SRF_CAEEL
ID SRF_CAEEL Reviewed; 327 AA.
AC Q18955;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serum response factor homolog {ECO:0000305};
DE AltName: Full=Uncoordinated protein 120 {ECO:0000312|WormBase:D1081.2};
GN Name=unc-120 {ECO:0000312|WormBase:D1081.2};
GN ORFNames=D1081.2 {ECO:0000312|WormBase:D1081.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15892873; DOI=10.1186/gb-2005-6-5-r45;
RA Baugh L.R., Wen J.C., Hill A.A., Slonim D.K., Brown E.L., Hunter C.P.;
RT "Synthetic lethal analysis of Caenorhabditis elegans posterior embryonic
RT patterning genes identifies conserved genetic interactions.";
RL Genome Biol. 6:RESEARCH0045.1-RESEARCH0045.8(2005).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17142668; DOI=10.1101/gad.1481706;
RA Fukushige T., Brodigan T.M., Schriefer L.A., Waterston R.H., Krause M.;
RT "Defining the transcriptional redundancy of early bodywall muscle
RT development in C. elegans: evidence for a unified theory of animal muscle
RT development.";
RL Genes Dev. 20:3395-3406(2006).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29314608; DOI=10.1111/acel.12713;
RA Mergoud Dit Lamarche A., Molin L., Pierson L., Mariol M.C., Bessereau J.L.,
RA Gieseler K., Solari F.;
RT "UNC-120/SRF independently controls muscle aging and lifespan in
RT Caenorhabditis elegans.";
RL Aging Cell 17:e12713-e12713(2018).
CC -!- FUNCTION: Transcription factor (By similarity). Regulates myogenesis,
CC in cooperation with transcription factors hlh-1 and hnd-1
CC (PubMed:15892873, PubMed:17142668). Required for maintenance of muscle
CC in adulthood (PubMed:29314608). {ECO:0000250|UniProtKB:Q9JM73,
CC ECO:0000269|PubMed:15892873, ECO:0000269|PubMed:17142668,
CC ECO:0000269|PubMed:29314608}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC ECO:0000269|PubMed:29314608}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle, varying with age, decreasing
CC twofold during the first week of adulthood.
CC {ECO:0000269|PubMed:17142668}.
CC -!- DISRUPTION PHENOTYPE: Mutants usually hatch and appear normal in early
CC L1, but become progressively paralyzed later during L1
CC (PubMed:17142668). Complete larval lethal, typically at late L1 or
CC early L2 (PubMed:17142668). Abnormal bodywall and egg-laying muscle in
CC hermaphrodites, but with no obvious abnormality of pharyngeal muscle or
CC other cell types (PubMed:17142668). Five percent of the progeny from
CC hlh-1, unc-120 double heterozygous parents exhibit partial absence of
CC bodywall muscle and reduced expression of myosin myo-3
CC (PubMed:17142668). RNAi-mediated knockdown causes a low frequency of
CC embryonic lethality, with embryos arresting paralyzed at the two-fold
CC stage; increases in frequency significantly on an hlh-1 or hnd-1 mutant
CC background (PubMed:15892873). RNAi-mediated knockdown causes those
CC embryos that survive to hatching to become uncoordinated, dumpy larvae
CC (PubMed:15892873). RNAi-mediated knockdown causes abnormalities in
CC muscle, including: altered mitochondrial morphology at day 6 of
CC adulthood, two-fold to five-fold down-regulation of transcript levels
CC at day 7 and significant increase in the number of autophagic vesicles
CC (PubMed:29314608). RNAi-mediated knockdown causes a reduction in
CC average lifespan by 16% (PubMed:29314608). RNAi-mediated knockdown on a
CC daf-2 mutant background causes a dramatic decrease in physical
CC performance at day 18 (PubMed:29314608). {ECO:0000269|PubMed:15892873,
CC ECO:0000269|PubMed:17142668, ECO:0000269|PubMed:29314608}.
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DR EMBL; BX284601; CAB00023.1; -; Genomic_DNA.
DR PIR; T20313; T20313.
DR RefSeq; NP_492296.1; NM_059895.4.
DR AlphaFoldDB; Q18955; -.
DR SMR; Q18955; -.
DR DIP; DIP-26080N; -.
DR STRING; 6239.D1081.2; -.
DR EPD; Q18955; -.
DR PaxDb; Q18955; -.
DR PeptideAtlas; Q18955; -.
DR EnsemblMetazoa; D1081.2.1; D1081.2.1; WBGene00006844.
DR GeneID; 172636; -.
DR KEGG; cel:CELE_D1081.2; -.
DR UCSC; D1081.2; c. elegans.
DR CTD; 172636; -.
DR WormBase; D1081.2; CE05534; WBGene00006844; unc-120.
DR eggNOG; KOG0015; Eukaryota.
DR GeneTree; ENSGT00400000022158; -.
DR HOGENOM; CLU_869421_0_0_1; -.
DR InParanoid; Q18955; -.
DR OMA; KMEYISN; -.
DR OrthoDB; 1214855at2759; -.
DR Reactome; R-CEL-9031628; NGF-stimulated transcription.
DR SignaLink; Q18955; -.
DR PRO; PR:Q18955; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006844; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Myogenesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..327
FT /note="Serum response factor homolog"
FT /id="PRO_0000451823"
FT DOMAIN 45..105
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 12..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 35045 MW; 264F65A54A97BC72 CRC64;
MTEAEDFAQL LQKLQNASPA LPEGTSSTPT PSSSTGLLPN GKKTKGRVKI KMEYINNKLR
RYTTFSKRKT GIMKKAFELS TLTGTQVMLL VASETGHVYT YATPKLQPMI SSDTGKAMIQ
SCLNAPGGDG SDVQPSRTEF TFDSGNGGNG MRKRKMLSDV MSAESSNNSP SMPNFTPFLA
PSMAPLFSTF GEDDYNNDES GDDSDSEEAS SDIKEEYQGS PTMVKQETTE IDSVTASLQQ
RIKEAMRQAA SNKQAIKKAK ITPPSSNMNN AAFLNPFLLQ GGANASNLLA TAARKGDDAG
SLTSNPFLSM GLNLQQLIES AAIASNE
