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DMD3_CAEEL
ID   DMD3_CAEEL              Reviewed;         250 AA.
AC   Q9XWN9; C8TDI6;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Doublesex- and mab-3-related transcription factor dmd-3 {ECO:0000305};
DE   AltName: Full=Doublesex-like 3 protein homolog {ECO:0000305};
GN   Name=dmd-3 {ECO:0000303|PubMed:18550714, ECO:0000312|WormBase:Y43F8C.10a};
GN   ORFNames=Y43F8C.10 {ECO:0000312|WormBase:Y43F8C.10a};
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, REPRESSION BY LIN-41,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=18550714; DOI=10.1242/dev.017046;
RA   Mason D.A., Rabinowitz J.S., Portman D.S.;
RT   "dmd-3, a doublesex-related gene regulated by tra-1, governs sex-specific
RT   morphogenesis in C. elegans.";
RL   Development 135:2373-2382(2008).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA   Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA   Shah K., Fitch D.H.;
RT   "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT   wide RNAi screen in Caenorhabditis elegans.";
RL   PLoS Genet. 7:E1002010-E1002010(2011).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22069471; DOI=10.1371/journal.pone.0026811;
RA   Siehr M.S., Koo P.K., Sherlekar A.L., Bian X., Bunkers M.R., Miller R.M.,
RA   Portman D.S., Lints R.;
RT   "Multiple doublesex-related genes specify critical cell fates in a C.
RT   elegans male neural circuit.";
RL   PLoS ONE 6:E26811-E26811(2011).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=28065609; DOI=10.1016/j.cub.2016.11.045;
RA   Serrano-Saiz E., Oren-Suissa M., Bayer E.A., Hobert O.;
RT   "Sexually Dimorphic Differentiation of a C. elegans Hub Neuron Is Cell
RT   Autonomously Controlled by a Conserved Transcription Factor.";
RL   Curr. Biol. 27:199-209(2017).
RN   [6] {ECO:0000305}
RP   REPRESSION BY LIN-41.
RX   PubMed=28111013; DOI=10.1016/j.molcel.2016.12.010;
RA   Aeschimann F., Kumari P., Bartake H., Gaidatzis D., Xu L., Ciosk R.,
RA   Grosshans H.;
RT   "LIN41 post-transcriptionally silences mRNAs by two distinct and position-
RT   dependent mechanisms.";
RL   Mol. Cell 65:476-489(2017).
RN   [7] {ECO:0000305}
RP   FUNCTION, REPRESSION BY LIN-41, AND TISSUE SPECIFICITY.
RX   PubMed=30910805; DOI=10.26508/lsa.201900335;
RA   Aeschimann F., Neagu A., Rausch M., Grosshans H.;
RT   "let-7 coordinates the transition to adulthood through a single primary and
RT   four secondary targets.";
RL   Life. Sci Alliance 2:0-0(2019).
CC   -!- FUNCTION: Transcriptional activator which promotes male-specific
CC       development (PubMed:18550714, PubMed:28065609). Acts partially
CC       redundantly with the transcription factor mab-3 to coordinate tail tip
CC       cell fusion and retraction and thereby regulate male tail tip
CC       morphogenesis (PubMed:18550714, PubMed:30910805). This is most likely
CC       through the regulation of downstream effectors such as eff-1
CC       (PubMed:18550714). May also negatively regulate the expression of other
CC       proteins implicated in male tail morphogenesis including nhr-25, vav-1
CC       and arl-1 in tail tip cells (PubMed:21408209). In males, plays a role
CC       in the development of ray A-neurons by negatively regulating the
CC       activity of the transcription factor ast-1 (PubMed:22069471). Plays a
CC       role in the male-specific differentiation of PHC sensory neurons into
CC       densely connected hub sensory neurons (PubMed:28065609). Plays a role
CC       in male mating behavior (PubMed:22069471).
CC       {ECO:0000269|PubMed:18550714, ECO:0000269|PubMed:21408209,
CC       ECO:0000269|PubMed:22069471, ECO:0000269|PubMed:28065609,
CC       ECO:0000269|PubMed:30910805}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
CC       Perikaryon {ECO:0000269|PubMed:22069471}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:Y43F8C.10a};
CC         IsoId=Q9XWN9-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:Y43F8C.10b};
CC         IsoId=Q9XWN9-2; Sequence=VSP_060329;
CC   -!- TISSUE SPECIFICITY: In males, expressed in the tail tip
CC       (PubMed:18550714, PubMed:21408209, PubMed:22069471, PubMed:30910805).
CC       Specifically, expressed in 15 male-specific muscles of the tail tip
CC       called the diagonal muscles, and also in core body muscles of both
CC       males and hermaphrodites (PubMed:22069471). In males, expressed in ray
CC       A-neurons (PubMed:18550714, PubMed:22069471). In males, expressed in
CC       PHC sensory neurons (PubMed:28065609). In males, it is also expressed
CC       in the hindgut, B lineage and somatic gonad (PubMed:18550714). In
CC       hermaphrodites, expressed in the anchor cell only (PubMed:18550714).
CC       {ECO:0000269|PubMed:18550714, ECO:0000269|PubMed:21408209,
CC       ECO:0000269|PubMed:22069471, ECO:0000269|PubMed:28065609,
CC       ECO:0000269|PubMed:30910805}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cells of the male tail tip from the
CC       L3 larval stage. Expression peaks during male tail tip retraction and
CC       decreases rapidly upon completion (PubMed:18550714). Not expressed in
CC       cells of the hermaphrodite tail tip at any developmental stage
CC       (PubMed:18550714). {ECO:0000269|PubMed:18550714}.
CC   -!- INDUCTION: Negatively regulated by lin-41 which causes degradation of
CC       the mRNA encoding this protein. {ECO:0000269|PubMed:18550714,
CC       ECO:0000269|PubMed:28111013, ECO:0000269|PubMed:30910805}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in male tail
CC       morphology defects. {ECO:0000269|PubMed:18550714}.
CC   -!- SIMILARITY: Belongs to the DMRT family. {ECO:0000305}.
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DR   EMBL; BX284605; CAA21612.2; -; Genomic_DNA.
DR   EMBL; BX284605; CBG22749.1; -; Genomic_DNA.
DR   PIR; T26871; T26871.
DR   RefSeq; NP_001256882.1; NM_001269953.1. [Q9XWN9-1]
DR   RefSeq; NP_001256883.1; NM_001269954.1. [Q9XWN9-2]
DR   AlphaFoldDB; Q9XWN9; -.
DR   SMR; Q9XWN9; -.
DR   IntAct; Q9XWN9; 2.
DR   STRING; 6239.Y43F8C.10a; -.
DR   PaxDb; Q9XWN9; -.
DR   EnsemblMetazoa; Y43F8C.10a.1; Y43F8C.10a.1; WBGene00012832. [Q9XWN9-1]
DR   EnsemblMetazoa; Y43F8C.10b.1; Y43F8C.10b.1; WBGene00012832. [Q9XWN9-2]
DR   GeneID; 189878; -.
DR   KEGG; cel:CELE_Y43F8C.10; -.
DR   UCSC; Y43F8C.10; c. elegans. [Q9XWN9-1]
DR   CTD; 189878; -.
DR   WormBase; Y43F8C.10a; CE39835; WBGene00012832; dmd-3. [Q9XWN9-1]
DR   WormBase; Y43F8C.10b; CE44151; WBGene00012832; dmd-3. [Q9XWN9-2]
DR   eggNOG; KOG3815; Eukaryota.
DR   GeneTree; ENSGT00970000196492; -.
DR   HOGENOM; CLU_122995_0_0_1; -.
DR   InParanoid; Q9XWN9; -.
DR   OMA; CIMVERR; -.
DR   OrthoDB; 1553372at2759; -.
DR   PhylomeDB; Q9XWN9; -.
DR   PRO; PR:Q9XWN9; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00012832; Expressed in larva and 2 other tissues.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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:0048675; P:axon extension; IMP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR   GO; GO:0048664; P:neuron fate determination; IMP:UniProtKB.
DR   GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   GO; GO:1902435; P:regulation of male mating behavior; IMP:UniProtKB.
DR   GO; GO:0110037; P:regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Sexual differentiation;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..250
FT                   /note="Doublesex- and mab-3-related transcription factor
FT                   dmd-3"
FT                   /id="PRO_0000448063"
FT   DNA_BIND        19..68
FT                   /note="DM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT   DNA_BIND        117..164
FT                   /note="DM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..111
FT                   /note="MNIEEILPELFGEKRVYYCQRCLNHGLREKRKNHKLSCTFRFCQCSNCIMVE
FT                   RRRQLNSRLMQIDGSRDEKPMTTLTMALTCSEEDQMECTSQSETTNESSGEDKDDGKPK
FT                   -> MTQTFIRLKSSVKVDRD (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060329"
SQ   SEQUENCE   250 AA;  28649 MW;  EF92481A482A7D61 CRC64;
     MNIEEILPEL FGEKRVYYCQ RCLNHGLREK RKNHKLSCTF RFCQCSNCIM VERRRQLNSR
     LMQIDGSRDE KPMTTLTMAL TCSEEDQMEC TSQSETTNES SGEDKDDGKP KERRPNCQRC
     AQHSVVNRLK GHKRACPFRD CFCAKCQVVV ERQKLMADQI KLRRRQKREK NNLNSEREAP
     IAHSMTPSPI DTVTTTTTPT SETSTPMCLK CAQQVIGYQQ LLSLLDPSAT LQDPMITLSA
     VLSACPHKNE
 
 
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