ID   CCD25_PONAB             Reviewed;         208 AA.
AC   Q5R9S1; Q5R842;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Coiled-coil domain-containing protein 25 {ECO:0000305};
GN   Name=CCDC25 {ECO:0000250|UniProtKB:Q86WR0};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Formation of NETs is
CC       also associated with cancer metastasis, NET-DNA acting as a chemotactic
CC       factor to attract cancer cells. Specifically binds NETs on its
CC       extracellular region, in particular the 8-OHdG-enriched DNA present in
CC       NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce
CC       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; CR859311; CAH91489.1; -; mRNA.
DR   EMBL; CR859912; CAH92068.1; -; mRNA.
DR   RefSeq; NP_001126204.1; NM_001132732.1.
DR   AlphaFoldDB; Q5R9S1; -.
DR   SMR; Q5R9S1; -.
DR   STRING; 9601.ENSPPYP00000020698; -.
DR   GeneID; 100173172; -.
DR   KEGG; pon:100173172; -.
DR   CTD; 55246; -.
DR   eggNOG; KOG3272; Eukaryota.
DR   HOGENOM; CLU_076656_0_1_1; -.
DR   InParanoid; Q5R9S1; -.
DR   OMA; DVWFHVH; -.
DR   OrthoDB; 1380409at2759; -.
DR   TreeFam; TF300013; -.
DR   Proteomes; UP000001595; Chromosome 8.
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   2: Evidence at transcript 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_0000233406"
FT   TOPO_DOM        1..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        67..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          21..25
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q86WR0"
FT   REGION          147..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          117..187
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        147..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:0000250|UniProtKB:Q86WR0"
FT   CONFLICT        46
FT                   /note="S -> P (in Ref. 1; CAH91489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="K -> R (in Ref. 1; CAH92068)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  24507 MW;  9066DC12D84494B6 CRC64;
     MVFYFTSSSV NSSAYTIYMG KDKYENEDLI KHGWPEDIWF HVDKLSSAHV YLRLHKGENI
     EDIPKEVLMD CAHLVKANSI QGCKMNNVNV VYTPWSNLKK TADMDVGQIG FHRQKDVKIV
     TVEKKVNEIL NRLEKTKVER FPDLAAEKEC RDREERNEKK AQIQEMKRRE KEEMKKKREM
     DELRSYSSLM KVENMSSNQD GNDSDEFM