5NT3A_CHICK
ID 5NT3A_CHICK Reviewed; 331 AA.
AC Q5ZID6; Q802T3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytosolic 5'-nucleotidase 3A {ECO:0000250|UniProtKB:Q9H0P0};
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9H0P0};
DE AltName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000250|UniProtKB:Q9H0P0};
DE Short=7-methylguanosine nucleotidase;
DE EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9H0P0};
DE AltName: Full=Cytosolic 5'-nucleotidase 3;
DE AltName: Full=Cytosolic 5'-nucleotidase III;
DE Short=cN-III;
DE AltName: Full=Pyrimidine 5'-nucleotidase 1;
DE Short=P5'N-1;
DE Short=P5N-1;
DE Short=PN-I;
GN Name=NT5C3A; Synonyms=NT5C3, PYN1; ORFNames=RCJMB04_27l2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 46-85; 150-158;
RP 220-243 AND 291-290, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Erythrocyte;
RX PubMed=12907448; DOI=10.1182/blood-2002-11-3388;
RA Mass M., Simo E., Dragon S.;
RT "Erythroid pyrimidine 5'-nucleotidase: cloning, developmental expression,
RT and regulation by cAMP and in vivo hypoxia.";
RL Blood 102:4198-4205(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RA Mass M., Dragon S.;
RT "Cloning and gene expression of pyrimidine 5'-nucleotidase in chick
RT embryonic erythrocytes.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Nucleotidase which shows specific activity towards cytidine
CC monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP
CC seems to be the preferred substrate. {ECO:0000250|UniProtKB:Q9H0P0}.
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:Q9H0P0};
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=2;
CC Name=2;
CC IsoId=Q5ZID6-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5ZID6-1; Sequence=VSP_021564;
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels until E13 and the
CC expression rises transiently between E13 and E16.
CC {ECO:0000269|PubMed:12907448}.
CC -!- INDUCTION: By norepinephrine/NE and adenosine which are released by the
CC embryo under hypoxic conditions. By stimulation of beta-
CC adrenergic/adenosine receptors in definitive red blood cells (RBC).
CC {ECO:0000269|PubMed:12907448}.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AF548635; AAQ12342.1; -; mRNA.
DR EMBL; AJ496195; CAD42712.1; -; mRNA.
DR EMBL; AJ720848; CAG32507.1; -; mRNA.
DR RefSeq; NP_989767.1; NM_204436.2. [Q5ZID6-1]
DR RefSeq; XP_015136753.1; XM_015281267.1. [Q5ZID6-3]
DR RefSeq; XP_015136759.1; XM_015281273.1. [Q5ZID6-1]
DR AlphaFoldDB; Q5ZID6; -.
DR SMR; Q5ZID6; -.
DR STRING; 9031.ENSGALP00000019881; -.
DR PaxDb; Q5ZID6; -.
DR Ensembl; ENSGALT00000062778; ENSGALP00000057361; ENSGALG00000031397. [Q5ZID6-1]
DR Ensembl; ENSGALT00000078633; ENSGALP00000054083; ENSGALG00000031397. [Q5ZID6-3]
DR Ensembl; ENSGALT00000094003; ENSGALP00000067277; ENSGALG00000031397. [Q5ZID6-1]
DR GeneID; 395080; -.
DR KEGG; gga:395080; -.
DR CTD; 51251; -.
DR VEuPathDB; HostDB:geneid_395080; -.
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR HOGENOM; CLU_048584_0_2_1; -.
DR InParanoid; Q5ZID6; -.
DR OMA; GPERMQI; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q5ZID6; -.
DR TreeFam; TF314663; -.
DR Reactome; R-GGA-73621; Pyrimidine catabolism.
DR PRO; PR:Q5ZID6; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000031397; Expressed in kidney and 13 other tissues.
DR ExpressionAtlas; Q5ZID6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006248; P:CMP catabolic process; IEA:Ensembl.
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 Alternative splicing; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Cytosolic 5'-nucleotidase 3A"
FT /id="PRO_0000064386"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 130
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 130
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 151
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9D020"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12907448, ECO:0000303|Ref.2"
FT /id="VSP_021564"
SQ SEQUENCE 331 AA; 37370 MW; 7AE5CFE0F280224A CRC64;
MDRAAVAKMG AVASASVCAL VGGVVLAQYI FTMKKKTGRK TKIIEMMPEF QKKTVHIKDP
GRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT CHNIIDNSKL ITEECRKKLL
QLKETYYAIE IDPALTIEEK YPYMVEWYNK SHALLIEQGL QKDKLAEVVR ESDVMLKEGY
ENFFDKLSEH NIPVFIFSAG IGDILEEVIH QAGVYHSNVK VVSNFMDFDE NGILKGFKGE
LIHVYNKHDG ALKNTEYFKQ LKDNSNIILL GDSQGDLSMA DGVANVEHIL KIGYLNDKVD
ELLEKYMDSY DIVLVKDESL EVANSILQKI L
