CCD25_MOUSE
ID CCD25_MOUSE Reviewed; 208 AA.
AC Q78PG9; Q9CSQ8; Q9CUF8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Coiled-coil domain-containing protein 25 {ECO:0000305};
GN Name=Ccdc25 {ECO:0000312|MGI:MGI:1914429};
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=Cerebellum, and Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and 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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=32528174; DOI=10.1038/s41586-020-2394-6;
RA Yang L., Liu Q., Zhang X., Liu X., Zhou B., Chen J., Huang D., Li J.,
RA Li H., Chen F., Liu J., Xing Y., Chen X., Su S., Song E.;
RT "DNA of neutrophil extracellular traps promotes cancer metastasis via
RT CCDC25.";
RL Nature 583:133-138(2020).
CC -!- FUNCTION: Transmembrane receptor that senses neutrophil extracellular
CC traps (NETs) and triggers the ILK-PARVB pathway to enhance cell
CC motility. NETs are mainly composed of DNA fibers and are released by
CC neutrophils to bind pathogens during inflammation (By similarity).
CC Formation of NETs is also associated with cancer metastasis, NET-DNA
CC acting as a chemotactic factor to attract cancer cells (By similarity).
CC Specifically binds NETs on its extracellular region, in particular the
CC 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the
CC ILK-PARVB cascade to induce cytoskeleton rearrangement and directional
CC migration of cells (By similarity). In the context of cancer, promotes
CC cancer metastasis by sensing NETs and promoting migration of tumor
CC cells (By similarity). {ECO:0000250|UniProtKB:Q86WR0}.
CC -!- SUBUNIT: Interacts (via cytoplasmic region) with ILK.
CC {ECO:0000250|UniProtKB:Q86WR0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WR0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q86WR0}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q86WR0}. Note=Localizes to
CC cytoplasmic membrane in tumor cells. {ECO:0000250|UniProtKB:Q86WR0}.
CC -!- DISRUPTION PHENOTYPE: In the context of cancer, mice display reduced
CC metastase formation, without affecting primary tumor growth.
CC {ECO:0000269|PubMed:32528174}.
CC -!- SIMILARITY: Belongs to the CCDC25 family. {ECO:0000305}.
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DR EMBL; AK012172; BAB28076.1; -; mRNA.
DR EMBL; AK016286; BAB30178.1; -; mRNA.
DR EMBL; AK078345; BAC37230.1; -; mRNA.
DR EMBL; AK089982; BAC41026.1; -; mRNA.
DR CCDS; CCDS27217.1; -.
DR RefSeq; NP_666056.1; NM_145944.4.
DR AlphaFoldDB; Q78PG9; -.
DR SMR; Q78PG9; -.
DR IntAct; Q78PG9; 1.
DR MINT; Q78PG9; -.
DR STRING; 10090.ENSMUSP00000022614; -.
DR iPTMnet; Q78PG9; -.
DR PhosphoSitePlus; Q78PG9; -.
DR CPTAC; non-CPTAC-3776; -.
DR EPD; Q78PG9; -.
DR MaxQB; Q78PG9; -.
DR PaxDb; Q78PG9; -.
DR PRIDE; Q78PG9; -.
DR ProteomicsDB; 281497; -.
DR Antibodypedia; 10313; 95 antibodies from 23 providers.
DR Ensembl; ENSMUST00000022614; ENSMUSP00000022614; ENSMUSG00000022035.
DR GeneID; 67179; -.
DR KEGG; mmu:67179; -.
DR UCSC; uc007ujq.1; mouse.
DR CTD; 55246; -.
DR MGI; MGI:1914429; Ccdc25.
DR VEuPathDB; HostDB:ENSMUSG00000022035; -.
DR eggNOG; KOG3272; Eukaryota.
DR GeneTree; ENSGT00390000004380; -.
DR HOGENOM; CLU_076656_0_1_1; -.
DR InParanoid; Q78PG9; -.
DR OMA; DVWFHVH; -.
DR OrthoDB; 1380409at2759; -.
DR PhylomeDB; Q78PG9; -.
DR TreeFam; TF300013; -.
DR BioGRID-ORCS; 67179; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Ccdc25; mouse.
DR PRO; PR:Q78PG9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q78PG9; protein.
DR Bgee; ENSMUSG00000022035; Expressed in jejunum and 61 other tissues.
DR ExpressionAtlas; Q78PG9; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR InterPro; IPR039730; Jlp2/Ccd25.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR PANTHER; PTHR13049; PTHR13049; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; DNA-binding; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..208
FT /note="Coiled-coil domain-containing protein 25"
FT /id="PRO_0000233405"
FT TOPO_DOM 1..105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 21..25
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86WR0"
FT REGION 144..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..187
FT /evidence="ECO:0000255"
FT COMPBIAS 144..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86WR0"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 156
FT /note="R -> G (in Ref. 1; BAB30178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 24480 MW; 60FF54684E72337F CRC64;
MVFYFTSSSV NSSTYTIYMG KDKYENEDLI KYGWPEDIWF HVDKLSSAHV YLRLQKGEKI
EDIPKEVLMD CAHLVKANSI QGCKMNNVNV VYTPWSNLKK TADMDVGQIG FHRQKDVKIV
TVEKKVNEIL NRLEKTKLEK FPDLAAEKEG RDREERNEKK AQIQEMKRKE KEEMKKKREM
DELRSYSSLM KVENMSSNQD GNDSDEFM
