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0HXD3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHOXD3
DescriptionHomeobox protein hox-d3 (hox-4a).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Helix-turn-helix (HTH) motifs are found in all known DNA binding proteinsthat regulate gene expression. The motif consists of approximately 20 residues and is characterised by 2 alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix of the HTH motif binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA . Thefirst helix helps to stabilise the structure . The HTH motif is very similar in sequence and structure to the N-terminal region of the lamda and other repressor proteins.nd has also been identified in many other DNA-binding proteins on the basis of sequence and structural similarity . One of the principal differences between HTH motifs in these different proteins arises from the stereochemical requirement for glycine in the turn.hich is needed to avoid steric interference of the beta-carbon with the main chain: for cro and other repressors the Gly appears to be mandatory.hile for many of the homeoticand other DNA-binding proteins the requirement is relaxed.
  IPR000047:Helix-turn-helix motif, lambda-like repressor
The homeobox domain was first identified in a number of drosophila homeotic and segmentation proteins.ut is now known to be well-conserved in many other animals.ncluding vertebrates . Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies . The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA . The first helix helps to stabilise the structure. The motif is very similar in sequence and structure in a wide range of DNA-binding proteins (e.g..ro and repressor proteins.omeotic proteins.tc.). One of the principal differences between HTH motifs in these different proteins arises from the stereo-chemical requirement for glycine in the turn which is needed to avoid steric interference of the beta-carbon with the main chain: for cro and repressor proteins the glycine appears to be mandatory.hile for many of the homeotic and other DNA-binding proteins the requirement is relaxed.
  IPR001356:Homeobox
The homeobox is a 60-residue motif first identified in a number of Drosophila homeotic and segmentation proteins.ut now known to be well-conserved in many other animals.ncluding vertebrates . Proteins containing homeobox domains are likely to play an important role in development - most are known to be sequence-specific DNA-binding transcription factors. The domain binds DNA through a helix-turn-helix (HTH) structure.Many homeodomain-containing proteins have now been sequenced and.hile the homeodomain flanking regions vary.haracteristic conserved sequences upstream of the domain allow the proteins to be grouped into 3 subfamilies: the so-called antennapedia.ngrailed and paired box proteins. Antennapedia.hich regulates the formation of leg structures in Drosophila.as one of the first homeotic genes studied and led to the discovery of the homeobox domain. Over expression of this gene in the wrong segment of the fruit fly can lead to the formation of leg structures in these segments. For example.ver expression in the head segment can lead to the formation of legs instead of antennae (hence the name antennapedia). The sequences of the antennapedia proteins contain a conserved hexapeptide 5-16 residues upstream of the homeobox.he specific function of which is unclear. The six Drosophila proteins that belong to this group are antennapedia (Antp).bdominal-A (abd-A).eformed (Dfd).roboscipedia (pb).ex combs reduced (scr) and ultrabithorax (ubx) and are collectively known as the antennapedia subfamily.In vertebrates the corresponding Hox genes are known as Hox-A2.3.4.5.6.7.ox-B1.2.3.4.5.6.7.8.ox-C4.5.6.8.ox-D1.3.4 and D8.Caenorhabditis elegans lin-39 and mab-5 are also members of the antennapedia subfamily.Arg and Lys are most frequently found in the last position of the hexapeptide; other amino acids are found in only a few cases.
  IPR001827:Homeobox protein, antennapedia type
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR009057:Homeodomain-like
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR012287:Homeodomain-related
IPR001356:Homeobox 
Evalue:-30.6382713317871 
Location:179-235IPR001827:ANTENNAPEDIA 
Evalue:0 
Location:143-150
SequencesProtein: HXD3_HUMAN (416 aa)
mRNA: BC005124 NM_006898
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 31 residues, 176737050-176737142Exon2: 210 residues, 176742004-176742629Exon3: 529 residues, 176744490-176746072Exon4: 2 residues, -Jump to HXD3_HUMANExon1: 31 residues, 176737050-176737142Exon2: 210 residues, 176742004-176742629Exon3: 529 residues, 176744490-176746072Exon4: 2 residues, -Jump to HXD3_HUMAN  
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