ID CDAC1_MOUSE Reviewed; 523 AA.
AC Q8BMD5; Q8BYL2; Q8BYN1; Q8C014; Q922P4; Q99KL2; Q9D7F3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Cytidine and dCMP deaminase domain-containing protein 1;
DE EC=3.5.4.5 {ECO:0000250|UniProtKB:Q9BWV3};
DE AltName: Full=Cytidine deaminase {ECO:0000305};
GN Name=Cdadc1;
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] (ISOFORMS 1; 3; 4 AND 6).
RC STRAIN=C57BL/6J;
RC TISSUE=Hypothalamus, Olfactory bulb, Tongue, and Wolffian duct;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 289-523 (ISOFORM 4).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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: Catalyzes the deamination of cytidine and deoxycytidine into
CC uridine and deoxyuridine, respectively. May play an important role in
CC testicular development and spermatogenesis.
CC {ECO:0000250|UniProtKB:Q9BWV3}.
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 Evidence={ECO:0000250|UniProtKB:Q9BWV3};
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 Evidence={ECO:0000250|UniProtKB:Q9BWV3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9GZX7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BWV3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BWV3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BMD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMD5-2; Sequence=VSP_027820, VSP_027823;
CC Name=3;
CC IsoId=Q8BMD5-3; Sequence=VSP_027821, VSP_027822;
CC Name=4;
CC IsoId=Q8BMD5-4; Sequence=VSP_027819, VSP_027824;
CC Name=6;
CC IsoId=Q8BMD5-6; Sequence=VSP_027817, VSP_027818;
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26191.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009280; BAB26191.1; ALT_FRAME; mRNA.
DR EMBL; AK032600; BAC27943.1; -; mRNA.
DR EMBL; AK032813; BAC28036.1; -; mRNA.
DR EMBL; AK038926; BAC30171.1; -; mRNA.
DR EMBL; AK039148; BAC30255.1; -; mRNA.
DR EMBL; BC004588; AAH04588.1; -; mRNA.
DR EMBL; BC006901; AAH06901.1; -; mRNA.
DR CCDS; CCDS36940.1; -. [Q8BMD5-1]
DR CCDS; CCDS49513.1; -. [Q8BMD5-2]
DR CCDS; CCDS49515.1; -. [Q8BMD5-4]
DR CCDS; CCDS88678.1; -. [Q8BMD5-3]
DR RefSeq; NP_001162007.1; NM_001168535.1.
DR RefSeq; NP_001162008.1; NM_001168536.1. [Q8BMD5-4]
DR RefSeq; NP_001162009.1; NM_001168537.1. [Q8BMD5-2]
DR RefSeq; NP_001162010.1; NM_001168538.1. [Q8BMD5-3]
DR RefSeq; NP_082262.1; NM_027986.3. [Q8BMD5-1]
DR RefSeq; XP_017171695.1; XM_017316206.1.
DR AlphaFoldDB; Q8BMD5; -.
DR SMR; Q8BMD5; -.
DR STRING; 10090.ENSMUSP00000153357; -.
DR iPTMnet; Q8BMD5; -.
DR PhosphoSitePlus; Q8BMD5; -.
DR MaxQB; Q8BMD5; -.
DR PaxDb; 10090-ENSMUSP00000128022; -.
DR ProteomicsDB; 283755; -. [Q8BMD5-1]
DR ProteomicsDB; 283756; -. [Q8BMD5-2]
DR ProteomicsDB; 283757; -. [Q8BMD5-3]
DR ProteomicsDB; 283758; -. [Q8BMD5-4]
DR ProteomicsDB; 283759; -. [Q8BMD5-6]
DR Antibodypedia; 23898; 188 antibodies from 21 providers.
DR DNASU; 71891; -.
DR Ensembl; ENSMUST00000022555.11; ENSMUSP00000022555.4; ENSMUSG00000021982.15. [Q8BMD5-2]
DR Ensembl; ENSMUST00000056997.15; ENSMUSP00000052233.8; ENSMUSG00000021982.15. [Q8BMD5-1]
DR Ensembl; ENSMUST00000167100.9; ENSMUSP00000128022.3; ENSMUSG00000021982.15. [Q8BMD5-3]
DR Ensembl; ENSMUST00000171683.3; ENSMUSP00000128064.2; ENSMUSG00000021982.15. [Q8BMD5-4]
DR GeneID; 71891; -.
DR KEGG; mmu:71891; -.
DR UCSC; uc007ueo.2; mouse. [Q8BMD5-1]
DR UCSC; uc007uep.2; mouse. [Q8BMD5-4]
DR UCSC; uc011zmw.1; mouse. [Q8BMD5-3]
DR UCSC; uc011zmx.1; mouse. [Q8BMD5-2]
DR AGR; MGI:1919141; -.
DR CTD; 81602; -.
DR MGI; MGI:1919141; Cdadc1.
DR VEuPathDB; HostDB:ENSMUSG00000021982; -.
DR eggNOG; KOG3127; Eukaryota.
DR GeneTree; ENSGT00940000153676; -.
DR HOGENOM; CLU_038832_1_0_1; -.
DR InParanoid; Q8BMD5; -.
DR OrthoDB; 2911935at2759; -.
DR PhylomeDB; Q8BMD5; -.
DR BioGRID-ORCS; 71891; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Cdadc1; mouse.
DR PRO; PR:Q8BMD5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BMD5; Protein.
DR Bgee; ENSMUSG00000021982; Expressed in supraoptic nucleus and 251 other cell types or tissues.
DR ExpressionAtlas; Q8BMD5; baseline and differential.
DR Genevisible; Q8BMD5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004126; F:cytidine deaminase activity; ISO:MGI.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0009972; P:cytidine deamination; ISO:MGI.
DR GO; GO:0070383; P:DNA cytosine deamination; ISO:MGI.
DR CDD; cd01286; deoxycytidylate_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 2.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..523
FT /note="Cytidine and dCMP deaminase domain-containing
FT protein 1"
FT /id="PRO_0000300493"
FT DOMAIN 71..169
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 318..483
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..284
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BWV3"
FT MOTIF 489..511
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BWV3"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027817"
FT VAR_SEQ 480..523
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027818"
FT VAR_SEQ 492..500
FT /note="NGVLRRRSA -> KHLSIKRSH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027819"
FT VAR_SEQ 492..499
FT /note="NGVLRRRS -> RSATTACF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027820"
FT VAR_SEQ 492..497
FT /note="NGVLRR -> SFFFMP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027821"
FT VAR_SEQ 498..523
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027822"
FT VAR_SEQ 500..523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027823"
FT VAR_SEQ 501..523
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027824"
FT CONFLICT 252
FT /note="H -> R (in Ref. 1; BAC30171)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..312
FT /note="IHN -> VHS (in Ref. 2; AAH04588)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="R -> H (in Ref. 1; BAC30171 and 2; AAH04588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59062 MW; 49E525840EE7B274 CRC64;
MKETDQMQSL EGSGAERSVG TQTGSMTGQI PRLSKVNLFT LLSLWMELFP GVEAQGQKSQ
KTEEESRGPL GDNEELTRVS TEKKQVKKTG LVVVKNMKII GLHCSSEDLH TGQIALIKHG
SRLKNCDLYF SRKPCSACLK MIVNAGVNRI SYWPSDPEIS LLTEASSSED AKLDAKAAER
LKSNSRAHVC VLLQPLVCYM VQFVEETSYK CDFIQKTAKA LPGADTDFYS ECKQERIKEY
EMLFLVSNEE RHKQILMTIG LESLCEDPYF SNLRQNMKDL ILLLATVASS VPNLKHFGFY
CSSPEQINEI HNQSLPQEVA RHCMVQARLL AYRTEDHKTG VGAVIWAEAK SRSCDGTGAM
YFIGCGYNAF PVGSEYADFP HMDDKHKDRE IRKFRYIIHA EQNALTFRCQ DIKPEERSMI
FVTKCPCDEC VPLIKGAGIK QIYAGDVDVG KKKADISYMK FGELEGVRKF TWQLNPSEAY
SLDPNEPERR ENGVLRRRSA KDEQRSSKRP RLETRSAGRA TLQ
//
