CTXA_DICDI
ID CTXA_DICDI Reviewed; 444 AA.
AC Q54HG2; O15813;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cortexillin-1;
DE AltName: Full=Cortexillin I;
GN Name=ctxA; ORFNames=DDB_G0289483;
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], HOMODIMER, INTERACTION WITH ACTIN, AND
RP SUBCELLULAR LOCATION.
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=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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 243-343.
RX PubMed=10745004; DOI=10.1016/s0969-2126(00)00100-3;
RA Burkhard P., Kammerer R.A., Steinmetz M.O., Bourenkov G.P., Aebi U.;
RT "The coiled-coil trigger site of the rod domain of cortexillin I unveils a
RT distinct network of interhelical and intrahelical salt bridges.";
RL Structure 8:223-230(2000).
RN [4]
RP FUNCTION.
RX PubMed=18039932; DOI=10.1083/jcb.200705068;
RA Jeon T.J., Lee D.-J., Lee S., Weeks G., Firtel R.A.;
RT "Regulation of Rap1 activity by RapGAP1 controls cell adhesion at the front
RT of chemotaxing cells.";
RL J. Cell Biol. 179:833-843(2007).
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. {ECO:0000269|PubMed:18039932}.
CC -!- SUBUNIT: Homodimer; parallel.
CC -!- INTERACTION:
CC Q54HG2; Q550R2: ctxB; NbExp=2; IntAct=EBI-1810875, EBI-1811057;
CC Q54HG2; Q54K32: rgaA; NbExp=2; IntAct=EBI-1810875, EBI-1808670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8752217}.
CC -!- SIMILARITY: Belongs to the cortexillin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L49527; AAB62275.1; -; mRNA.
DR EMBL; AAFI02000141; EAL62673.1; -; Genomic_DNA.
DR RefSeq; XP_636175.1; XM_631083.1.
DR PDB; 1D7M; X-ray; 2.70 A; A/B=243-343.
DR PDB; 4J4A; X-ray; 1.65 A; A/B/C/D/E/F/G/H/I/J/K/L=304-328.
DR PDBsum; 1D7M; -.
DR PDBsum; 4J4A; -.
DR AlphaFoldDB; Q54HG2; -.
DR SMR; Q54HG2; -.
DR DIP; DIP-52435N; -.
DR IntAct; Q54HG2; 3.
DR STRING; 44689.DDB0191103; -.
DR PaxDb; Q54HG2; -.
DR EnsemblProtists; EAL62673; EAL62673; DDB_G0289483.
DR GeneID; 8627162; -.
DR KEGG; ddi:DDB_G0289483; -.
DR dictyBase; DDB_G0289483; ctxA.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_621778_0_0_1; -.
DR InParanoid; Q54HG2; -.
DR OMA; WCKNTTT; -.
DR PhylomeDB; Q54HG2; -.
DR EvolutionaryTrace; Q54HG2; -.
DR PRO; PR:Q54HG2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:dictyBase.
DR GO; GO:0045180; C:basal cortex; 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:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031255; C:lateral part of motile cell; IDA:dictyBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IGI:dictyBase.
DR GO; GO:0051764; P:actin crosslink formation; IDA:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0000916; P:actomyosin contractile ring contraction; 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:0036089; P:cleavage furrow formation; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:dictyBase.
DR GO; GO:0050982; P:detection of mechanical stimulus; IMP:dictyBase.
DR GO; GO:0045184; P:establishment of protein localization; IGI:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR GO; GO:1905345; P:protein localization to cleavage furrow; 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 GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
DR GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP: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 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..444
FT /note="Cortexillin-1"
FT /id="PRO_0000312776"
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..352
FT /evidence="ECO:0000255"
FT COILED 410..434
FT /evidence="ECO:0000255"
FT HELIX 303..324
FT /evidence="ECO:0007829|PDB:4J4A"
SQ SEQUENCE 444 AA; 50505 MW; 9884C6BC15BEE958 CRC64;
MAGKDWEIVQ EKAFTAWVNS VLDKRGEKIS DVGKDLSDGV KLIFFLELIS SKKFNKKYDF
EPKARINMIQ NVALALKFLD EELKIKVQGI GSEDFVDNNK KMILGFLWTL YRKYRIAVIS
EGDKSSEEGL LLWCKNTTTG YDGVNITSFT KSFRDGLAFL ALSHKFEPES FKFQEFEAMD
PIARLNAAFD FAEKGLGVPK LLEAEEVMRG TTDERSLVLY TSLFFHAYRA KEEKARLESS
KNEMANRLAG LENSLESEKV SREQLIKQKD QLNSLLASLE SEGAEREKRL RELEAKLDET
LKNLELEKLA RMELEARLAK TEKDRAILEL KLAEAIDEKS KLEQQIEATR IRGAAEAQGL
GLLRKNLDTH VHDLLKWQKL TMENSSSSSI DDQIIVEVSG LPFGEQVKHL ATKLEAENLA
IMKLLNQKED DLKAQKLKSS KSKK
