LOCUS       NM_001785                809 bp    mRNA    linear   PRI 01-AUG-2024
DEFINITION  Homo sapiens cytidine deaminase (CDA), mRNA.
ACCESSION   NM_001785
VERSION     NM_001785.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 809)
  AUTHORS   Lumeau,A., Bery,N., Frances,A., Gayral,M., Labrousse,G.,
            Ribeyre,C., Lopez,C., Nevot,A., El Kaoutari,A., Hanoun,N.,
            Sarot,E., Perrier,M., Pont,F., Cerapio,J.P., Fournie,J.J.,
            Lopez,F., Madrid-Mencia,M., Pancaldi,V., Pillaire,M.J.,
            Bergoglio,V., Torrisani,J., Dusetti,N., Hoffmann,J.S., Buscail,L.,
            Lutzmann,M. and Cordelier,P.
  TITLE     Cytidine Deaminase Resolves Replicative Stress and Protects
            Pancreatic Cancer from DNA-Targeting Drugs
  JOURNAL   Cancer Res 84 (7), 1013-1028 (2024)
   PUBMED   38294491
  REMARK    GeneRIF: Cytidine Deaminase Resolves Replicative Stress and
            Protects Pancreatic Cancer from DNA-Targeting Drugs.
REFERENCE   2  (bases 1 to 809)
  AUTHORS   Hong,K.U., Tagnedji,A.H., Doll,M.A., Walls,K.M. and Hein,D.W.
  TITLE     Upregulation of cytidine deaminase in NAT1 knockout breast cancer
            cells
  JOURNAL   J Cancer Res Clin Oncol 149 (8), 5047-5060 (2023)
   PUBMED   36329350
  REMARK    GeneRIF: Upregulation of cytidine deaminase in NAT1 knockout breast
            cancer cells.
REFERENCE   3  (bases 1 to 809)
  AUTHORS   Kurup,H.M., Kvach,M.V., Harjes,S., Jameson,G.B., Harjes,E. and
            Filichev,V.V.
  TITLE     Seven-membered ring nucleobases as inhibitors of human cytidine
            deaminase and APOBEC3A
  JOURNAL   Org Biomol Chem 21 (24), 5117-5128 (2023)
   PUBMED   37282621
  REMARK    GeneRIF: Seven-membered ring nucleobases as inhibitors of human
            cytidine deaminase and APOBEC3A.
            Publication Status: Online-Only
REFERENCE   4  (bases 1 to 809)
  AUTHORS   Silveira,S.C., Buhagiar-Labarchede,G., Onclercq-Delic,R.,
            Gemble,S., Bou Samra,E., Mameri,H., Duchambon,P., Machon,C.,
            Guitton,J. and Amor-Gueret,M.
  TITLE     A decrease in NAMPT activity impairs basal PARP-1 activity in
            cytidine deaminase deficient-cells, independently of NAD
  JOURNAL   Sci Rep 10 (1), 13907 (2020)
   PUBMED   32807821
  REMARK    GeneRIF: A decrease in NAMPT activity impairs basal PARP-1 activity
            in cytidine deaminase deficient-cells, independently of NAD(.)
            Publication Status: Online-Only
REFERENCE   5  (bases 1 to 809)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (bases 1 to 809)
  AUTHORS   Gran,C., Boyum,A., Johansen,R.F., Lovhaug,D. and Seeberg,E.C.
  TITLE     Growth inhibition of granulocyte-macrophage colony-forming cells by
            human cytidine deaminase requires the catalytic function of the
            protein
  JOURNAL   Blood 91 (11), 4127-4135 (1998)
   PUBMED   9596658
REFERENCE   7  (bases 1 to 809)
  AUTHORS   Laliberte,J. and Momparler,R.L.
  TITLE     Human cytidine deaminase: purification of enzyme, cloning, and
            expression of its complementary DNA
  JOURNAL   Cancer Res 54 (20), 5401-5407 (1994)
   PUBMED   7923172
REFERENCE   8  (bases 1 to 809)
  AUTHORS   Saccone,S., Besati,C., Andreozzi,L., Della Valle,G., Garattini,E.
            and Terao,M.
  TITLE     Assignment of the human cytidine deaminase (CDA) gene to chromosome
            1 band p35-p36.2
  JOURNAL   Genomics 22 (3), 661-662 (1994)
   PUBMED   8001985
REFERENCE   9  (bases 1 to 809)
  AUTHORS   Kuhn,K., Bertling,W.M. and Emmrich,F.
  TITLE     Cloning of a functional cDNA for human cytidine deaminase (CDD) and
            its use as a marker of monocyte/macrophage differentiation
  JOURNAL   Biochem Biophys Res Commun 190 (1), 1-7 (1993)
   PUBMED   8422236
REFERENCE   10 (bases 1 to 809)
  AUTHORS   Wentworth,D.F. and Wolfenden,R.
  TITLE     On the interaction of 3,4,5,6-tetrahydrouridine with human liver
            cytidine deaminase
  JOURNAL   Biochemistry 14 (23), 5099-5105 (1975)
   PUBMED   53069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD675458.1 and BC054036.1.
            
            On Nov 23, 2018 this sequence version replaced NM_001785.2.
            
            Summary: This gene encodes an enzyme involved in pyrimidine
            salvaging. The encoded protein forms a homotetramer that catalyzes
            the irreversible hydrolytic deamination of cytidine and
            deoxycytidine to uridine and deoxyuridine, respectively. It is one
            of several deaminases responsible for maintaining the cellular
            pyrimidine pool. Mutations in this gene are associated with
            decreased sensitivity to the cytosine nucleoside analogue cytosine
            arabinoside used in the treatment of certain childhood leukemias.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L27943.1, BC054036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375071.4/ ENSP00000364212.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-537               CD675458.1         135-671
            538-670             BC054036.1         569-701
            671-809             BC054036.1         703-841
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     gene            1..809
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /note="cytidine deaminase"
                     /db_xref="GeneID:978"
                     /db_xref="HGNC:HGNC:1712"
                     /db_xref="MIM:123920"
     exon            1..187
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /inference="alignment:Splign:2.1.0"
     CDS             34..474
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /EC_number="3.5.4.5"
                     /note="cytidine aminohydrolase; cytosine nucleoside
                     deaminase; small cytidine deaminase"
                     /codon_start=1
                     /product="cytidine deaminase"
                     /protein_id="NP_001776.1"
                     /db_xref="CCDS:CCDS210.1"
                     /db_xref="GeneID:978"
                     /db_xref="HGNC:HGNC:1712"
                     /db_xref="MIM:123920"
                     /translation="MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLT
                     QEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGAC
                     RQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ"
     exon            188..299
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /inference="alignment:Splign:2.1.0"
     exon            300..357
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /inference="alignment:Splign:2.1.0"
     exon            358..809
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /inference="alignment:Splign:2.1.0"
     regulatory      785..790
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /note="hexamer: TATAAA"
     polyA_site      809
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /note="major polyA site"
ORIGIN      
        1 cccgctgctc tgctgcctgc ccggggtacc aacatggccc agaagcgtcc tgcctgcacc
       61 ctgaagcctg agtgtgtcca gcagctgctg gtttgctccc aggaggccaa gaagtcagcc
      121 tactgcccct acagtcactt tcctgtgggg gctgccctgc tcacccagga ggggagaatc
      181 ttcaaagggt gcaacataga aaatgcctgc tacccgctgg gcatctgtgc tgaacggacc
      241 gctatccaga aggccgtctc agaagggtac aaggatttca gggcaattgc tatcgccagt
      301 gacatgcaag atgattttat ctctccatgt ggggcctgca ggcaagtcat gagagagttt
      361 ggcaccaact ggcccgtgta catgaccaag ccggatggta cgtatattgt catgacggtc
      421 caggagctgc tgccctcctc ctttgggcct gaggacctgc agaagaccca gtgacagcca
      481 gagaatgccc actgcctgta acagccacct ggagaacttc ataaagatgt ctcacagccc
      541 tggggacacc tgcccagtgg gccccagccc tacagggact gggcaaagat gatgtttcca
      601 gattacactc cagcctgagt cagcacccct cctagcaacc tgccttggga cttagaacac
      661 cgccgccccc tgccccacct ttcctttcct tcctgtgggc cctctttcaa agtccagcct
      721 agtctggact gcttccccat cagccttccc aaggttctat cctgttccga gcaacttttc
      781 taattataaa catcacagaa catcctgga
//
