5NTD_RAT
ID 5NTD_RAT Reviewed; 576 AA.
AC P21588;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5;
DE AltName: Full=Ecto-5'-nucleotidase;
DE AltName: CD_antigen=CD73;
DE Flags: Precursor;
GN Name=Nt5e; Synonyms=Nt5, Nte;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2298743; DOI=10.1016/s0021-9258(19)39958-2;
RA Misumi Y., Ogata S., Hirose S., Ikehara Y.;
RT "Primary structure of rat liver 5'-nucleotidase deduced from the cDNA.
RT Presence of the COOH-terminal hydrophobic domain for possible post-
RT translational modification by glycophospholipid.";
RL J. Biol. Chem. 265:2178-2183(1990).
RN [2]
RP PROTEIN SEQUENCE OF 538-551, AND GPI-ANCHOR AT SER-551.
RC TISSUE=Liver;
RX PubMed=2148114; DOI=10.1021/bi00486a021;
RA Ogata S., Hayashi Y., Misumi Y., Ikehara Y.;
RT "Membrane-anchoring domain of rat liver 5'-nucleotidase: identification of
RT the COOH-terminal serine-523 covalently attached with a glycolipid.";
RL Biochemistry 29:7923-7927(1990).
CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable
CC nucleosides.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; J05214; AAA40621.1; -; mRNA.
DR PIR; A35036; A35036.
DR AlphaFoldDB; P21588; -.
DR SMR; P21588; -.
DR STRING; 10116.ENSRNOP00000015057; -.
DR BindingDB; P21588; -.
DR ChEMBL; CHEMBL1075214; -.
DR DrugCentral; P21588; -.
DR GuidetoPHARMACOLOGY; 1232; -.
DR GlyGen; P21588; 5 sites.
DR iPTMnet; P21588; -.
DR PhosphoSitePlus; P21588; -.
DR PaxDb; P21588; -.
DR PRIDE; P21588; -.
DR UCSC; RGD:61956; rat.
DR RGD; 61956; Nt5e.
DR eggNOG; KOG4419; Eukaryota.
DR InParanoid; P21588; -.
DR PhylomeDB; P21588; -.
DR BRENDA; 3.1.3.5; 5301.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR Reactome; R-RNO-73621; Pyrimidine catabolism.
DR Reactome; R-RNO-74259; Purine catabolism.
DR PRO; PR:P21588; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:RGD.
DR GO; GO:0008198; F:ferrous iron binding; IDA:RGD.
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:0046086; P:adenosine biosynthetic process; ISO:RGD.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:RGD.
DR GO; GO:0046032; P:ADP catabolic process; ISO:RGD.
DR GO; GO:0006196; P:AMP catabolic process; IDA:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0110148; P:biomineralization; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEP:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0010035; P:response to inorganic substance; ISO:RGD.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..28
FT CHAIN 29..551
FT /note="5'-nucleotidase"
FT /id="PRO_0000000019"
FT PROPEP 552..576
FT /note="Removed in mature form"
FT /id="PRO_0000000020"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 502..508
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 551
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:2148114"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..59
FT /evidence="ECO:0000250"
FT DISULFID 355..360
FT /evidence="ECO:0000250"
FT DISULFID 367..389
FT /evidence="ECO:0000250"
FT DISULFID 478..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 63969 MW; 9EB75DD51E678AA6 CRC64;
MRPAAATAPK WLLLALSALL PLWPTAKSWE LTIMHTNDVH SRLEQTSDDS TKCLNASLCV
GGVARLFTKV QQIRKEEPNV LLLDAGDQYQ GTIWFTVYKG LEVAHFMNLL GYDAMALGNH
EFDNGVEGLI DPLLRNVKFP ILSANIKARG PLAPQISGLY LPYKVLSVGG EVVGIVGYTS
KETPFLSNPG TNLVFEDEVT ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDV
VVGGHTNTFL YTGNPPSKEV PAGKYPFIVT SDDGRKVPVV QAYAFGKYLG YLKVEFDDKG
NVVTSYGNPI LLNSTIREDA AIKADINQWR IKLDNYSTQE LGRTIVYLNG SAQECRFREC
NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI DERNNGTITW ENLAAVLPFG
GTFDLVQLKG STLKKAFEHS VHRYGQSTGE FLQVGGIHVV YDISRKPWDR VVQLKVLCTK
CRVPIYEPLE MDKVYKVVLP SYLVNGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVI
YPAVEGRIKF SAASHYQGSF PLIILSFWAV ILVLYQ
