ID   CDD_MOUSE               Reviewed;         146 AA.
AC   P56389; Q9D7V3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=Cytidine deaminase;
DE            EC=3.5.4.5;
DE   AltName: Full=Cytidine aminohydrolase;
GN   Name=Cda; Synonyms=Cdd;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Liver;
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).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH CYTIDINE, SUBUNIT,
RP   COFACTOR, ACTIVE SITE, SUBSTRATE-BINDING REGION, AND ZINC-BINDING SITES.
RX   PubMed=16784234; DOI=10.1021/bi060345f;
RA   Teh A.H., Kimura M., Yamamoto M., Tanaka N., Yamaguchi I., Kumasaka T.;
RT   "The 1.48 A resolution crystal structure of the homotetrameric cytidine
RT   deaminase from mouse.";
RL   Biochemistry 45:7825-7833(2006).
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC       2'-deoxycytidine for UMP synthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC         Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC         Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16784234};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16784234}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; AK008793; BAB25898.1; -; mRNA.
DR   EMBL; BC050114; AAH50114.1; -; mRNA.
DR   CCDS; CCDS18826.1; -.
DR   RefSeq; NP_082452.1; NM_028176.1.
DR   PDB; 1ZAB; X-ray; 2.36 A; A/B/C/D=1-146.
DR   PDB; 2FR5; X-ray; 1.48 A; A/B/C/D=1-146.
DR   PDB; 2FR6; X-ray; 2.07 A; A/B/C/D=1-146.
DR   PDBsum; 1ZAB; -.
DR   PDBsum; 2FR5; -.
DR   PDBsum; 2FR6; -.
DR   AlphaFoldDB; P56389; -.
DR   SMR; P56389; -.
DR   BioGRID; 215267; 4.
DR   IntAct; P56389; 1.
DR   MINT; P56389; -.
DR   STRING; 10090.ENSMUSP00000030535; -.
DR   BindingDB; P56389; -.
DR   ChEMBL; CHEMBL2110; -.
DR   iPTMnet; P56389; -.
DR   PhosphoSitePlus; P56389; -.
DR   jPOST; P56389; -.
DR   MaxQB; P56389; -.
DR   PaxDb; 10090-ENSMUSP00000030535; -.
DR   PeptideAtlas; P56389; -.
DR   ProteomicsDB; 281351; -.
DR   Pumba; P56389; -.
DR   Antibodypedia; 29806; 348 antibodies from 30 providers.
DR   DNASU; 72269; -.
DR   Ensembl; ENSMUST00000030535.4; ENSMUSP00000030535.4; ENSMUSG00000028755.4.
DR   GeneID; 72269; -.
DR   KEGG; mmu:72269; -.
DR   UCSC; uc008vkw.1; mouse.
DR   AGR; MGI:1919519; -.
DR   CTD; 978; -.
DR   MGI; MGI:1919519; Cda.
DR   VEuPathDB; HostDB:ENSMUSG00000028755; -.
DR   eggNOG; KOG0833; Eukaryota.
DR   GeneTree; ENSGT00390000000911; -.
DR   HOGENOM; CLU_097262_1_2_1; -.
DR   InParanoid; P56389; -.
DR   OMA; LTHFTCV; -.
DR   OrthoDB; 102874at2759; -.
DR   PhylomeDB; P56389; -.
DR   TreeFam; TF314486; -.
DR   BRENDA; 3.5.4.5; 3474.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-73614; Pyrimidine salvage.
DR   BioGRID-ORCS; 72269; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Cda; mouse.
DR   EvolutionaryTrace; P56389; -.
DR   PRO; PR:P56389; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P56389; Protein.
DR   Bgee; ENSMUSG00000028755; Expressed in right kidney and 86 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0004126; F:cytidine deaminase activity; IDA:MGI.
DR   GO; GO:0019239; F:deaminase activity; ISO:MGI.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0001882; F:nucleoside binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071217; P:cellular response to external biotic stimulus; IEA:Ensembl.
DR   GO; GO:0006248; P:CMP catabolic process; ISO:MGI.
DR   GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
DR   GO; GO:0006249; P:dCMP catabolic process; ISO:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0045980; P:negative regulation of nucleotide metabolic process; ISS:UniProtKB.
DR   GO; GO:0046898; P:response to cycloheximide; IEA:Ensembl.
DR   GO; GO:0044206; P:UMP salvage; IDA:MGI.
DR   CDD; cd01283; cytidine_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   NCBIfam; TIGR01354; cyt_deam_tetra; 1.
DR   PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR   PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
DR   Genevisible; P56389; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..146
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000171683"
FT   DOMAIN          13..140
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        67
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:16784234"
FT   BINDING         54..56
FT                   /ligand="substrate"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   HELIX           13..26
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   HELIX           100..108
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:2FR5"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:2FR5"
SQ   SEQUENCE   146 AA;  16131 MW;  D4181CE6BA9CD794 CRC64;
     MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF SGCNIENACY
     PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG ACRQVMREFG TDWAVYMTKP
     DGTFVVRTVQ ELLPASFGPE DLQKIQ
//