FBXA_DICDI
ID FBXA_DICDI Reviewed; 1247 AA.
AC Q9Y0T2; Q550Q0; Q9U9T1; Q9U9U5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=F-box/WD repeat-containing protein A;
DE Short=F-box protein A;
DE AltName: Full=Protein cheater A;
GN Name=fbxA; Synonyms=chtA; ORFNames=DDB_G0276887;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10898960; DOI=10.1006/dbio.2000.9793;
RA Nelson M.K., Clark A., Abe T., Nomura A., Yadava N., Funair C.J.,
RA Jermyn K.A., Mohanty S., Firtel R.A., Williams J.G.;
RT "An F-Box/WD40 repeat-containing protein important for Dictyostelium cell-
RT type proportioning, slug behaviour, and culmination.";
RL Dev. Biol. 224:42-59(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 1-720,
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3-1;
RX PubMed=10725352; DOI=10.1073/pnas.97.7.3292;
RA Ennis H.L., Dao D.N., Pukatzki S.U., Kessin R.H.;
RT "Dictyostelium amoebae lacking an F-box protein form spores rather than
RT stalk in chimeras with wild type.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3292-3297(2000).
RN [3]
RP SEQUENCE REVISION TO 1025.
RA Franke J.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH CULA AND REGA.
RX PubMed=11390363; DOI=10.1101/gad.871101;
RA Mohanty S., Lee S., Yadava N., Dealy M.J., Johnson R.S., Firtel R.A.;
RT "Regulated protein degradation controls PKA function and cell-type
RT differentiation in Dictyostelium.";
RL Genes Dev. 15:1435-1448(2001).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12796307; DOI=10.1128/ec.2.3.618-626.2003;
RA Tekinay T., Ennis H.L., Wu M.Y., Nelson M., Kessin R.H., Ratner D.I.;
RT "Genetic interactions of the E3 ubiquitin ligase component FbxA with cyclic
RT AMP metabolism and a histidine kinase signaling pathway during
RT Dictyostelium discoideum development.";
RL Eukaryot. Cell 2:618-626(2003).
RN [8]
RP FUNCTION.
RX PubMed=17496139; DOI=10.1073/pnas.0702723104;
RA Gilbert O.M., Foster K.R., Mehdiabadi N.J., Strassmann J.E., Queller D.C.;
RT "High relatedness maintains multicellular cooperation in a social amoeba by
RT controlling cheater mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8913-8917(2007).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. May target the cAMP phosphodiesterase regA for degradation
CC leading to an increase in cAMP and PKA activity. Promotes development
CC of prestalk cells as opposed to prespores within the developing
CC fruiting body. Required for culmination and fruiting body development.
CC {ECO:0000269|PubMed:10725352, ECO:0000269|PubMed:10898960,
CC ECO:0000269|PubMed:11390363, ECO:0000269|PubMed:12796307,
CC ECO:0000269|PubMed:17496139}.
CC -!- SUBUNIT: Component of an SCF complex including at least culA. Formation
CC of this complex appears to require activity of the MAP kinase erk2.
CC Interacts with regA. {ECO:0000269|PubMed:11390363}.
CC -!- DEVELOPMENTAL STAGE: Not expressed during vegetative growth. Expressed
CC from around 4 hours following the induction of starvation. Expression
CC peaks around 14 hours (first finger/slug stage), and drops around 18
CC hours (Mexican hat stage). Expressed at high levels in prestalk cells.
CC Also expressed in spores that have risen to the top of the fruiting
CC body and undergone encapsulation. {ECO:0000269|PubMed:10725352,
CC ECO:0000269|PubMed:10898960, ECO:0000269|PubMed:12796307}.
CC -!- DISRUPTION PHENOTYPE: Cells preferentially form spores within chimeric
CC cell populations and are more likely to survive adverse conditions than
CC their wild type counterparts, which accumulate preferentially within
CC the stalk. Such mutants have been termed 'cheaters'. Over time, mutant
CC cheaters may be expected to dominate mixed populations, as they ensure
CC their own survival at the expense of their altruistic wild type
CC counterparts. The spread of cheater mutants may be limited by the high
CC degree of relatedness within naturally occurring populations of
CC Dictyostelium discoideum. Altruistic behavior may be preserved from the
CC damaging effects of mutant cheaters by the formation of clonal fruiting
CC bodies, in which all cells exhibit cooperative behavior.
CC {ECO:0000269|PubMed:12796307}.
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; AF151733; AAD40673.1; -; Genomic_DNA.
DR EMBL; AF151111; AAD37799.2; -; Genomic_DNA.
DR EMBL; AF151112; AAD37800.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68945.1; -; Genomic_DNA.
DR RefSeq; XP_642882.1; XM_637790.1.
DR AlphaFoldDB; Q9Y0T2; -.
DR SMR; Q9Y0T2; -.
DR STRING; 44689.DDB0185042; -.
DR PaxDb; Q9Y0T2; -.
DR EnsemblProtists; EAL68945; EAL68945; DDB_G0276887.
DR GeneID; 8620748; -.
DR KEGG; ddi:DDB_G0276887; -.
DR dictyBase; DDB_G0276887; fbxA.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_266138_0_0_1; -.
DR InParanoid; Q9Y0T2; -.
DR OMA; NGWVIQG; -.
DR PRO; PR:Q9Y0T2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:dictyBase.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:dictyBase.
DR GO; GO:0099139; P:cheating during chimeric sorocarp development; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:dictyBase.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.530.20; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50848; START; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Fruiting body; Reference proteome;
KW Repeat; Sporulation; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..1247
FT /note="F-box/WD repeat-containing protein A"
FT /id="PRO_0000327394"
FT DOMAIN 1..214
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT DOMAIN 631..677
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 895..934
FT /note="WD 1"
FT REPEAT 945..984
FT /note="WD 2"
FT REPEAT 988..1025
FT /note="WD 3"
FT REPEAT 1029..1073
FT /note="WD 4"
FT REPEAT 1076..1114
FT /note="WD 5"
FT REPEAT 1119..1158
FT /note="WD 6"
FT REPEAT 1218..1247
FT /note="WD 7"
FT REGION 484..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 228
FT /note="K -> M (in Ref. 1; AAD40673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1247 AA; 142388 MW; E2F90D3D6522AACC CRC64;
MQYVNGNDIS SQSIHEVLEL AFSTKIPWTK LEYESSEKHI IHSYSSHERG IYLSKGVAEF
NISPENMYEL LLDISSRSKW DFHCREAHII EEYDHLNHII HLNFTNPLIS NLDMNLYRSC
KYDPQERLFV IAMRSIELED GDVDQFECLP NGWVIQGLRG QKDKCKMTFV QQCDLRDIEL
QRIPGYKSFN SKERLEDFQF LTLFPATVSG RLAKIFESIE LYISNNVKDI ETKDIRISIM
EKAEKEVNEM FGTTNPDYGW KIYLKKLDME ILIKKTTSGY YMIGKGSFSS RYSPELLADV
LYQKNPFEWD TFYDKTKLVE SINSSIREVE VHYRMWRNTI TMRLLQSVKK GPGNFSSVHW
RSICSPNYQV ADGIEVHYLP TALLNYGLGD GSFTSFLAAI EVKGYPTPWE EEMVTKMFAA
RIISNQNSII NHVNKLTGGS EMIRELPVIP SVQHHCGDVG SHIGTPQVYN AMVENFADIL
LDEGNKDGNV VSSKNKRKRN KNNENKNNNN DNIIDEEIEQ EEENIEKDQQ QTQQQQTQKQ
QQQQQQQQKT QQQPQQQQQQ PQEQQQNHSQ LKKEIKPTRP SIRFTYLLSN SSSGQRPIAW
YESKKQPFLF LVSDSSERKG KIQRKTYYFS NSGFDNLPEE VVQIIFSNLS AINIVNLSLV
CKRFKMATDS PILWKNLYKS NPLFHKKTPK RKQIIHSNLS NDENKVNSNS GDSADGSSSQ
EEEEQQQQNQ QQNQQQNQQQ QQQQTFDLSN INLNDPISLL MVFTNGIIPQ NLSPTEIINV
GGIVSQIDLN DLSNVETLIQ QLPHQVLSLI QMNTLDAKIQ HLSMISGMPA TIGQESPINK
NSSDNPKPNA YNKRDNNSYI PDEEFINWKS HYTEKHKQSK RWVNMEPIRI TPLKGHNRAI
KAVKSEGNSA ITVSTEKKIK FWNLNTGQCI GDYEGESGVL SVEYDHTQKS SCIWPLSDYT
KVHIGHKNGT VTMVDFIEQP IEVIHTSRPT NLADGFDFTF PGKYLIWEHT IIHYWDVETS
TLLWNELNAH TKKITQSKIV AQHELSNKGI VFTTSSDKSA KVWDLTNGTC INTLVGHSYA
VNCIEPIGDY MALTGSTDKT LKLWDLRQAS TFISSYSTKH TGPIRCISYQ EKNGIVLSGS
DDGSIIAFNL DNWNLSNISV VKKPIFNNVI GNIGTTTTTT TTTTTTTTTT TSTTNNTNVP
EIPKINLGTF KDSKRLHNHE SAVTCIESDE AGFISGSQNG LVLRWDF
