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7-methylguanosine phosphate-specific 5'-nucleotidase (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3B) (Cytosolic 5'-nucleotidase III-like protein) (cN-III-like protein) (EC 3.1.3.5) (N(7)-methylguanylate 5'-phosphatase)

 5NT3B_HUMAN             Reviewed;         300 AA.
Q969T7; A8MWB9; C9JKC4; Q7L3B7;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 4.
05-DEC-2018, entry version 140.
RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000305|PubMed:23223233};
Short=7-methylguanosine nucleotidase;
EC=3.1.3.91 {ECO:0000269|PubMed:23223233};
AltName: Full=Cytosolic 5'-nucleotidase 3B;
AltName: Full=Cytosolic 5'-nucleotidase III-like protein {ECO:0000305|PubMed:23223233};
Short=cN-III-like protein;
EC=3.1.3.5 {ECO:0000269|PubMed:23223233};
AltName: Full=N(7)-methylguanylate 5'-phosphatase;
Name=NT5C3B; Synonyms=NT5C3L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS VAL-209
AND CYS-213.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
VAL-209 AND CYS-213.
TISSUE=Liver, Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=23223233; DOI=10.1074/jbc.M112.426700;
Buschmann J., Moritz B., Jeske M., Lilie H., Schierhorn A., Wahle E.;
"Identification of Drosophila and Human 7-Methyl GMP-specific
Nucleotidases.";
J. Biol. Chem. 288:2441-2451(2013).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=24603684; DOI=10.1371/journal.pone.0090915;
Monecke T., Buschmann J., Neumann P., Wahle E., Ficner R.;
"Crystal structures of the novel cytosolic 5'-nucleotidase IIIB
explain its preference for m7GMP.";
PLoS ONE 9:90915-90915(2014).
-!- FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate
(m(7)GMP) to 7-methylguanosine and inorganic phosphate
(PubMed:23223233, PubMed:24603684). The specific activity for
m(7)GMP may protect cells against undesired salvage of m(7)GMP and
its incorporation into nucleic acids (PubMed:23223233). Also has
weak activity for CMP (PubMed:23223233, PubMed:24603684). UMP and
purine nucleotides are poor substrates (PubMed:23223233).
{ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + N(7)-methylguanosine 5'-phosphate = N(7)-
methylguanosine + phosphate; Xref=Rhea:RHEA:37107,
ChEBI:CHEBI:15377, ChEBI:CHEBI:20794, ChEBI:CHEBI:43474,
ChEBI:CHEBI:58285; EC=3.1.3.91;
Evidence={ECO:0000269|PubMed:23223233};
-!- CATALYTIC ACTIVITY:
Reaction=CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:29367,
ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474,
ChEBI:CHEBI:60377; EC=3.1.3.91;
Evidence={ECO:0000269|PubMed:23223233};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043;
EC=3.1.3.5; Evidence={ECO:0000269|PubMed:23223233};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.8 uM for m(7)GMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:23223233};
KM=8 uM for m(7)GMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:24603684};
KM=79 uM for CMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:23223233, ECO:0000269|PubMed:24603684};
KM=355 uM for GMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:23223233};
KM=456 uM for AMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:23223233};
KM=439 uM for UMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:23223233};
Vmax=0.41 umol/min/mg enzyme with m(7)GMP as substrate
{ECO:0000269|PubMed:23223233};
Vmax=12 umol/min/mg enzyme with CMP as substrate
{ECO:0000269|PubMed:23223233};
Vmax=0.13 umol/min/mg enzyme with GMP as substrate
{ECO:0000269|PubMed:23223233};
Vmax=0.07 umol/min/mg enzyme with AMP as substrate
{ECO:0000269|PubMed:23223233};
Vmax=10.7 umol/min/mg enzyme with UMP as substrate
{ECO:0000269|PubMed:23223233};
Note=kcat is 0.24 sec(-1) with m(7)GMP. kcat is 7 sec(-1) with
CMP. kcat is 0.07 sec(-1) with GMP. kcat is 0.04 sec(-1) with
AMP. kcat is 6.2 sec(-1) with UMP.;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23223233}.
-!- INTERACTION:
P40692:MLH1; NbExp=3; IntAct=EBI-2932564, EBI-744248;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q969T7-1; Sequence=Displayed;
Name=2;
IsoId=Q969T7-2; Sequence=VSP_046297;
-!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC091172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60771.1; -; Genomic_DNA.
EMBL; BC013742; AAH13742.2; -; mRNA.
EMBL; BC014132; AAH14132.2; -; mRNA.
EMBL; BC016971; AAH16971.2; -; mRNA.
EMBL; BC067788; AAH67788.1; -; mRNA.
CCDS; CCDS11410.2; -. [Q969T7-1]
RefSeq; NP_443167.4; NM_052935.4. [Q969T7-1]
UniGene; Hs.237536; -.
ProteinModelPortal; Q969T7; -.
SMR; Q969T7; -.
BioGrid; 125410; 4.
IntAct; Q969T7; 1.
STRING; 9606.ENSP00000389948; -.
DEPOD; Q969T7; -.
iPTMnet; Q969T7; -.
PhosphoSitePlus; Q969T7; -.
BioMuta; NT5C3B; -.
DMDM; 476007845; -.
EPD; Q969T7; -.
MaxQB; Q969T7; -.
PaxDb; Q969T7; -.
PeptideAtlas; Q969T7; -.
PRIDE; Q969T7; -.
ProteomicsDB; 75844; -.
DNASU; 115024; -.
Ensembl; ENST00000435506; ENSP00000389948; ENSG00000141698. [Q969T7-1]
GeneID; 115024; -.
KEGG; hsa:115024; -.
UCSC; uc021txo.2; human. [Q969T7-1]
CTD; 115024; -.
EuPathDB; HostDB:ENSG00000141698.16; -.
GeneCards; NT5C3B; -.
HGNC; HGNC:28300; NT5C3B.
HPA; HPA030786; -.
HPA; HPA057095; -.
neXtProt; NX_Q969T7; -.
OpenTargets; ENSG00000141698; -.
eggNOG; KOG3128; Eukaryota.
eggNOG; ENOG410ZQJ8; LUCA.
GeneTree; ENSGT00390000012959; -.
HOGENOM; HOG000244931; -.
HOVERGEN; HBG059750; -.
KO; K01081; -.
OMA; KAHDLLC; -.
OrthoDB; EOG091G0BCN; -.
TreeFam; TF314663; -.
Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
SABIO-RK; Q969T7; -.
GenomeRNAi; 115024; -.
PRO; PR:Q969T7; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141698; Expressed in 201 organ(s), highest expression level in testis.
CleanEx; HS_NT5C3L; -.
ExpressionAtlas; Q969T7; baseline and differential.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0008253; F:5'-nucleotidase activity; TAS:Reactome.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
CDD; cd07504; HAD_5NT; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
Pfam; PF05822; UMPH-1; 1.
SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
Nucleotide-binding; Polymorphism; Reference proteome.
CHAIN 1 300 7-methylguanosine phosphate-specific 5'-
nucleotidase.
/FTId=PRO_0000328948.
REGION 156 157 Substrate binding.
{ECO:0000250|UniProtKB:Q9H0P0}.
ACT_SITE 41 41 Nucleophile.
{ECO:0000250|UniProtKB:Q9W197}.
ACT_SITE 43 43 Proton donor.
{ECO:0000250|UniProtKB:Q9W197}.
METAL 41 41 Magnesium.
{ECO:0000250|UniProtKB:Q9W197}.
METAL 43 43 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9W197}.
METAL 230 230 Magnesium.
{ECO:0000250|UniProtKB:Q9W197}.
BINDING 88 88 CMP. {ECO:0000250|UniProtKB:Q9W197}.
BINDING 88 88 N(7)-methyl-GMP.
{ECO:0000250|UniProtKB:Q9W197}.
BINDING 205 205 Substrate.
{ECO:0000250|UniProtKB:Q9H0P0}.
MOD_RES 256 256 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 8 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046297.
VARIANT 209 209 A -> V (in dbSNP:rs1046403).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_042582.
VARIANT 213 213 S -> C (in dbSNP:rs1046404).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_042583.
SEQUENCE 300 AA; 34389 MW; 3E221583153381F8 CRC64;
MAEEVSTLMK ATVLMRQPGR VQEIVGALRK GGGDRLQVIS DFDMTLSRFA YNGKRCPSSY
NILDNSKIIS EECRKELTAL LHHYYPIEID PHRTVKEKLP HMVEWWTKAH NLLCQQKIQK
FQIAQVVRES NAMLREGYKT FFNTLYHNNI PLFIFSAGIG DILEEIIRQM KVFHPNIHIV
SNYMDFNEDG FLQGFKGQLI HTYNKNSSAC ENSGYFQQLE GKTNVILLGD SIGDLTMADG
VPGVQNILKI GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLQHILC QGVQLEMQGP


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