CDC24_YEAST
ID CDC24_YEAST Reviewed; 854 AA.
AC P11433; D6VPH5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cell division control protein 24;
DE AltName: Full=Calcium regulatory protein;
GN Name=CDC24; Synonyms=CLS4; OrderedLocusNames=YAL041W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3301539; DOI=10.1016/0378-1119(87)90354-4;
RA Miyamoto S., Ohya Y., Ohsumi Y., Anraku Y.;
RT "Nucleotide sequence of the CLS4 (CDC24) gene of Saccharomyces
RT cerevisiae.";
RL Gene 54:125-132(1987).
RN [2]
RP SEQUENCE REVISION, AND SIMILARITY TO CDC24 FAMILY.
RX PubMed=1755844; DOI=10.1016/0006-291x(91)91233-3;
RA Miyamoto S., Ohya Y., Sano Y., Sakaguchi S., Iida H., Anraku Y.;
RT "A DBL-homologous region of the yeast CLS4/CDC24 gene product is important
RT for Ca(2+)-modulated bud assembly.";
RL Biochem. Biophys. Res. Commun. 181:604-610(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP INTERACTION WITH AXL2, AND FUNCTION.
RX PubMed=17460121; DOI=10.1091/mbc.e06-09-0822;
RA Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.;
RT "Sequential and distinct roles of the cadherin domain-containing protein
RT Axl2p in cell polarization in yeast cell cycle.";
RL Mol. Biol. Cell 18:2542-2560(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Promotes the exchange of CDC42-bound GDP by GTP. Controls the
CC polarity of calmodulin, and the calcium regulatory process of bud
CC emergence. CDC24 may be involved in the initial selection and
CC organization of the budding site. {ECO:0000269|PubMed:17460121}.
CC -!- SUBUNIT: Interacts with AXL2. {ECO:0000269|PubMed:17460121}.
CC -!- INTERACTION:
CC P11433; P29366: BEM1; NbExp=22; IntAct=EBI-4220, EBI-3508;
CC P11433; P19073: CDC42; NbExp=4; IntAct=EBI-4220, EBI-4274;
CC P11433; P48562: CLA4; NbExp=5; IntAct=EBI-4220, EBI-4750;
CC P11433; P21268: FAR1; NbExp=8; IntAct=EBI-4220, EBI-6780;
CC P11433; Q08229: NBA1; NbExp=6; IntAct=EBI-4220, EBI-36841;
CC P11433; P18851: STE4; NbExp=6; IntAct=EBI-4220, EBI-7390;
CC -!- MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M16809; AAA82871.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04990.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06945.1; -; Genomic_DNA.
DR PIR; A27477; A27477.
DR RefSeq; NP_009359.1; NM_001178186.1.
DR PDB; 1PQS; NMR; -; A=778-854.
DR PDB; 1Q1O; NMR; -; A=761-854.
DR PDB; 1TZ1; NMR; -; A=780-854.
DR PDB; 2KFJ; NMR; -; A=761-854.
DR PDB; 2KFK; NMR; -; B=761-854.
DR PDBsum; 1PQS; -.
DR PDBsum; 1Q1O; -.
DR PDBsum; 1TZ1; -.
DR PDBsum; 2KFJ; -.
DR PDBsum; 2KFK; -.
DR AlphaFoldDB; P11433; -.
DR SMR; P11433; -.
DR BioGRID; 31724; 704.
DR ComplexPortal; CPX-3462; CLA4-BEM1-CDC24 polarity complex.
DR ComplexPortal; CPX-977; CDC24-FAR1-Gbetagamma complex.
DR DIP; DIP-2228N; -.
DR IntAct; P11433; 41.
DR MINT; P11433; -.
DR STRING; 4932.YAL041W; -.
DR iPTMnet; P11433; -.
DR MaxQB; P11433; -.
DR PaxDb; P11433; -.
DR PRIDE; P11433; -.
DR EnsemblFungi; YAL041W_mRNA; YAL041W; YAL041W.
DR GeneID; 851190; -.
DR KEGG; sce:YAL041W; -.
DR SGD; S000000039; CDC24.
DR VEuPathDB; FungiDB:YAL041W; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000174094; -.
DR HOGENOM; CLU_007879_0_0_1; -.
DR InParanoid; P11433; -.
DR OMA; GYRIAKF; -.
DR BioCyc; YEAST:G3O-28849-MON; -.
DR EvolutionaryTrace; P11433; -.
DR PRO; PR:P11433; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P11433; protein.
DR GO; GO:0120171; C:Cdc24p-Far1p-Gbetagamma complex; IDA:SGD.
DR GO; GO:0005938; C:cell cortex; IC:ComplexPortal.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000935; C:division septum; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0120157; C:PAR polarity complex; IPI:ComplexPortal.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0043577; P:chemotropism; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:SGD.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0010969; P:regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IC:ComplexPortal.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IC:ComplexPortal.
DR GO; GO:0031106; P:septin ring organization; IMP:SGD.
DR CDD; cd13246; PH_Scd1; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF06395; CDC24; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..854
FT /note="Cell division control protein 24"
FT /id="PRO_0000080934"
FT DOMAIN 135..246
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 278..454
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 478..668
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 761..854
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:1Q1O"
FT STRAND 780..784
FT /evidence="ECO:0007829|PDB:1PQS"
FT HELIX 792..801
FT /evidence="ECO:0007829|PDB:1PQS"
FT TURN 802..806
FT /evidence="ECO:0007829|PDB:1PQS"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:1PQS"
FT TURN 821..823
FT /evidence="ECO:0007829|PDB:1PQS"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:1PQS"
FT HELIX 833..844
FT /evidence="ECO:0007829|PDB:1PQS"
FT STRAND 848..852
FT /evidence="ECO:0007829|PDB:1PQS"
SQ SEQUENCE 854 AA; 96940 MW; 856BCAF4EB0A67D1 CRC64;
MAIQTRFASG TSLSDLKPKP SATSISIPMQ NVMNKPVTEQ DSLFHICANI RKRLEVLPQL
KPFLQLAYQS SEVLSERQSL LLSQKQHQEL LKSNGANRDS SDLAPTLRSS SISTATSLMS
MEGISYTNSN PSATPNMEDT LLTFSMGILP ITMDCDPVTQ LSQLFQQGAP LCILFNSVKP
QFKLPVIASD DLKVCKKSIY DFILGCKKHF AFNDEELFTI SDVFANSTSQ LVKVLEVVET
LMNSSPTIFP SKSKTQQIMN AENQHRHQPQ QSSKKHNEYV KIIKEFVATE RKYVHDLEIL
DKYRQQLLDS NLITSEELYM LFPNLGDAID FQRRFLISLE INALVEPSKQ RIGALFMHSK
HFFKLYEPWS IGQNAAIEFL SSTLHKMRVD ESQRFIINNK LELQSFLYKP VQRLCRYPLL
VKELLAESSD DNNTKELEAA LDISKNIARS INENQRRTEN HQVVKKLYGR VVNWKGYRIS
KFGELLYFDK VFISTTNSSS EPEREFEVYL FEKIIILFSE VVTKKSASSL ILKKKSSTSA
SISASNITDN NGSPHHSYHK RHSNSSSSNN IHLSSSSAAA IIHSSTNSSD NNSNNSSSSS
LFKLSANEPK LDLRGRIMIM NLNQIIPQNN RSLNITWESI KEQGNFLLKF KNEETRDNWS
SCLQQLIHDL KNEQFKARHH SSTSTTSSTA KSSSMMSPTT TMNTPNHHNS RQTHDSMASF
SSSHMKRVSD VLPKRRTTSS SFESEIKSIS ENFKNSIPES SILFRISYNN NSNNTSSSEI
FTLLVEKVWN FDDLIMAINS KISNTHNNNI SPITKIKYQD EDGDFVVLGS DEDWNVAKEM
LAENNEKFLN IRLY
