5NTD_HUMAN
ID 5NTD_HUMAN Reviewed; 574 AA.
AC P21589; B3KQI8; O75520; Q5W116;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 219.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP GPI-ANCHOR AT SER-549.
RC TISSUE=Placenta;
RX PubMed=2129526; DOI=10.1111/j.1432-1033.1990.tb19158.x;
RA Misumi Y., Ogata S., Ohkubo K., Hirose S., Ikehara Y.;
RT "Primary structure of human placental 5'-nucleotidase and identification of
RT the glycolipid anchor in the mature form.";
RL Eur. J. Biochem. 191:563-569(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113.
RC TISSUE=Placenta;
RX PubMed=8566797; DOI=10.1016/0378-1119(95)00574-9;
RA Hansen K.R., Resta R., Webb C.F., Thompson L.F.;
RT "Isolation and characterization of the promoter of the human 5'-
RT nucleotidase (CD73)-encoding gene.";
RL Gene 167:307-312(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-489, AND VARIANT ALA-376.
RC TISSUE=Leukocyte;
RA Zanoni L., Rosi F., Pagani R., Marinello E.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 27-40.
RC TISSUE=Placenta;
RX PubMed=2173922; DOI=10.1016/0006-291x(90)91601-n;
RA Klemens M.R., Sherman W.R., Holmberg N.J., Ruedi J.M., Low M.G.,
RA Thompson L.F.;
RT "Characterization of soluble vs membrane-bound human placental 5'-
RT nucleotidase.";
RL Biochem. Biophys. Res. Commun. 172:1371-1377(1990).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-311; ASN-333 AND ASN-403.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333.
RC TISSUE=Leukemic T-cell;
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 [9]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=21933152; DOI=10.1042/bj20111263;
RA Garavaglia S., Bruzzone S., Cassani C., Canella L., Allegrone G.,
RA Sturla L., Mannino E., Millo E., De Flora A., Rizzi M.;
RT "The high-resolution crystal structure of periplasmic Haemophilus
RT influenzae NAD nucleotidase reveals a novel enzymatic function of human
RT CD73 related to NAD metabolism.";
RL Biochem. J. 441:131-141(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 27-549 IN COMPLEXES WITH ATP
RP ANALOG AND ZINC IONS, SUBUNIT, GLYCOSYLATION AT ASN-311, AND DISULFIDE
RP BONDS.
RX PubMed=23142347; DOI=10.1016/j.str.2012.10.001;
RA Knapp K., Zebisch M., Pippel J., El-Tayeb A., Muller C.E., Strater N.;
RT "Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into
RT the regulation of purinergic signaling.";
RL Structure 20:2161-2173(2012).
RN [12]
RP VARIANT CALJA TYR-358.
RX PubMed=21288095; DOI=10.1056/nejmoa0912923;
RA St Hilaire C., Ziegler S.G., Markello T.C., Brusco A., Groden C., Gill F.,
RA Carlson-Donohoe H., Lederman R.J., Chen M.Y., Yang D., Siegenthaler M.P.,
RA Arduino C., Mancini C., Freudenthal B., Stanescu H.C., Zdebik A.A.,
RA Chaganti R.K., Nussbaum R.L., Kleta R., Gahl W.A., Boehm M.;
RT "NT5E mutations and arterial calcifications.";
RL N. Engl. J. Med. 364:432-442(2011).
RN [13]
RP CHARACTERIZATION OF VARIANT CALJA TYR-358.
RX PubMed=24887587; DOI=10.1371/journal.pone.0098568;
RA Fausther M., Lavoie E.G., Goree J.R., Baldini G., Dranoff J.A.;
RT "NT5E mutations that cause human disease are associated with intracellular
RT mistrafficking of NT5E protein.";
RL PLoS ONE 9:E98568-E98568(2014).
CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable
CC nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities.
CC {ECO:0000269|PubMed:21933152}.
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:23142347}.
CC -!- INTERACTION:
CC P21589; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-6393623, EBI-13044680;
CC P21589; Q8WWF5: ZNRF4; NbExp=3; IntAct=EBI-6393623, EBI-2129267;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2129526};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2129526}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21589-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21589-2; Sequence=VSP_043076;
CC -!- DISEASE: Calcification of joints and arteries (CALJA) [MIM:211800]: A
CC condition characterized by adult-onset calcification of the lower
CC extremity arteries, including the iliac, femoral and tibial arteries,
CC and hand and foot capsule joints. Age of onset has been reported as
CC early as the second decade of life, usually involving intense joint
CC pain or calcification in the hands. {ECO:0000269|PubMed:21288095,
CC ECO:0000269|PubMed:24887587}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NT5EID44492ch6q14.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55740; CAA39271.1; -; mRNA.
DR EMBL; AK075008; BAG52050.1; -; mRNA.
DR EMBL; AL135903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U21730; AAA96950.1; -; Genomic_DNA.
DR EMBL; AF069067; AAC98672.1; -; Genomic_DNA.
DR CCDS; CCDS5002.1; -. [P21589-1]
DR CCDS; CCDS56439.1; -. [P21589-2]
DR PIR; S11032; S11032.
DR RefSeq; NP_001191742.1; NM_001204813.1. [P21589-2]
DR RefSeq; NP_002517.1; NM_002526.3. [P21589-1]
DR PDB; 4H1S; X-ray; 2.20 A; A/B=27-549.
DR PDB; 4H1Y; X-ray; 1.58 A; P=27-549.
DR PDB; 4H2B; X-ray; 1.70 A; A=27-549.
DR PDB; 4H2F; X-ray; 1.85 A; A=27-549.
DR PDB; 4H2G; X-ray; 1.55 A; A=27-549.
DR PDB; 4H2I; X-ray; 2.00 A; A=27-549.
DR PDB; 6HXW; X-ray; 2.78 A; A/B=27-553.
DR PDB; 6S7F; X-ray; 2.05 A; A=27-549.
DR PDB; 6S7H; X-ray; 1.85 A; A=27-549.
DR PDB; 6TVE; X-ray; 1.05 A; P=27-549.
DR PDB; 6TVG; X-ray; 1.48 A; A=27-549.
DR PDB; 6TVX; X-ray; 2.60 A; A=27-549.
DR PDB; 6TW0; X-ray; 2.50 A; A=27-549.
DR PDB; 6TWA; X-ray; 2.00 A; A=27-549.
DR PDB; 6TWF; X-ray; 2.50 A; A=27-549.
DR PDB; 6VC9; X-ray; 2.25 A; A=27-549.
DR PDB; 6VCA; X-ray; 3.73 A; A/B/C/D=27-549.
DR PDB; 6XUE; X-ray; 1.94 A; A/B=27-549.
DR PDB; 6XUG; X-ray; 2.09 A; A/B=27-549.
DR PDB; 6XUQ; X-ray; 1.97 A; A=27-549.
DR PDB; 6YE1; X-ray; 2.66 A; A/B=27-549.
DR PDB; 6YE2; X-ray; 2.44 A; A/B=27-549.
DR PDB; 6Z9B; X-ray; 2.17 A; A=27-549.
DR PDB; 6Z9D; X-ray; 1.90 A; A=27-549.
DR PDB; 7BBJ; X-ray; 2.72 A; A/B=27-549.
DR PDB; 7JV8; X-ray; 2.46 A; A/B/C/D=27-549.
DR PDB; 7JV9; X-ray; 2.70 A; A/B=27-549.
DR PDB; 7P9N; X-ray; 1.55 A; A=27-549.
DR PDB; 7P9R; X-ray; 1.41 A; A=27-549.
DR PDB; 7P9T; X-ray; 1.79 A; A=27-549.
DR PDB; 7PA4; X-ray; 1.45 A; A=27-549.
DR PDB; 7PB5; X-ray; 1.28 A; A=27-549.
DR PDB; 7PBA; X-ray; 1.42 A; A=27-549.
DR PDB; 7PBB; X-ray; 1.47 A; A=27-549.
DR PDB; 7PBY; X-ray; 1.13 A; A=27-549.
DR PDB; 7PCP; X-ray; 1.38 A; A=27-549.
DR PDB; 7PD9; X-ray; 1.39 A; A=27-549.
DR PDB; 7QGA; X-ray; 1.50 A; A=27-549.
DR PDB; 7QGL; X-ray; 1.50 A; A=27-549.
DR PDB; 7QGM; X-ray; 2.90 A; A=1-549.
DR PDB; 7QGO; X-ray; 2.21 A; A=27-549.
DR PDBsum; 4H1S; -.
DR PDBsum; 4H1Y; -.
DR PDBsum; 4H2B; -.
DR PDBsum; 4H2F; -.
DR PDBsum; 4H2G; -.
DR PDBsum; 4H2I; -.
DR PDBsum; 6HXW; -.
DR PDBsum; 6S7F; -.
DR PDBsum; 6S7H; -.
DR PDBsum; 6TVE; -.
DR PDBsum; 6TVG; -.
DR PDBsum; 6TVX; -.
DR PDBsum; 6TW0; -.
DR PDBsum; 6TWA; -.
DR PDBsum; 6TWF; -.
DR PDBsum; 6VC9; -.
DR PDBsum; 6VCA; -.
DR PDBsum; 6XUE; -.
DR PDBsum; 6XUG; -.
DR PDBsum; 6XUQ; -.
DR PDBsum; 6YE1; -.
DR PDBsum; 6YE2; -.
DR PDBsum; 6Z9B; -.
DR PDBsum; 6Z9D; -.
DR PDBsum; 7BBJ; -.
DR PDBsum; 7JV8; -.
DR PDBsum; 7JV9; -.
DR PDBsum; 7P9N; -.
DR PDBsum; 7P9R; -.
DR PDBsum; 7P9T; -.
DR PDBsum; 7PA4; -.
DR PDBsum; 7PB5; -.
DR PDBsum; 7PBA; -.
DR PDBsum; 7PBB; -.
DR PDBsum; 7PBY; -.
DR PDBsum; 7PCP; -.
DR PDBsum; 7PD9; -.
DR PDBsum; 7QGA; -.
DR PDBsum; 7QGL; -.
DR PDBsum; 7QGM; -.
DR PDBsum; 7QGO; -.
DR AlphaFoldDB; P21589; -.
DR SMR; P21589; -.
DR BioGRID; 110962; 77.
DR DIP; DIP-59992N; -.
DR IntAct; P21589; 44.
DR MINT; P21589; -.
DR STRING; 9606.ENSP00000257770; -.
DR BindingDB; P21589; -.
DR ChEMBL; CHEMBL5957; -.
DR DrugBank; DB00987; Cytarabine.
DR DrugBank; DB00806; Pentoxifylline.
DR GuidetoPHARMACOLOGY; 1232; -.
DR DEPOD; NT5E; -.
DR GlyGen; P21589; 4 sites.
DR iPTMnet; P21589; -.
DR PhosphoSitePlus; P21589; -.
DR SwissPalm; P21589; -.
DR BioMuta; NT5E; -.
DR DMDM; 112825; -.
DR CPTAC; CPTAC-552; -.
DR EPD; P21589; -.
DR jPOST; P21589; -.
DR MassIVE; P21589; -.
DR MaxQB; P21589; -.
DR PaxDb; P21589; -.
DR PeptideAtlas; P21589; -.
DR PRIDE; P21589; -.
DR ProteomicsDB; 53883; -. [P21589-1]
DR ProteomicsDB; 53884; -. [P21589-2]
DR ABCD; P21589; 24 sequenced antibodies.
DR Antibodypedia; 3007; 1275 antibodies from 51 providers.
DR CPTC; P21589; 1 antibody.
DR DNASU; 4907; -.
DR Ensembl; ENST00000257770.8; ENSP00000257770.3; ENSG00000135318.12. [P21589-1]
DR Ensembl; ENST00000369651.7; ENSP00000358665.3; ENSG00000135318.12. [P21589-2]
DR GeneID; 4907; -.
DR KEGG; hsa:4907; -.
DR MANE-Select; ENST00000257770.8; ENSP00000257770.3; NM_002526.4; NP_002517.1.
DR UCSC; uc003pko.5; human. [P21589-1]
DR CTD; 4907; -.
DR DisGeNET; 4907; -.
DR GeneCards; NT5E; -.
DR HGNC; HGNC:8021; NT5E.
DR HPA; ENSG00000135318; Tissue enhanced (cervix, retina).
DR MalaCards; NT5E; -.
DR MIM; 129190; gene.
DR MIM; 211800; phenotype.
DR neXtProt; NX_P21589; -.
DR OpenTargets; ENSG00000135318; -.
DR Orphanet; 289601; Hereditary arterial and articular multiple calcification syndrome.
DR PharmGKB; PA31804; -.
DR VEuPathDB; HostDB:ENSG00000135318; -.
DR eggNOG; KOG4419; Eukaryota.
DR GeneTree; ENSGT00530000063775; -.
DR HOGENOM; CLU_005854_7_1_1; -.
DR OMA; VQPFTNM; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P21589; -.
DR TreeFam; TF323589; -.
DR BioCyc; MetaCyc:HS05981-MON; -.
DR BRENDA; 3.1.3.5; 2681.
DR PathwayCommons; P21589; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR Reactome; R-HSA-73621; Pyrimidine catabolism.
DR Reactome; R-HSA-74259; Purine catabolism.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; P21589; -.
DR SIGNOR; P21589; -.
DR BioGRID-ORCS; 4907; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; NT5E; human.
DR GeneWiki; NT5E; -.
DR GenomeRNAi; 4907; -.
DR Pharos; P21589; Tchem.
DR PRO; PR:P21589; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P21589; protein.
DR Bgee; ENSG00000135318; Expressed in stromal cell of endometrium and 197 other tissues.
DR ExpressionAtlas; P21589; baseline and differential.
DR Genevisible; P21589; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
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:0046086; P:adenosine biosynthetic process; IEA:Ensembl.
DR GO; GO:0046032; P:ADP catabolic process; IEA:Ensembl.
DR GO; GO:0006196; P:AMP catabolic process; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IDA:MGI.
DR GO; GO:0110148; P:biomineralization; IDA:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:CACAO.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IDA:MGI.
DR GO; GO:0010035; P:response to inorganic substance; IDA: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 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2173922"
FT CHAIN 27..549
FT /note="5'-nucleotidase"
FT /evidence="ECO:0000269|PubMed:2129526"
FT /id="PRO_0000000015"
FT PROPEP 550..574
FT /note="Removed in mature form"
FT /id="PRO_0000000016"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2G,
FT ECO:0007744|PDB:4H2I"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2G,
FT ECO:0007744|PDB:4H2I"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2G,
FT ECO:0007744|PDB:4H2I"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H2I"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2I"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2I"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2I"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2I"
FT BINDING 500..506
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2I"
FT SITE 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:23142347"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:23142347"
FT LIPID 549
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:2129526"
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:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23142347, ECO:0007744|PDB:4H1S"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 51..57
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT DISULFID 353..358
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT DISULFID 365..387
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT DISULFID 476..479
FT /evidence="ECO:0000269|PubMed:23142347,
FT ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y,
FT ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F,
FT ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I"
FT VAR_SEQ 404..453
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_043076"
FT VARIANT 358
FT /note="C -> Y (in CALJA; absence from the plasma-membrane;
FT exhibits no catalytic AMPase activity; dbSNP:rs387906620)"
FT /evidence="ECO:0000269|PubMed:21288095,
FT ECO:0000269|PubMed:24887587"
FT /id="VAR_065185"
FT VARIANT 376
FT /note="T -> A (in dbSNP:rs2229523)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022091"
FT VARIANT 379
FT /note="M -> T (in dbSNP:rs2229524)"
FT /id="VAR_048103"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6TVE"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:6TVE"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4H2G"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:6TVE"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:7P9T"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:6TVE"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:6TVE"
FT TURN 439..443
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 491..498
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:6TVE"
FT HELIX 524..535
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:6TVE"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:6TVE"
SQ SEQUENCE 574 AA; 63368 MW; A99AF170AB7EAECE CRC64;
MCPRAARAPA TLLLALGAVL WPAAGAWELT ILHTNDVHSR LEQTSEDSSK CVNASRCMGG
VARLFTKVQQ IRRAEPNVLL LDAGDQYQGT IWFTVYKGAE VAHFMNALRY DAMALGNHEF
DNGVEGLIEP LLKEAKFPIL SANIKAKGPL ASQISGLYLP YKVLPVGDEV VGIVGYTSKE
TPFLSNPGTN LVFEDEITAL QPEVDKLKTL NVNKIIALGH SGFEMDKLIA QKVRGVDVVV
GGHSNTFLYT GNPPSKEVPA GKYPFIVTSD DGRKVPVVQA YAFGKYLGYL KIEFDERGNV
ISSHGNPILL NSSIPEDPSI KADINKWRIK LDNYSTQELG KTIVYLDGSS QSCRFRECNM
GNLICDAMIN NNLRHTDEMF WNHVSMCILN GGGIRSPIDE RNNGTITWEN LAAVLPFGGT
FDLVQLKGST LKKAFEHSVH RYGQSTGEFL QVGGIHVVYD LSRKPGDRVV KLDVLCTKCR
VPSYDPLKMD EVYKVILPNF LANGGDGFQM IKDELLRHDS GDQDINVVST YISKMKVIYP
AVEGRIKFST GSHCHGSFSL IFLSLWAVIF VLYQ
