ID   CTXB_POLPP              Reviewed;         449 AA.
AC   Q9Y0T3; D3BT40;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cortexillin-2;
DE   AltName: Full=Cortexillin II;
GN   Name=ctxB; ORFNames=PPL_11332;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFA75257.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF151102; AAD40021.1; -; Genomic_DNA.
DR   EMBL; ADBJ01000056; EFA75257.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q9Y0T3; -.
DR   SMR; Q9Y0T3; -.
DR   STRING; 670386.Q9Y0T3; -.
DR   OrthoDB; 901502at2759; -.
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; 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; PS50021; CH; 2.
PE   3: Inferred from homology;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome;
KW   Repeat.
FT   CHAIN           1..449
FT                   /note="Cortexillin-2"
FT                   /id="PRO_0000312779"
FT   DOMAIN          10..119
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          128..233
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          1..231
FT                   /note="Actin-binding"
FT   COILED          232..364
FT                   /evidence="ECO:0000255"
FT   COILED          408..441
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  51168 MW;  0CE7D61DA5DE92C8 CRC64;
     MTDLHKEWEK VQEMAFASWV NSVLEKRGGV EKISDVSTDL SDGVKLIFFL ESVSGKKFPK
     KFDLEPKTRI LRIQNLHLAM LFVDEDLKVK VQGVAAEEFV DNNKKMILGF LWTLYRKYRI
     SVINEGDKSS EEGLLAWVKK TTDGYSGVNI TNFKASFRDG NAYLALAHKF DPSVFKYDEF
     SGKDQIERLN AAFDFAEKGL GIPKLLDAES LSKGNVDERS IILYTSLFFH AYRAKEEREA
     LEASQNSLAN KLASLEQSLE GEKTSQDELA RQKKELEESL RLIRQQNEQR NQRIADIQSK
     IDDALRGIDD EKMAKLDLES RLSKTEKDKA ILELKLAETL DENERLRNKI EEDKKRAAAE
     AEGLGLLRTH IGHQITDIAK WQSFLDNPEA VPYTKTPVNL EAELASLQFE EQAKRLGSKV
     ENENISLEKY LSLKEEELKS AGAPKKRTK