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 16-JUN-2009, entry version 49. DE RecName: Full=Putative cytosolic 5'-nucleotidase 3; DE EC=3.1.3.5; DE AltName: Full=Putative pyrimidine 5'-nucleotidase; GN ORFNames=F25B5.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U23172; AAK67227.1; -; Genomic_DNA. DR EMBL; U23172; AAK67228.1; -; Genomic_DNA. DR EMBL; U23172; AAL27245.1; -; Genomic_DNA. DR RefSeq; NP_498293.1; -. DR UniGene; Cel.17714; -. DR IntAct; Q09315; 1. DR Ensembl; F25B5.3; Caenorhabditis elegans. DR GeneID; 175843; -. DR KEGG; cel:F25B5.3; -. DR WormBase; WBGene00017775; F25B5.3. DR WormPep; F25B5.3a; CE26890. DR WormPep; F25B5.3b; CE28001. DR WormPep; F25B5.3c; CE29776. DR OMA; Q09315; EKIPHME. DR BRENDA; 3.1.3.5; 672. DR NextBio; 889908; -. DR ArrayExpress; Q09315; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR006434; HAD-SF_hydro_IE. DR InterPro; IPR018012; HAD-SF_hydro_IE_pln. DR PANTHER; PTHR13045; HAD-SF_hydro_IE; 1. DR Pfam; PF05822; UMPH-1; 1. DR TIGRFAMs; TIGR01544; HAD-SF-IE; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding. FT CHAIN 1 376 Putative cytosolic 5'-nucleotidase 3. FT /FTId=PRO_0000065315. FT REGION 236 237 Substrate binding (By similarity). FT ACT_SITE 119 119 Nucleophile (By similarity). FT ACT_SITE 121 121 Proton donor (By similarity). FT METAL 119 119 Magnesium (By similarity). FT METAL 121 121 Magnesium; via carbonyl oxygen (By FT similarity). FT METAL 312 312 Magnesium (By similarity). FT BINDING 286 286 Substrate (By similarity). FT VAR_SEQ 1 49 Missing (in isoform c). FT /FTId=VSP_002446. FT VAR_SEQ 1 30 MSNKVARRLGKCLFVSGRRFESRQSILQLR -> MGHCFSV FT FSSKETINC (in isoform a). FT /FTId=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 //