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CDAC1_MOUSE
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   03-AUG-2022, entry version 128.
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. [Q8BMD5-1]
DR   AlphaFoldDB; Q8BMD5; -.
DR   SMR; Q8BMD5; -.
DR   STRING; 10090.ENSMUSP00000128022; -.
DR   iPTMnet; Q8BMD5; -.
DR   PhosphoSitePlus; Q8BMD5; -.
DR   MaxQB; Q8BMD5; -.
DR   PaxDb; Q8BMD5; -.
DR   PRIDE; Q8BMD5; -.
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; 180 antibodies from 21 providers.
DR   DNASU; 71891; -.
DR   Ensembl; ENSMUST00000022555; ENSMUSP00000022555; ENSMUSG00000021982. [Q8BMD5-2]
DR   Ensembl; ENSMUST00000056997; ENSMUSP00000052233; ENSMUSG00000021982. [Q8BMD5-1]
DR   Ensembl; ENSMUST00000167100; ENSMUSP00000128022; ENSMUSG00000021982. [Q8BMD5-3]
DR   Ensembl; ENSMUST00000171683; ENSMUSP00000128064; ENSMUSG00000021982. [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   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; 1569973at2759; -.
DR   PhylomeDB; Q8BMD5; -.
DR   BioGRID-ORCS; 71891; 2 hits in 72 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 248 other 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   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; PTHR11086; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 2.
DR   SUPFAM; SSF53927; SSF53927; 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
 
 
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