5NTD_MOUSE
ID 5NTD_MOUSE Reviewed; 576 AA.
AC Q61503; Q3U3S1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 188.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=8224905; DOI=10.1016/0378-1119(93)90635-g;
RA Resta R., Hooker S.W., Hansen K.R., Laurent A.B., Park J.L.,
RA Blackburn M.R., Knudsen T.B., Thompson L.F.;
RT "Murine ecto-5'-nucleotidase (CD73): cDNA cloning and tissue
RT distribution.";
RL Gene 133:171-177(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313 AND ASN-335.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; L12059; AAC13542.1; -; mRNA.
DR EMBL; AK028723; BAC26084.1; -; mRNA.
DR EMBL; AK029979; BAC26714.1; -; mRNA.
DR EMBL; AK154614; BAE32714.1; -; mRNA.
DR CCDS; CCDS23386.1; -.
DR PIR; JC2001; JC2001.
DR RefSeq; NP_035981.1; NM_011851.4.
DR AlphaFoldDB; Q61503; -.
DR SMR; Q61503; -.
DR IntAct; Q61503; 1.
DR STRING; 10090.ENSMUSP00000034992; -.
DR BindingDB; Q61503; -.
DR ChEMBL; CHEMBL4680034; -.
DR GlyConnect; 2099; 1 N-Linked glycan (2 sites).
DR GlyGen; Q61503; 4 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q61503; -.
DR PhosphoSitePlus; Q61503; -.
DR jPOST; Q61503; -.
DR MaxQB; Q61503; -.
DR PaxDb; Q61503; -.
DR PeptideAtlas; Q61503; -.
DR PRIDE; Q61503; -.
DR ProteomicsDB; 296423; -.
DR Antibodypedia; 3007; 1275 antibodies from 51 providers.
DR DNASU; 23959; -.
DR Ensembl; ENSMUST00000034992; ENSMUSP00000034992; ENSMUSG00000032420.
DR GeneID; 23959; -.
DR KEGG; mmu:23959; -.
DR UCSC; uc009qyj.2; mouse.
DR CTD; 4907; -.
DR MGI; MGI:99782; Nt5e.
DR VEuPathDB; HostDB:ENSMUSG00000032420; -.
DR eggNOG; KOG4419; Eukaryota.
DR GeneTree; ENSGT00530000063775; -.
DR HOGENOM; CLU_005854_7_1_1; -.
DR InParanoid; Q61503; -.
DR OMA; VQPFTNM; -.
DR OrthoDB; 484599at2759; -.
DR PhylomeDB; Q61503; -.
DR TreeFam; TF323589; -.
DR BRENDA; 3.1.3.5; 3474.
DR Reactome; R-MMU-196807; Nicotinate metabolism.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR Reactome; R-MMU-74259; Purine catabolism.
DR BioGRID-ORCS; 23959; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q61503; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q61503; protein.
DR Bgee; ENSMUSG00000032420; Expressed in epithelium of stomach and 199 other tissues.
DR ExpressionAtlas; Q61503; baseline and differential.
DR Genevisible; Q61503; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008253; F:5'-nucleotidase activity; IMP:MGI.
DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0046085; P:adenosine metabolic process; ISO:MGI.
DR GO; GO:0046032; P:ADP catabolic process; IMP:MGI.
DR GO; GO:0006196; P:AMP catabolic process; IMP:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0110148; P:biomineralization; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; ISO:MGI.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
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; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..551
FT /note="5'-nucleotidase"
FT /id="PRO_0000000017"
FT PROPEP 552..576
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000018"
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:0000250"
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:0000269|PubMed:19349973"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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; 63864 MW; 29D697928A5D5915 CRC64;
MRPAAAKVPK WLLLALSALL PQWPAASAWE LTILHTNDVH SRLEQTSDDS TKCLNASLCV
GGVARLFTKV QQIRKEEPNV LFLDAGDQYQ GTIWFTVYKG LEVAHFMNIL GYDAMALGNH
EFDNGVEGLI DPLLRNVKFP ILSANIKARG PLAHQISGLF LPSKVLSVGG EVVGIVGYTS
KETPFLSNPG TNLVFEDEIS ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDI
VVGGHSNTFL YTGNPPSKEV PAGKYPFIVT ADDGRQVPVV QAYAFGKYLG YLKVEFDDKG
NVITSYGNPI LLNSSIPEDA TIKADINQWR IKLDNYSTQE LGRTIVYLDG STQTCRFREC
NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI DEKNNGTITW ENLAAVLPFG
GTFDLVQLKG STLKKAFEHS VHRYGQSTGE FLQVGGIHVV YDINRKPWNR VVQLEVLCTK
CRVPIYEPLE MDKVYKVTLP SYLANGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVV
YPAVEGRIKF SAASHYQGSF PLVILSFWAM ILILYQ
