVIS DFDMTLSRFA YNGQRCPSSH
NILDNSKIIS EDCRKELTEL FHHYYPIEID PHRTIKEKLP HMVQWWSKAH SLLCQQRIQK
VQIAQVVGES TAMLREGYKT FFDTLYQNNI PLFIFSAGIG DILEEIIRQM KVFHPNIHIV
SNYMDFSEDG FLKGFKGQLI HTYNKNSSVC ENSSYFQQLQ NKTNIILLGD SIGDLTMADG
VPGVQNILKI GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLRHILY QGDCVELQGS
