FOS1_CAEEL
ID FOS1_CAEEL Reviewed; 467 AA.
AC G5ECG2; G5EDK8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Transcription factor fos-1 {ECO:0000305};
GN Name=fos-1 {ECO:0000312|WormBase:F29G9.4b};
GN Synonyms=evl-5 {ECO:0000312|WormBase:F29G9.4a};
GN ORFNames=F29G9.4 {ECO:0000312|WormBase:F29G9.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:AAX37359.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION (ISOFORM A),
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15960981; DOI=10.1016/j.cell.2005.03.031;
RA Sherwood D.R., Butler J.A., Kramer J.M., Sternberg P.W.;
RT "FOS-1 promotes basement-membrane removal during anchor-cell invasion in C.
RT elegans.";
RL Cell 121:951-962(2005).
RN [2] {ECO:0000312|EMBL:CCD64134.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD64134.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION (ISOFORM A), DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP PROBABLE INTERACTION WITH JUN-1.
RX PubMed=17942488; DOI=10.1242/dev.002741;
RA Oommen K.S., Newman A.P.;
RT "Co-regulation by Notch and Fos is required for cell fate specification of
RT intermediate precursors during C. elegans uterine development.";
RL Development 134:3999-4009(2007).
RN [4] {ECO:0000305}
RP FUNCTION (ISOFORM A), AND DISRUPTION PHENOTYPE.
RX PubMed=17488621; DOI=10.1016/j.devcel.2007.03.003;
RA Sapir A., Choi J., Leikina E., Avinoam O., Valansi C., Chernomordik L.V.,
RA Newman A.P., Podbilewicz B.;
RT "AFF-1, a FOS-1-regulated fusogen, mediates fusion of the anchor cell in C.
RT elegans.";
RL Dev. Cell 12:683-698(2007).
RN [5] {ECO:0000305}
RP FUNCTION (ISOFORM B), TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19570917; DOI=10.1091/mbc.e08-08-0833;
RA Hiatt S.M., Duren H.M., Shyu Y.J., Ellis R.E., Hisamoto N., Matsumoto K.,
RA Kariya K., Kerppola T.K., Hu C.D.;
RT "Caenorhabditis elegans FOS-1 and JUN-1 regulate plc-1 expression in the
RT spermatheca to control ovulation.";
RL Mol. Biol. Cell 20:3888-3895(2009).
RN [6] {ECO:0000305}
RP FUNCTION (ISOFORM B), SUBUNIT, DISRUPTION PHENOTYPE, INTERACTION WITH KGB-1
RP AND HDA-1, MUTAGENESIS OF THR-440; THR-452 AND THR-454, AND PHOSPHORYLATION
RP AT THR-440; THR-452 AND THR-454.
RX PubMed=23437011; DOI=10.1371/journal.pgen.1003315;
RA Hattori A., Mizuno T., Akamatsu M., Hisamoto N., Matsumoto K.;
RT "The Caenorhabditis elegans JNK signaling pathway activates expression of
RT stress response genes by derepressing the Fos/HDAC repressor complex.";
RL PLoS Genet. 9:E1003315-E1003315(2013).
RN [7] {ECO:0000305}
RP FUNCTION (ISOFORM A), AND DISRUPTION PHENOTYPE.
RX PubMed=24553288; DOI=10.1242/dev.102434;
RA Wang Z., Chi Q., Sherwood D.R.;
RT "MIG-10 (lamellipodin) has netrin-independent functions and is a FOS-1A
RT transcriptional target during anchor cell invasion in C. elegans.";
RL Development 141:1342-1353(2014).
CC -!- FUNCTION: Developmentally regulated transcription factor which binds
CC and recognizes the enhancer DNA sequence 5'-TGA[CG]TCA-3'
CC (PubMed:23437011). {ECO:0000269|PubMed:23437011}.
CC -!- FUNCTION: [Isoform a]: Plays a role the development of the reproductive
CC system, controlling events including anchor cell (AC) fusion and
CC invasion (PubMed:15960981, PubMed:17488621). Regulates downstream
CC transcriptional targets, including zmp-1, cdh-3, him-4 and mig10b, to
CC promote the removal of the gonadal basement membrane during AC invasion
CC (PubMed:15960981, PubMed:24553288). Regulates aff-1 expression to
CC promote AC fusion (PubMed:17488621). With jun-1 regulates egl-1 and
CC lin-12 expression to allow uterine cell specification and development
CC (PubMed:17942488). {ECO:0000269|PubMed:15960981,
CC ECO:0000269|PubMed:17488621, ECO:0000269|PubMed:17942488,
CC ECO:0000269|PubMed:24553288}.
CC -!- FUNCTION: [Isoform b]: Required for ovulation (PubMed:19570917).
CC Controls plc-1 expression in the spermatheca to regulate spermathecal
CC valve dilation (PubMed:19570917). Acts with hda-1 as a downstream
CC repressor of the kgb-1 mediated stress response pathway that
CC transcriptionally represses genes involved in the response to heavy
CC metals, such as kreg-1 (PubMed:23437011). {ECO:0000269|PubMed:19570917,
CC ECO:0000269|PubMed:23437011}.
CC -!- SUBUNIT: Homodimer (PubMed:23437011). Heterodimer; with jun-1
CC (PubMed:17942488). Interacts with kgb-1 and hda-1 (PubMed:23437011).
CC {ECO:0000269|PubMed:23437011, ECO:0000305|PubMed:17942488}.
CC -!- INTERACTION:
CC G5ECG2; G5ECU7: jun-1; NbExp=3; IntAct=EBI-6728159, EBI-2414388;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15960981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000303|PubMed:17942488};
CC Name=b {ECO:0000312|WormBase:F29G9.4b}; Synonyms=a
CC {ECO:0000303|PubMed:17942488};
CC IsoId=G5ECG2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F29G9.4a}; Synonyms=b
CC {ECO:0000303|PubMed:17942488};
CC IsoId=G5ECG2-2; Sequence=VSP_057614;
CC -!- TISSUE SPECIFICITY: Expressed in anchor cells (PubMed:15960981).
CC Isoform a is expressed in somatic gonad cells that neighbor anchor
CC cells (PubMed:15960981, PubMed:19570917). Isoform b is expressed in
CC vulval cells, the uterine cells that neighbor anchor cells and the
CC spermatheca (PubMed:15960981, PubMed:19570917).
CC {ECO:0000269|PubMed:15960981, ECO:0000269|PubMed:19570917}.
CC -!- DEVELOPMENTAL STAGE: [Isoform a]: Detected before the L2 molt stage
CC (PubMed:15960981). Expressed throughout ventral uterine intermediate
CC precursor cells (PubMed:17942488). {ECO:0000269|PubMed:15960981,
CC ECO:0000269|PubMed:17942488}.
CC -!- PTM: May be phosphorylated by kgb-1. Phosphorylation at Thr-440
CC increases sensitivity to heavy metal stress. Phosphorylation inhibits
CC homodimer formation, and promotes association with target promoters.
CC {ECO:0000269|PubMed:23437011}.
CC -!- DISRUPTION PHENOTYPE: [Isoform a]: Animals are sterile and display a
CC protruding vulva phenotype (PubMed:17942488). Animals have uterine
CC defects lacking both a uterine lumen and a utse-like process;
CC subsequently fail to develop a differentiated uterus. Furthermore,
CC uterine seam cell genes egl-13 and lin-11 are not expressed during late
CC larval development (PubMed:17942488). At the L3 developmental stage, AC
CC display either failed or delayed invasion leading to the defective
CC removal of the gonadal basement-membrane (PubMed:15960981,
CC PubMed:17488621). AC do not fuse (PubMed:17488621). AC specific
CC expression of lin-3 is increased, but zmp-1, him-4 and aff-1 expression
CC is undetectable and cdh-3 expression is reduced (PubMed:15960981,
CC PubMed:17488621). RNAi-mediated knockdown of both isoforms results in
CC sterility, a protruding vulva and exploded through the vulva phenotypes
CC (PubMed:17942488, PubMed:19570917). Animals have an undifferentiated
CC uterus and lack uterine egl-13 expression (PubMed:17942488). Animals
CC also display an endomitotic oocytes phenotype, which is due to improper
CC distal spermathecal valve dilation and reduced plc-1 expression in the
CC spermatheca (PubMed:19570917). Animals have no mig-10b expression in AC
CC (PubMed:24553288). RNAi-mediated knockdown of isoform b results in an
CC everted/protruded vulval phenotype in adults (PubMed:23437011).
CC {ECO:0000269|PubMed:15960981, ECO:0000269|PubMed:17488621,
CC ECO:0000269|PubMed:17942488, ECO:0000269|PubMed:19570917,
CC ECO:0000269|PubMed:23437011, ECO:0000269|PubMed:24553288}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; AY835432; AAX37359.1; -; mRNA.
DR EMBL; AY835433; AAX37360.1; -; mRNA.
DR EMBL; FO080494; CCD64133.1; -; Genomic_DNA.
DR EMBL; FO080494; CCD64134.1; -; Genomic_DNA.
DR PIR; T31799; T31799.
DR RefSeq; NP_001033480.1; NM_001038391.3.
DR RefSeq; NP_001033481.1; NM_001038392.3. [G5ECG2-1]
DR AlphaFoldDB; G5ECG2; -.
DR SMR; G5ECG2; -.
DR IntAct; G5ECG2; 3.
DR STRING; 6239.F29G9.4b; -.
DR iPTMnet; G5ECG2; -.
DR EPD; G5ECG2; -.
DR PaxDb; G5ECG2; -.
DR EnsemblMetazoa; F29G9.4a.1; F29G9.4a.1; WBGene00001345. [G5ECG2-2]
DR EnsemblMetazoa; F29G9.4a.2; F29G9.4a.2; WBGene00001345. [G5ECG2-2]
DR EnsemblMetazoa; F29G9.4a.3; F29G9.4a.3; WBGene00001345. [G5ECG2-2]
DR EnsemblMetazoa; F29G9.4a.4; F29G9.4a.4; WBGene00001345. [G5ECG2-2]
DR EnsemblMetazoa; F29G9.4a.5; F29G9.4a.5; WBGene00001345. [G5ECG2-2]
DR EnsemblMetazoa; F29G9.4b.1; F29G9.4b.1; WBGene00001345. [G5ECG2-1]
DR GeneID; 178987; -.
DR KEGG; cel:CELE_F29G9.4; -.
DR CTD; 178987; -.
DR WormBase; F29G9.4a; CE27375; WBGene00001345; fos-1. [G5ECG2-2]
DR WormBase; F29G9.4b; CE39151; WBGene00001345; fos-1. [G5ECG2-1]
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; G5ECG2; -.
DR OMA; SSPMVQY; -.
DR OrthoDB; 1737689at2759; -.
DR PRO; PR:G5ECG2; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001345; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:WormBase.
DR GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:WormBase.
DR GO; GO:0034769; P:basement membrane disassembly; IMP:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR GO; GO:1903854; P:negative regulation of stress response to copper ion; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:WormBase.
DR GO; GO:0060142; P:regulation of syncytium formation by plasma membrane fusion; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..467
FT /note="Transcription factor fos-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432855"
FT DOMAIN 163..226
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..205
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 212..219
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23437011"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23437011"
FT MOD_RES 454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23437011"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform a)"
FT /id="VSP_057614"
FT MUTAGEN 440
FT /note="T->A: Decreased phosphorylation by kgb-1. Loss of
FT phosphorylation by kgb-1; when associated with A-452 and A-
FT 454."
FT /evidence="ECO:0000269|PubMed:23437011"
FT MUTAGEN 452
FT /note="T->A: Loss of phosphorylation by kgb-1; when
FT associated with A-440 and A-454."
FT /evidence="ECO:0000269|PubMed:23437011"
FT MUTAGEN 454
FT /note="T->A: Loss of phosphorylation by kgb-1; when
FT associated with A-440 and A-452."
FT /evidence="ECO:0000269|PubMed:23437011"
SQ SEQUENCE 467 AA; 51899 MW; 3127084AD2284E1F CRC64;
MFEQPSSTTN TTTSSGSGSD SNHYFELGPR NPINQAHPTS VIVPPRQHHH QIHQQQTDNS
PLTPCTPYYP SNAYGLPLFF GTDFLQFQPS DIPSPLTPNI SSPLTPHPFG PIPAIPTNQI
YNRTFTDFYS TAASSPMVQY STVKKSSAGR KPKEEDNMED DDDDKRLKRR QRNKEAAARC
RQRRIDLMKE LQDQVNDFKN SNDKKMAECN NIRNKLNSLK NYLETHDCKL SREERTHEIN
RLIIPPSTVP PSQPYLQHSL RVHPPRADSV PYSIRSGHSS SSSEQHSPVE DYKPSIDQLL
LPPISCIQNI KDRNINSMPP PALPASTSAA GIHVITSIPV SHANSLHGRS ENVFAEPERK
IPKIELDQTL TSLTMPDDVE RPSALPTLSR IVENQPITTP SRPFRLGGEY QNQTPQSTGN
GLFGGPPGPF DLLSSNTGLT PSGQPTMNFV STPTPIQPHP DADLRPL
