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5'-nucleotidase (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (CD antigen CD73)

 5NTD_MOUSE              Reviewed;         576 AA.
Q61503; Q3U3S1;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 2.
28-MAR-2018, entry version 163.
RecName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
AltName: Full=Ecto-5'-nucleotidase;
AltName: CD_antigen=CD73;
Flags: Precursor;
Name=Nt5e; Synonyms=Nt5, Nte;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=8224905; DOI=10.1016/0378-1119(93)90635-G;
Resta R., Hooker S.W., Hansen K.R., Laurent A.B., Park J.L.,
Blackburn M.R., Knudsen T.B., Thompson L.F.;
"Murine ecto-5'-nucleotidase (CD73): cDNA cloning and tissue
distribution.";
Gene 133:171-177(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313 AND ASN-335.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane
permeable nucleosides.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L12059; AAC13542.1; -; mRNA.
EMBL; AK028723; BAC26084.1; -; mRNA.
EMBL; AK029979; BAC26714.1; -; mRNA.
EMBL; AK154614; BAE32714.1; -; mRNA.
CCDS; CCDS23386.1; -.
PIR; JC2001; JC2001.
RefSeq; NP_035981.1; NM_011851.4.
UniGene; Mm.244235; -.
ProteinModelPortal; Q61503; -.
SMR; Q61503; -.
IntAct; Q61503; 3.
MINT; Q61503; -.
STRING; 10090.ENSMUSP00000034992; -.
iPTMnet; Q61503; -.
PhosphoSitePlus; Q61503; -.
MaxQB; Q61503; -.
PaxDb; Q61503; -.
PeptideAtlas; Q61503; -.
PRIDE; Q61503; -.
Ensembl; ENSMUST00000034992; ENSMUSP00000034992; ENSMUSG00000032420.
GeneID; 23959; -.
KEGG; mmu:23959; -.
UCSC; uc009qyj.2; mouse.
CTD; 4907; -.
MGI; MGI:99782; Nt5e.
eggNOG; KOG4419; Eukaryota.
eggNOG; COG0737; LUCA.
GeneTree; ENSGT00530000063775; -.
HOGENOM; HOG000247215; -.
HOVERGEN; HBG000026; -.
InParanoid; Q61503; -.
KO; K19970; -.
OMA; CRFQECN; -.
OrthoDB; EOG091G08IK; -.
PhylomeDB; Q61503; -.
TreeFam; TF323589; -.
Reactome; R-MMU-196807; Nicotinate metabolism.
Reactome; R-MMU-73621; Pyrimidine catabolism.
Reactome; R-MMU-74259; Purine catabolism.
PRO; PR:Q61503; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032420; -.
CleanEx; MM_NT5E; -.
ExpressionAtlas; Q61503; baseline and differential.
Genevisible; Q61503; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0008253; F:5'-nucleotidase activity; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0046086; P:adenosine biosynthetic process; IMP:MGI.
GO; GO:0006196; P:AMP catabolic process; IMP:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
Gene3D; 3.60.21.10; -; 1.
Gene3D; 3.90.780.10; -; 1.
InterPro; IPR008334; 5'-Nucleotdase_C.
InterPro; IPR036907; 5'-Nucleotdase_C_sf.
InterPro; IPR006146; 5'-Nucleotdase_CS.
InterPro; IPR006179; 5_nucleotidase/apyrase.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
PANTHER; PTHR11575; PTHR11575; 1.
Pfam; PF02872; 5_nucleotid_C; 1.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR01607; APYRASEFAMLY.
SUPFAM; SSF55816; SSF55816; 1.
PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
Nucleotide-binding; Reference proteome; Signal; Zinc.
SIGNAL 1 28 {ECO:0000250}.
CHAIN 29 551 5'-nucleotidase.
/FTId=PRO_0000000017.
PROPEP 552 576 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000000018.
REGION 502 508 Substrate binding. {ECO:0000250}.
METAL 38 38 Zinc 1. {ECO:0000250}.
METAL 40 40 Zinc 1. {ECO:0000250}.
METAL 87 87 Zinc 1. {ECO:0000250}.
METAL 87 87 Zinc 2. {ECO:0000250}.
METAL 119 119 Zinc 2. {ECO:0000250}.
METAL 222 222 Zinc 2. {ECO:0000250}.
METAL 245 245 Zinc 2. {ECO:0000250}.
BINDING 247 247 Substrate. {ECO:0000250}.
BINDING 356 356 Substrate. {ECO:0000250}.
BINDING 392 392 Substrate. {ECO:0000250}.
BINDING 397 397 Substrate. {ECO:0000250}.
BINDING 419 419 Substrate. {ECO:0000250}.
SITE 120 120 Transition state stabilizer.
{ECO:0000250}.
SITE 123 123 Transition state stabilizer.
{ECO:0000250}.
LIPID 551 551 GPI-anchor amidated serine.
{ECO:0000250}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 59 {ECO:0000250}.
DISULFID 355 360 {ECO:0000250}.
DISULFID 367 389 {ECO:0000250}.
DISULFID 478 481 {ECO:0000250}.
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


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