ID   CTXA_POLPP              Reviewed;         440 AA.
AC   Q9Y0T4; D3BQG3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Cortexillin-1;
DE   AltName: Full=Cortexillin I;
GN   Name=ctxA; ORFNames=PPL_10148;
OS   Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS   pallidum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC   Acytosteliaceae; Heterostelium.
OX   NCBI_TaxID=670386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26659 / Pp 5 / PN500;
RX   PubMed=10433831; DOI=10.1006/dbio.1999.9353;
RA   Fey P., Cox E.C.;
RT   "Cortexillin I is required for development in Polysphondylium.";
RL   Dev. Biol. 212:414-424(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26659 / Pp 5 / PN500;
RX   PubMed=21757610; DOI=10.1101/gr.121137.111;
RA   Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA   Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA   Schaap P., Gloeckner G.;
RT   "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT   origins for complex intercellular communication.";
RL   Genome Res. 21:1882-1891(2011).
CC   -!- FUNCTION: Actin-bundling protein. When linked to F-actin the actin
CC       filaments form preferentially anti-parallel bundles that associate into
CC       meshworks. Plays a major role in cytokinesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; parallel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cortexillin family. {ECO:0000305}.
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DR   EMBL; AF151101; AAD40020.1; -; Genomic_DNA.
DR   EMBL; ADBJ01000047; EFA76383.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y0T4; -.
DR   SMR; Q9Y0T4; -.
DR   STRING; 670386.Q9Y0T4; -.
DR   OMA; WCKNTTT; -.
DR   OrthoDB; 543832at2759; -.
DR   Proteomes; UP000001396; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd00014; CH; 2.
DR   Gene3D; 1.10.418.10; -; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR015383; Cortexillin-I_coiled-coil.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF09304; Cortex-I_coil; 1.
DR   SMART; SM00033; CH; 2.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS50021; CH; 2.
PE   3: Inferred from homology;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome;
KW   Repeat.
FT   CHAIN           1..440
FT                   /note="Cortexillin-1"
FT                   /id="PRO_0000312777"
FT   DOMAIN          8..115
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          124..229
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          1..227
FT                   /note="Actin-binding"
FT   COILED          227..355
FT                   /evidence="ECO:0000255"
FT   COILED          403..436
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   440 AA;  50186 MW;  01902DCA14C7ED10 CRC64;
     MAGKDWEIVQ EKAFTAWVNS VLDKRGEKIS DVAKDLSDGV KLIFFLELIS GKKFNKKFDY
     EPKARINMIQ NLALALHFLE DELKIKVQGI GAEDFVDNNK KMILGFLWTL YRKYRIAVIS
     EGDKSSEEGL LLWCKNTTTG YNGVNVTSFT KTFRDGLAYL ALAHKFDQSQ FNFADYEKLD
     PIARLNAAFE YAEKGLGVPK LLEAEEVMRG TTDERSLVLY TSLFFHAYRA KEEKERLEAS
     KSDLASKLAG LQNSLESEKL SREQLIKQKD ELKSLLASLE GEAAEREKFL RELEAKLEEI
     LKNLELERLA RMELESRLSK MEKDKAILEL KLAEAQDEKA RLEAQIEADR IRSAAEAQSL
     GLLRKHLDQH VQDLIKWQKL SIENSSSTFD DQIIEEVSGL PFGEQVKHLA TKLEDENKAI
     QKLLLSKEDD LKTAKKKAGK