CMPK2_MOUSE
ID CMPK2_MOUSE Reviewed; 447 AA.
AC Q3U5Q7; Q3UCI7; Q5XKG5; Q62316; Q6PFG7; Q9DC34;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=UMP-CMP kinase 2, mitochondrial;
DE EC=2.7.4.14;
DE AltName: Full=Nucleoside-diphosphate kinase;
DE EC=2.7.4.6;
DE AltName: Full=Thymidylate kinase LPS-inducible member;
DE Short=TYKi;
DE Flags: Precursor;
GN Name=Cmpk2; Synonyms=Tyki;
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=Bone marrow, and Lung;
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 STRAIN=C57BL/6J, and Czech II; 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).
RN [3]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=7751651;
RA Lee C.G.L., O'Brien W.E.;
RT "A unique member of the thymidylate kinase family that is induced during
RT macrophage activation.";
RL J. Immunol. 154:6094-6102(1995).
RN [4]
RP INDUCTION.
RX PubMed=16996144; DOI=10.1016/j.jneuroim.2006.07.007;
RA Lund S., Christensen K.V., Hedtjarn M., Mortensen A.L., Hagberg H.,
RA Falsig J., Hasseldam H., Schrattenholz A., Poerzgen P., Leist M.;
RT "The dynamics of the LPS triggered inflammatory response of murine
RT microglia under different culture and in vivo conditions.";
RL J. Neuroimmunol. 180:71-87(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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).
CC -!- FUNCTION: May participate in dUTP and dCTP synthesis in mitochondria.
CC Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the
CC pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP
CC as phosphate donor. Also displays broad nucleoside diphosphate kinase
CC activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.14;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.14;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- INDUCTION: By lipopolysaccharides in macrophages and in primary
CC microglia. {ECO:0000269|PubMed:16996144, ECO:0000269|PubMed:7751651}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58770.1; Type=Miscellaneous discrepancy; Note=Sequence differs due to frameshifts, sequencing errors and other discrepancies.; Evidence={ECO:0000305};
CC Sequence=AAH27329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH57565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23396.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE29625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE29646.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE29803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE29932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK004595; BAB23396.1; ALT_FRAME; mRNA.
DR EMBL; AK153469; BAE32020.1; -; mRNA.
DR EMBL; AK150512; BAE29625.1; ALT_INIT; mRNA.
DR EMBL; AK150543; BAE29646.1; ALT_INIT; mRNA.
DR EMBL; AK150725; BAE29803.1; ALT_INIT; mRNA.
DR EMBL; AK150885; BAE29932.1; ALT_INIT; mRNA.
DR EMBL; AK153429; BAE31987.1; ALT_INIT; mRNA.
DR EMBL; BC027329; AAH27329.1; ALT_INIT; mRNA.
DR EMBL; BC057565; AAH57565.1; ALT_INIT; mRNA.
DR EMBL; L32973; AAA58770.1; ALT_SEQ; mRNA.
DR CCDS; CCDS49039.1; -.
DR RefSeq; NP_065582.3; NM_020557.4.
DR AlphaFoldDB; Q3U5Q7; -.
DR SMR; Q3U5Q7; -.
DR STRING; 10090.ENSMUSP00000020969; -.
DR iPTMnet; Q3U5Q7; -.
DR PhosphoSitePlus; Q3U5Q7; -.
DR SwissPalm; Q3U5Q7; -.
DR EPD; Q3U5Q7; -.
DR jPOST; Q3U5Q7; -.
DR MaxQB; Q3U5Q7; -.
DR PaxDb; Q3U5Q7; -.
DR PeptideAtlas; Q3U5Q7; -.
DR PRIDE; Q3U5Q7; -.
DR ProteomicsDB; 285502; -.
DR Antibodypedia; 26409; 87 antibodies from 21 providers.
DR DNASU; 22169; -.
DR Ensembl; ENSMUST00000020969; ENSMUSP00000020969; ENSMUSG00000020638.
DR GeneID; 22169; -.
DR KEGG; mmu:22169; -.
DR UCSC; uc007nfj.1; mouse.
DR CTD; 129607; -.
DR MGI; MGI:99830; Cmpk2.
DR VEuPathDB; HostDB:ENSMUSG00000020638; -.
DR eggNOG; KOG3327; Eukaryota.
DR GeneTree; ENSGT00940000154030; -.
DR HOGENOM; CLU_049896_0_0_1; -.
DR InParanoid; Q3U5Q7; -.
DR OMA; MAPPRCF; -.
DR OrthoDB; 1450196at2759; -.
DR PhylomeDB; Q3U5Q7; -.
DR TreeFam; TF328875; -.
DR BioGRID-ORCS; 22169; 0 hits in 70 CRISPR screens.
DR PRO; PR:Q3U5Q7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q3U5Q7; protein.
DR Bgee; ENSMUSG00000020638; Expressed in small intestine Peyer's patch and 236 other tissues.
DR Genevisible; Q3U5Q7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; ISO:MGI.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0004798; F:thymidylate kinase activity; ISO:MGI.
DR GO; GO:0033862; F:UMP kinase activity; ISO:MGI.
DR GO; GO:0009041; F:uridylate kinase activity; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006233; P:dTDP biosynthetic process; ISO:MGI.
DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006227; P:dUDP biosynthetic process; ISO:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR014505; UMP-CMP_kinase_2.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR PIRSF; PIRSF019736; dTMP_TKRP1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Mitochondrion; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..447
FT /note="UMP-CMP kinase 2, mitochondrial"
FT /id="PRO_0000331525"
FT COILED 380..412
FT /evidence="ECO:0000255"
FT BINDING 259..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="G -> R (in Ref. 1; BAE29625)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> K (in Ref. 1; BAE32020)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="E -> G (in Ref. 1; BAE32020)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> G (in Ref. 1; BAE29625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50036 MW; 37CBACA251A40CFC CRC64;
MALISRPRAP LWLGRLSRRL CGRHQACMGT MARPRRFTVE LPDCSLTHFV LGDATDHRDA
RLAELLGPPG RSYALCVPLA PGEGCGPRVQ AARVHHRLLQ QLRRGPLQRC QLSKLLGYGP
GDQAGEAQHG FLLRDPCDHP DTRRDLLQLL GSCQEAARPQ LAEFQADSQG LLWQRLWELQ
GDRQVQVDCA CVLPAQEPHL HPLLPDLLNS AVFQDRDAAR AVLEECTSFI PEARAVLDLV
DQCPKEVQKG KFQVIAIEGL DATGKTTLTQ SVSESLKAVL LQSPPPCISQ WRKIFDDEPT
IIRRAFYSLG NYLVASEIAK ESTNFPVIVD RYWHSTATYA IATEVSGGLQ YLPPAHHPVY
QWPGDLLKPD LVLLLTVNSE ERVRRLQGRG QEKTKEEAEL EANNVFRQKV EMTYQRMENP
SCHLVDASPS RETVLQKVLE LIQSSGR
