ID A0A384BQ19_URSMA Unreviewed; 331 AA.
AC A0A384BQ19;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=5'-nucleotidase {ECO:0000256|RuleBase:RU361276};
DE EC=3.1.3.5 {ECO:0000256|RuleBase:RU361276};
GN Name=NT5C3A {ECO:0000313|Ensembl:ENSUMAP00000003310,
GN ECO:0000313|RefSeq:XP_008684693.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008684693.1};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000003310}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008684693.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008684693.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023710};
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:0000256|ARBA:ARBA00000815,
CC ECO:0000256|RuleBase:RU361276};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361276}.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00008389, ECO:0000256|RuleBase:RU361276}.
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DR RefSeq; XP_008684693.1; XM_008686471.2.
DR STRING; 29073.ENSUMAP00000003310; -.
DR Ensembl; ENSUMAT00000004067.1; ENSUMAP00000003310.1; ENSUMAG00000002813.1.
DR GeneID; 103658960; -.
DR KEGG; umr:103658960; -.
DR CTD; 51251; -.
DR OrthoDB; 531581at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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; 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:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361276};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361276};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080,
KW ECO:0000256|RuleBase:RU361276};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361276};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680}.
SQ SEQUENCE 331 AA; 37478 MW; FB3BF3E82B7CAD8A CRC64;
MDRAAVARMG AVASASVCVL VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF QRSSVRIKNP
ARVEEIICGL IKGGAPKLQI ITDFDMTLSR FSYEGKRCPT CHYVIDNSKL VTDECRKKLL
QLKEKYYAIE IDPGLTMEEK YPYMVEWYTK SHGLLVEQAL PKAKLKEIVA ESDVMLKEGY
ENFFDKLQEY GIPVFIFSAG IGDILEEVIH QAGVYHPNIT VVSNFMDFDD NGVLKGFKGE
LIHVFNKHDG ALKNTEYFNR LKDNSNIILL GDSQGDIRMA DGVANVEHIL KIGYLNDRVD
ELLEKYMDSY DIVLVKDESL DVANSILQKI L
//