5NTD_BOVIN
ID 5NTD_BOVIN Reviewed; 574 AA.
AC Q05927; Q24K05;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8340354; DOI=10.1093/oxfordjournals.jbchem.a124090;
RA Suzuki K., Furukawa Y., Tamura H., Ejiri N., Suematsu H., Taguchi R.,
RA Nakamura S., Suzuki Y., Ikezawa H.;
RT "Purification and cDNA cloning of bovine liver 5'-nucleotidase, a GPI-
RT anchored protein, and its expression in COS cells.";
RL J. Biochem. 113:607-613(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP SUBUNIT.
RX PubMed=10825541; DOI=10.1016/s0167-4838(00)00035-2;
RA Martinez-Martinez A., Munoz-Delgado E., Campoy F.J., Flores-Flores C.,
RA Rodriguez-Lopez J.N., Fini C., Vidal C.J.;
RT "The ecto-5'-nucleotidase subunits in dimers are not linked by disulfide
RT bridges but by non-covalent bonds.";
RL Biochim. Biophys. Acta 1478:300-308(2000).
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. {ECO:0000269|PubMed:10825541}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
CC -!- CAUTION: The homodimer was initially thought to be disulfide bonded;
CC however it is not the case. {ECO:0000305|PubMed:10825541}.
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DR EMBL; D14541; BAA03408.1; -; mRNA.
DR EMBL; S64302; AAB27698.1; -; mRNA.
DR EMBL; BC114093; AAI14094.1; -; mRNA.
DR EMBL; BT026240; ABG67079.1; -; mRNA.
DR PIR; JX0269; JX0269.
DR RefSeq; NP_776554.2; NM_174129.3.
DR AlphaFoldDB; Q05927; -.
DR SMR; Q05927; -.
DR STRING; 9913.ENSBTAP00000054917; -.
DR PaxDb; Q05927; -.
DR GeneID; 281363; -.
DR KEGG; bta:281363; -.
DR CTD; 4907; -.
DR eggNOG; KOG4419; Eukaryota.
DR InParanoid; Q05927; -.
DR OrthoDB; 484599at2759; -.
DR SABIO-RK; Q05927; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0009166; P:nucleotide catabolic process; IEA:InterPro.
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..26
FT CHAIN 27..549
FT /note="5'-nucleotidase"
FT /id="PRO_0000000013"
FT PROPEP 550..574
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000014"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 500..506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 549
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..57
FT /evidence="ECO:0000250"
FT DISULFID 353..358
FT /evidence="ECO:0000250"
FT DISULFID 365..387
FT /evidence="ECO:0000250"
FT DISULFID 476..479
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="A -> P (in Ref. 1; BAA03408/AAB27698)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="DA -> ES (in Ref. 1; BAA03408/AAB27698)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..438
FT /note="EHS -> DDT (in Ref. 1; BAA03408/AAB27698)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="A -> R (in Ref. 1; BAA03408/AAB27698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62966 MW; DF5BF74E05BFE0A3 CRC64;
MNPGAARTPA LRILALGALL WPAARPWELT ILHTNDVHSR LEQTSEDSSK CVNASRCVGG
VARLATKVHQ IRRAEPHVLL LDAGDQYQGT IWFTVYKGTE VAHFMNALGY DAMALGNHEF
DNGVEGLIDP LLKEVNFPIL SANIKAKGPL ASKISGLYSP YKILTVGDEV VGIVGYTSKE
TPFLSNPGTN LVFEDEITAL QPEVDKLKTL NVNKIIALGH SGFEVDKLIA QKVKGVDVVV
GGHSNTFLYT GNPPSKEVPA GQYPFIVTSD DGRKVPVVQA YAFGKYLGYL KVEFDEKGNV
VTSHGNPILL NSSIPEDPNI KADINKWRVK LDNYSTQELG KTIVYLDGTA QSCRFRECNM
GNLICDAMIN NNLRHPDEMS WNHVSMCILN GGGIRSPIDE RNNGTITWEN LAAVLPFGGT
FDLVQLKGST LKKAFEHSVH RYGQATGEFL QVGGIHVVYD ISRNPGDRVV KLEVLCTQCR
VPSYEPLRMD KVYKVILPSF LVSGGDGFQM IKDEKIKHDS GDQDINVVSG YISKMKVLYP
AVEGRIQFSA GSHCCGSFSL IFLSVLAVII ILYQ
