CCD25_DANRE
ID CCD25_DANRE Reviewed; 207 AA.
AC Q7T312;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Coiled-coil domain-containing protein 25 {ECO:0000305};
GN Name=ccdc25 {ECO:0000250|UniProtKB:Q86WR0};
GN ORFNames=zgc:64173 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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. Specifically binds
CC NETs on its extracellular region, in particular the 8-OHdG-enriched DNA
CC present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to
CC induce cytoskeleton rearrangement and directional migration of cells.
CC {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 -!- SIMILARITY: Belongs to the CCDC25 family. {ECO:0000305}.
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DR EMBL; AL845306; CAI20930.1; -; Genomic_DNA.
DR EMBL; BC053297; AAH53297.1; -; mRNA.
DR RefSeq; NP_956682.1; NM_200388.1.
DR AlphaFoldDB; Q7T312; -.
DR SMR; Q7T312; -.
DR STRING; 7955.ENSDARP00000030117; -.
DR iPTMnet; Q7T312; -.
DR PaxDb; Q7T312; -.
DR PRIDE; Q7T312; -.
DR Ensembl; ENSDART00000037282; ENSDARP00000030117; ENSDARG00000021753.
DR GeneID; 393359; -.
DR KEGG; dre:393359; -.
DR CTD; 55246; -.
DR ZFIN; ZDB-GENE-040426-1389; ccdc25.
DR eggNOG; KOG3272; Eukaryota.
DR GeneTree; ENSGT00390000004380; -.
DR HOGENOM; CLU_076656_0_1_1; -.
DR InParanoid; Q7T312; -.
DR OMA; DVWFHVH; -.
DR OrthoDB; 1380409at2759; -.
DR PhylomeDB; Q7T312; -.
DR TreeFam; TF300013; -.
DR PRO; PR:Q7T312; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000021753; Expressed in spleen and 28 other tissues.
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 Cell membrane; Coiled coil; DNA-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="Coiled-coil domain-containing protein 25"
FT /id="PRO_0000233407"
FT TOPO_DOM 1..104
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 20..24
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86WR0"
FT REGION 140..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..189
FT /evidence="ECO:0000255"
FT COMPBIAS 140..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 207 AA; 24380 MW; F523402BB308A014 CRC64;
MVFYFTSAVV SPPHTIYMGK DKYENEDLIK YGWPEDIWFH VDKLSSAHVY LRMPKGTTID
DIPKEVLIDC VQLVKNNSIQ GCKMNNINIV YTPWSNLKKT ADMDIGQIGF HRQKEVKIVA
VEKKINEIVN RLEKTKEERY PDLAAEKESR DREERNEKKA QIQEQKKKEK EEVKKKKEME
DLKNYTSLMK SDNMTTNEDG YDSDDFM
