5NT1A_HUMAN
ID 5NT1A_HUMAN Reviewed; 368 AA.
AC Q9BXI3; Q3SYB9; Q5TG98; Q9BWT8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytosolic 5'-nucleotidase 1A;
DE Short=cN1A;
DE EC=3.1.3.5 {ECO:0000269|PubMed:11133996};
DE AltName: Full=Cytosolic 5'-nucleotidase IA;
DE Short=cN-I;
DE Short=cN-IA;
GN Name=NT5C1A;
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=11133996; DOI=10.1074/jbc.m011218200;
RA Hunsucker S.A., Spychala J., Mitchell B.S.;
RT "Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside
RT analog resistance.";
RL J. Biol. Chem. 276:10498-10504(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Lowenstein J.M., Huang J., Steiner A.;
RT "5'-nucleotidase I from human heart.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of
CC deoxyribonucleotides and has a broad substrate specificity. Helps to
CC regulate adenosine levels in heart during ischemia and hypoxia.
CC {ECO:0000269|PubMed:11133996}.
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 Evidence={ECO:0000269|PubMed:11133996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by ADP. {ECO:0000269|PubMed:11133996}.
CC -!- INTERACTION:
CC Q9BXI3; Q16543: CDC37; NbExp=3; IntAct=EBI-10441581, EBI-295634;
CC Q9BXI3; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-10441581, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Detected at
CC intermediate levels in heart, brain, kidney and pancreas.
CC {ECO:0000269|PubMed:11133996}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase type 3 family.
CC {ECO:0000305}.
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DR EMBL; AF331801; AAK01294.1; -; mRNA.
DR EMBL; AY028778; AAK30000.1; -; mRNA.
DR EMBL; AL035404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103879; AAI03880.1; -; mRNA.
DR EMBL; BC103880; AAI03881.1; -; mRNA.
DR CCDS; CCDS440.1; -.
DR RefSeq; NP_115915.1; NM_032526.2.
DR AlphaFoldDB; Q9BXI3; -.
DR BioGRID; 124149; 31.
DR IntAct; Q9BXI3; 5.
DR STRING; 9606.ENSP00000235628; -.
DR DEPOD; NT5C1A; -.
DR iPTMnet; Q9BXI3; -.
DR PhosphoSitePlus; Q9BXI3; -.
DR BioMuta; NT5C1A; -.
DR DMDM; 47116736; -.
DR MassIVE; Q9BXI3; -.
DR PaxDb; Q9BXI3; -.
DR PeptideAtlas; Q9BXI3; -.
DR PRIDE; Q9BXI3; -.
DR ProteomicsDB; 79426; -.
DR Antibodypedia; 54865; 207 antibodies from 25 providers.
DR DNASU; 84618; -.
DR Ensembl; ENST00000235628.2; ENSP00000235628.1; ENSG00000116981.4.
DR GeneID; 84618; -.
DR KEGG; hsa:84618; -.
DR MANE-Select; ENST00000235628.2; ENSP00000235628.1; NM_032526.3; NP_115915.1.
DR UCSC; uc001cdq.1; human.
DR CTD; 84618; -.
DR DisGeNET; 84618; -.
DR GeneCards; NT5C1A; -.
DR HGNC; HGNC:17819; NT5C1A.
DR HPA; ENSG00000116981; Group enriched (skeletal muscle, tongue).
DR MIM; 610525; gene.
DR neXtProt; NX_Q9BXI3; -.
DR OpenTargets; ENSG00000116981; -.
DR PharmGKB; PA31799; -.
DR VEuPathDB; HostDB:ENSG00000116981; -.
DR eggNOG; ENOG502QRJF; Eukaryota.
DR GeneTree; ENSGT00390000017767; -.
DR HOGENOM; CLU_060123_0_0_1; -.
DR OMA; IRTLMAW; -.
DR OrthoDB; 694318at2759; -.
DR PhylomeDB; Q9BXI3; -.
DR TreeFam; TF329831; -.
DR BioCyc; MetaCyc:HS04074-MON; -.
DR BRENDA; 3.1.3.5; 2681.
DR PathwayCommons; Q9BXI3; -.
DR Reactome; R-HSA-73621; Pyrimidine catabolism.
DR Reactome; R-HSA-74259; Purine catabolism.
DR SABIO-RK; Q9BXI3; -.
DR SignaLink; Q9BXI3; -.
DR BioGRID-ORCS; 84618; 8 hits in 1073 CRISPR screens.
DR GenomeRNAi; 84618; -.
DR Pharos; Q9BXI3; Tbio.
DR PRO; PR:Q9BXI3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BXI3; protein.
DR Bgee; ENSG00000116981; Expressed in gastrocnemius and 83 other tissues.
DR Genevisible; Q9BXI3; HS.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0046085; P:adenosine metabolic process; IBA:GO_Central.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006196; P:AMP catabolic process; IDA:MGI.
DR GO; GO:0046059; P:dAMP catabolic process; IDA:MGI.
DR GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR GO; GO:0006204; P:IMP catabolic process; IDA:MGI.
DR GO; GO:0009116; P:nucleoside metabolic process; NAS:UniProtKB.
DR InterPro; IPR010394; 5-nucleotidase.
DR PANTHER; PTHR31367; PTHR31367; 1.
DR Pfam; PF06189; 5-nucleotidase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..368
FT /note="Cytosolic 5'-nucleotidase 1A"
FT /id="PRO_0000144795"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 9..11
FT /note="Missing (in Ref. 2; AAK30000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41021 MW; 7FB3CCEED50BA50D CRC64;
MEPGQPREPQ EPREPGPGAE TAAAPVWEEA KIFYDNLAPK KKPKSPKPQN AVTIAVSSRA
LFRMDEEQQI YTEQGVEEYV RYQLEHENEP FSPGPAFPFV KALEAVNRRL RELYPDSEDV
FDIVLMTNNH AQVGVRLINS INHYDLFIER FCMTGGNSPI CYLKAYHTNL YLSADAEKVR
EAIDEGIAAA TIFSPSRDVV VSQSQLRVAF DGDAVLFSDE SERIVKAHGL DRFFEHEKAH
ENKPLAQGPL KGFLEALGRL QKKFYSKGLR LECPIRTYLV TARSAASSGA RALKTLRSWG
LETDEALFLA GAPKGPLLEK IRPHIFFDDQ MFHVAGAQEM GTVAAHVPYG VAQTPRRTAP
AKQAPSAQ
