HND1_CAEEL
ID HND1_CAEEL Reviewed; 226 AA.
AC Q18612;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Hand transcription factor 1 {ECO:0000303|PubMed:12756172};
GN Name=hnd-1 {ECO:0000312|WormBase:C44C10.8};
GN ORFNames=C44C10.8 {ECO:0000312|WormBase:C44C10.8};
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12756172; DOI=10.1242/dev.00483;
RA Mathies L.D., Henderson S.T., Kimble J.;
RT "The C. elegans Hand gene controls embryogenesis and early gonadogenesis.";
RL Development 130:2881-2892(2003).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION, 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).
CC -!- FUNCTION: Probable transcription factor which regulates early embryonic
CC myogenesis, in cooperation with transcription factors unc-120 and hlh-1
CC (PubMed:15892873, PubMed:17142668). Involved in controlling the number
CC and position of somatic gonadal precursor cells (SGPs) in the gonadal
CC primordium, and embryonic body shape (PubMed:12756172).
CC {ECO:0000269|PubMed:12756172, ECO:0000269|PubMed:15892873,
CC ECO:0000269|PubMed:17142668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the MS, C and D embryonic lineages,
CC which develop into somatic gonadal precursor cells (SGPs), other
CC mesodermal cells and bodywall muscle (PubMed:12756172). Expression is
CC abolished in most body muscle cells by the comma stage of
CC embryogenesis, but continues in the SGPs (Z1 and Z4), and then is
CC abolished shortly after assembly of the gonadal primordium
CC (PubMed:12756172). {ECO:0000269|PubMed:12756172}.
CC -!- DISRUPTION PHENOTYPE: Adults are viable and fertile, but with a
CC moderate frequency of somatic gonad defects, which increases on an ehn-
CC 3 mutant background (PubMed:12756172). Low frequency of embryonic
CC lethality, with embryos arresting paralyzed at the two-fold stage;
CC increases in frequency significantly on an hlh-1 or unc-120 mutant
CC background (PubMed:12756172, PubMed:15892873, PubMed:17142668). Many
CC embryos that survive to hatch become uncoordinated, dumpy larvae with
CC variable body shape defects, typically in the posterior
CC (PubMed:15892873, PubMed:12756172). One quarter of the embryos from
CC homozygous hnd-1;hlh-1 heterozygous parents exhibit reduced expression
CC of myosin myo-3 (PubMed:17142668). On a unc-120 mutant background,
CC progeny show reduced expression of myo-3 at mid-embryogenesis
CC (PubMed:17142668). RNAi-mediated knockdown results in abnormal number
CC and positioning of the somatic gonadal precursor cells (SGPs) and
CC influences the maintenance of primordial germ cells (PGCs) in L1 larvae
CC (PubMed:15892873). {ECO:0000269|PubMed:12756172,
CC ECO:0000269|PubMed:15892873, ECO:0000269|PubMed:17142668}.
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DR EMBL; BX284606; CAA93634.1; -; Genomic_DNA.
DR PIR; T19921; T19921.
DR RefSeq; NP_509952.1; NM_077551.1.
DR AlphaFoldDB; Q18612; -.
DR SMR; Q18612; -.
DR IntAct; Q18612; 7.
DR STRING; 6239.C44C10.8; -.
DR PaxDb; Q18612; -.
DR EnsemblMetazoa; C44C10.8.1; C44C10.8.1; WBGene00001981.
DR GeneID; 183457; -.
DR KEGG; cel:CELE_C44C10.8; -.
DR UCSC; C44C10.8; c. elegans.
DR CTD; 183457; -.
DR WormBase; C44C10.8; CE05415; WBGene00001981; hnd-1.
DR eggNOG; ENOG502SX5H; Eukaryota.
DR HOGENOM; CLU_1251686_0_0_1; -.
DR InParanoid; Q18612; -.
DR OMA; LQQRIPY; -.
DR OrthoDB; 1066762at2759; -.
DR SignaLink; Q18612; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001981; Expressed in embryo and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0008406; P:gonad development; IMP:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Myogenesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..226
FT /note="Hand transcription factor 1"
FT /id="PRO_0000451824"
FT DOMAIN 23..77
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..36
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 37..77
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 26450 MW; 0FBAD90D3E686FD5 CRC64;
MVKSTTAGNN AVSSLESTDS KKSRKEKSRE KEHRRAQCIN SAFEILQQHI PYLKSEERKS
LPKIKTLRLA MQYIDHLKKL LGGNEMLETD CNESRPLTHS DFRVNISNEI RIRNSYRERA
HNQELDEATV KRILAREDQR RRCSSVPEGI QRYTPYQSRQ FGPISNNVCN FRHVDANQYN
TNFMEYQTQM VQVANFPNQF SHEYYNYGTF PVIDPTSLEN SNPILQ