5NT3_CAEEL
ID 5NT3_CAEEL Reviewed; 376 AA.
AC Q09315; Q95QJ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative cytosolic 5'-nucleotidase 3 {ECO:0000250|UniProtKB:Q9D020};
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9D020};
DE AltName: Full=Putative pyrimidine 5'-nucleotidase;
GN ORFNames=F25B5.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:Q9D020};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=b;
CC IsoId=Q09315-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q09315-2; Sequence=VSP_002447;
CC Name=c;
CC IsoId=Q09315-3; Sequence=VSP_002446;
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
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DR EMBL; FO081045; CCD68774.1; -; Genomic_DNA.
DR EMBL; FO081045; CCD68775.1; -; Genomic_DNA.
DR EMBL; FO081045; CCD68776.1; -; Genomic_DNA.
DR RefSeq; NP_498293.1; NM_065892.4. [Q09315-1]
DR RefSeq; NP_498294.1; NM_065893.3. [Q09315-2]
DR RefSeq; NP_741162.1; NM_171142.3.
DR AlphaFoldDB; Q09315; -.
DR SMR; Q09315; -.
DR BioGRID; 41064; 1.
DR STRING; 6239.F25B5.3b; -.
DR EPD; Q09315; -.
DR PaxDb; Q09315; -.
DR EnsemblMetazoa; F25B5.3a.1; F25B5.3a.1; WBGene00017775. [Q09315-2]
DR EnsemblMetazoa; F25B5.3b.1; F25B5.3b.1; WBGene00017775. [Q09315-1]
DR EnsemblMetazoa; F25B5.3c.1; F25B5.3c.1; WBGene00017775. [Q09315-3]
DR GeneID; 175843; -.
DR KEGG; cel:CELE_F25B5.3; -.
DR UCSC; F25B5.3c.4; c. elegans. [Q09315-1]
DR CTD; 175843; -.
DR WormBase; F25B5.3a; CE26890; WBGene00017775; -. [Q09315-2]
DR WormBase; F25B5.3b; CE28001; WBGene00017775; -. [Q09315-1]
DR WormBase; F25B5.3c; CE29776; WBGene00017775; -. [Q09315-3]
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR InParanoid; Q09315; -.
DR OMA; NTHFISN; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q09315; -.
DR Reactome; R-CEL-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-CEL-73621; Pyrimidine catabolism.
DR PRO; PR:Q09315; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017775; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q09315; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..376
FT /note="Putative cytosolic 5'-nucleotidase 3"
FT /id="PRO_0000065315"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_002446"
FT VAR_SEQ 1..30
FT /note="MSNKVARRLGKCLFVSGRRFESRQSILQLR -> MGHCFSVFSSKETINC
FT (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_002447"
SQ SEQUENCE 376 AA; 42146 MW; C5077AB7A8C8D979 CRC64;
MSNKVARRLG KCLFVSGRRF ESRQSILQLR TETLTDTPLS ATLDQSQFSM FKAAEIVNAA
AACAEAECIE QLKKTDVVPL LMNYLLGEEQ ILVADPTAVA AKLRKMVVGG AGKTVVISDF
DYTLSRFANE QGERLSTTHG VFDDNVMRLK PELGQKFVDL KNKYYPIEFS PNLTMEEKIP
HMEKWWGTSH SLIVNEKFSK NTIEDFVRQS RIVFKDGAED FIEALDAHNI PLVIFSAGIG
NIIEYFLQQK LGAIPRNTHF ISNMILFDED DNACAFSEPL IHTFCKNSSV IQKETSFFHD
IAGRVNVILL GDSMGDIHMD VGVERDGPTL KVGYYNGSLD DTAALQHYEE VYDIVLIHDP
TLNVAQKIVD IINSSH
