ID 5NT3B_RAT Reviewed; 300 AA.
AC Q6AYP7; F8WG43;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 126.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH78963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC078963; AAH78963.1; ALT_INIT; mRNA.
DR RefSeq; NP_001007724.2; NM_001007723.2.
DR RefSeq; XP_017452886.1; XM_017597397.1.
DR AlphaFoldDB; Q6AYP7; -.
DR SMR; Q6AYP7; -.
DR BioGRID; 262082; 1.
DR IntAct; Q6AYP7; 3.
DR STRING; 10116.ENSRNOP00000022430; -.
DR PhosphoSitePlus; Q6AYP7; -.
DR jPOST; Q6AYP7; -.
DR PaxDb; 10116-ENSRNOP00000022430; -.
DR Ensembl; ENSRNOT00000022430.7; ENSRNOP00000022430.3; ENSRNOG00000016475.8.
DR Ensembl; ENSRNOT00055057534; ENSRNOP00055047426; ENSRNOG00055033290.
DR Ensembl; ENSRNOT00060046439; ENSRNOP00060038598; ENSRNOG00060026778.
DR Ensembl; ENSRNOT00065055942; ENSRNOP00065046071; ENSRNOG00065032522.
DR GeneID; 360629; -.
DR KEGG; rno:360629; -.
DR UCSC; RGD:1359229; rat.
DR AGR; RGD:1359229; -.
DR CTD; 115024; -.
DR RGD; 1359229; Nt5c3b.
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR HOGENOM; CLU_048584_0_2_1; -.
DR InParanoid; Q6AYP7; -.
DR OMA; WQQSHEL; -.
DR OrthoDB; 531581at2759; -.
DR TreeFam; TF314663; -.
DR Reactome; R-RNO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR SABIO-RK; Q6AYP7; -.
DR PRO; PR:Q6AYP7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000016475; Expressed in ovary and 20 other cell types or tissues.
DR ExpressionAtlas; Q6AYP7; baseline and differential.
DR Genevisible; Q6AYP7; RN.
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; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR NCBIfam; TIGR01544; HAD-SF-IE; 1.
DR PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR13045:SF15; 7-METHYLGUANOSINE PHOSPHATE-SPECIFIC 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05822; UMPH-1; 1.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..300
FT /note="7-methylguanosine phosphate-specific 5'-
FT nucleotidase"
FT /id="PRO_0000328950"
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"
SQ SEQUENCE 300 AA; 34536 MW; 73AD8E974981E20A CRC64;
MAEEVSSLMK ATVLMRQPGR VQEIVSALRR GGGDRLQVIS DFDMTLSRFA YNGQRCPSSH
NILDNSKIIS EDCRKELTEL FHHYYPIEID PHRTIKEKLP HMVQWWSKAH SLLCQQRIQK
FQIAQVVGES TAMLREGYKM FFDTLYHNNI PLFIFSAGIG DILEEIIRQM KVFHPNIHIV
SNYMDFSEDG FLKGFKGQLI HTYNKNSSVC ENSSYFQQLR NKTNIILLGD SIGDLTMADG
VPGVQNILKI GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLQHILR QGDCVELQGS
//
