ID   CTXB_DICDI              Reviewed;         441 AA.
AC   Q550R2; O15814; Q8MNG7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cortexillin-2;
DE   AltName: Full=Cortexillin II;
GN   Name=ctxB; ORFNames=DDB_G0276893;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=8752217; DOI=10.1016/s0092-8674(00)80136-1;
RA   Faix J., Steinmetz M., Boves H., Kammerer R.A., Lottspeich F., Mintert U.,
RA   Murphy J., Stock A., Aebi U., Gerisch G.;
RT   "Cortexillins, major determinants of cell shape and size, are actin-
RT   bundling proteins with a parallel coiled-coil tail.";
RL   Cell 86:631-642(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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. Negatively regulates
CC       cortical localization of rapgap1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; parallel. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q550R2; Q54HG2: ctxA; NbExp=2; IntAct=EBI-1811057, EBI-1810875;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cortexillin family. {ECO:0000305}.
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DR   EMBL; L46371; AAB62274.1; -; mRNA.
DR   EMBL; AAFI02000019; EAL68948.1; -; Genomic_DNA.
DR   RefSeq; XP_642870.1; XM_637778.1.
DR   AlphaFoldDB; Q550R2; -.
DR   SMR; Q550R2; -.
DR   IntAct; Q550R2; 2.
DR   STRING; 44689.DDB0185031; -.
DR   PaxDb; Q550R2; -.
DR   PRIDE; Q550R2; -.
DR   EnsemblProtists; EAL68948; EAL68948; DDB_G0276893.
DR   GeneID; 8620736; -.
DR   KEGG; ddi:DDB_G0276893; -.
DR   dictyBase; DDB_G0276893; ctxB.
DR   eggNOG; KOG0035; Eukaryota.
DR   HOGENOM; CLU_621778_0_0_1; -.
DR   InParanoid; Q550R2; -.
DR   OMA; AWCKKTT; -.
DR   PhylomeDB; Q550R2; -.
DR   Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR   PRO; PR:Q550R2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR   GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR   GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR   GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; ISS:dictyBase.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:dictyBase.
DR   GO; GO:0019887; F:protein kinase regulator activity; IGI:dictyBase.
DR   GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IGI:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR   GO; GO:0032060; P:bleb assembly; IGI:dictyBase.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:dictyBase.
DR   GO; GO:0045184; P:establishment of protein localization; IGI:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR   GO; GO:0043087; P:regulation of GTPase activity; IGI:dictyBase.
DR   GO; GO:0043520; P:regulation of myosin II filament assembly; IGI:dictyBase.
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   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome;
KW   Repeat.
FT   CHAIN           1..441
FT                   /note="Cortexillin-2"
FT                   /id="PRO_0000312778"
FT   DOMAIN          9..117
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          126..231
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          1..229
FT                   /note="Actin-binding"
FT   COILED          229..362
FT                   /evidence="ECO:0000255"
FT   COILED          406..430
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  50460 MW;  CED37127A2F5CFD1 CRC64;
     MDLNKEWEKV QEMAFTSWVN SVLEKRGCDK ISDVSTDLSD GVKLIYFLES VSGKKFPKKF
     DLEPKTRIMR VQNLHLAMLF IDEDLKIKVQ GVAAEEFVDN NKKMILGFLW TLYRKYRISV
     INEGDKSSEE GLLAWCKKTT EGYNNVNITG FKSSFRDGHG FLALAHKYDP TVFKYDEYEG
     HDNIARLNAA FDFAEKGLGI PKLLEAESLS KGNVDERSIV LYTSLFFHAF RAKEEREALE
     ASQNSLNNKL ASLEQSLEGE KHSQEELVKQ KKDLEDALNK IREQNDNRNS RITDLQSKID
     DALRGLDDEK LAKLDLESRL AKCEKDKAIL ELKLAEILDE KDRLEKKIDE DKKRAEAERL
     GLGLIRQHLA AQFSDIHKWQ SFLEHPETVP YTGTPVDLDS ELSSLSFEEQ AKKLASKLES
     ENILIEKYLN GKEEAKAAAK K