DMD10_CAEEL
ID DMD10_CAEEL Reviewed; 348 AA.
AC G5EEJ1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Doublesex- and mab-3-related transcription factor dmd-10 {ECO:0000303|PubMed:33665029};
GN Name=dmd-10 {ECO:0000312|WormBase:C34D1.1};
GN Synonyms=dmd-11 {ECO:0000312|WormBase:C34D1.1};
GN ORFNames=C34D1.1 {ECO:0000312|WormBase:C34D1.1};
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]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27144354; DOI=10.1038/nature17977;
RA Oren-Suissa M., Bayer E.A., Hobert O.;
RT "Sex-specific pruning of neuronal synapses in Caenorhabditis elegans.";
RL Nature 533:206-211(2016).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33665029; DOI=10.7717/peerj.10892;
RA Durbeck J., Breton C., Suter M., Luth E.S., McGehee A.M.;
RT "The Doublesex/Mab-3 domain transcription factor DMD-10 regulates ASH-
RT dependent behavioral responses.";
RL PeerJ 9:e10892-e10892(2021).
CC -!- FUNCTION: Transcription factor (By similarity). Plays a role in
CC neuronal signaling in polymodal sensory neuron ASH, downstream of
CC sensory receptor activation (PubMed:33665029). Required for maintenance
CC of AVG synapses (PubMed:27144354). {ECO:0000250|UniProtKB:Q9QZ59,
CC ECO:0000269|PubMed:27144354, ECO:0000269|PubMed:33665029}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
CC -!- TISSUE SPECIFICITY: Dimorphically expressed in the dimorphically
CC connected interneuron AVG; expression is observed in the AVG in males,
CC but not in hermaphrodites. {ECO:0000269|PubMed:27144354}.
CC -!- DISRUPTION PHENOTYPE: Decreased response to nose touch, but normal
CC motor and sensory behaviors and normal levels of glutamate receptor
CC glr-1 (PubMed:33665029). Small but significant decrease in response to
CC high osmolarity (PubMed:33665029). Decreased reversal responses to
CC direct stimulation of the polymodal sensory neuron ASH as compared to
CC wild type (PubMed:33665029). Defects in male mating behavior; reduced
CC efficiency in locating vulva of partner (PubMed:27144354). Alterations
CC in AVG interneuron synaptic wiring in a dmd-5 mutant background
CC (PubMed:27144354). {ECO:0000269|PubMed:27144354,
CC ECO:0000269|PubMed:33665029}.
CC -!- SIMILARITY: Belongs to the DMRT family. {ECO:0000305}.
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DR EMBL; BX284605; CAB01491.3; -; Genomic_DNA.
DR RefSeq; NP_506288.2; NM_073887.3.
DR AlphaFoldDB; G5EEJ1; -.
DR SMR; G5EEJ1; -.
DR STRING; 6239.C34D1.1; -.
DR PaxDb; G5EEJ1; -.
DR EnsemblMetazoa; C34D1.1.1; C34D1.1.1; WBGene00007929.
DR GeneID; 183202; -.
DR KEGG; cel:CELE_C34D1.1; -.
DR CTD; 183202; -.
DR WormBase; C34D1.1; CE54228; WBGene00007929; dmd-10.
DR eggNOG; KOG3815; Eukaryota.
DR GeneTree; ENSGT00970000196492; -.
DR HOGENOM; CLU_973992_0_0_1; -.
DR InParanoid; G5EEJ1; -.
DR OrthoDB; 1751871at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007929; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0007548; P:sex differentiation; IBA:GO_Central.
DR Gene3D; 4.10.1040.10; -; 2.
DR InterPro; IPR001275; DM_DNA-bd.
DR InterPro; IPR036407; DM_DNA-bd_sf.
DR InterPro; IPR026607; DMRT.
DR PANTHER; PTHR12322; PTHR12322; 2.
DR Pfam; PF00751; DM; 2.
DR SMART; SM00301; DM; 2.
DR SUPFAM; SSF82927; SSF82927; 2.
DR PROSITE; PS40000; DM_1; 2.
DR PROSITE; PS50809; DM_2; 2.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..348
FT /note="Doublesex- and mab-3-related transcription factor
FT dmd-10"
FT /id="PRO_0000453457"
FT DNA_BIND 43..91
FT /note="DM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT DNA_BIND 119..166
FT /note="DM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT REGION 316..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38837 MW; 85354DA822575E90 CRC64;
MVADVLRQSV LVPISMYPQY PVPRRYTTSV FKEYQKKKKI YYCQRCLNHD VPRPRKNHKC
ECPYADCTCE KCGLVEKRRI LNIRLQNYNQ FNIENENDSK LIIVEDDDKK KQGERVPNCQ
KCGQHGRKSR LKGHKRSCPF RECPCAKCAV VSERQKLMAD QIKIRRRQRK DTLLTFAKNS
ITSTMFPSNQ ISLNALNSLL YGSINTSPQP LLSSPTSSDA SSCSPSMPFT PSIPMFMPTS
ADCSPTTQTP TSSIPSSIAS TSPLMTSLPL RLSGFPLLNI RDPSAEASLL NLGCNADAAA
LLKTILDQYR MLEEASMSMS SSPSKDDESG DEDSDGLNSN SIIDVITV
