TENM3

{{Short description|Protein-coding gene in the species Homo sapiens}} {{#invoke:Infobox_gene|getTemplateData|QID=Q18041985}} '''Teneurin-3''', also known as '''Ten-m3''', '''Odz3''', '''Ten-m/Odz3''', '''Tenascin-like molecule major 3''' or '''Teneurin transmembrane protein 3''', is a protein that, in humans, is encoded by the ''TENM3'', or ''ODZ3'', gene.<ref name="pmid7684246">{{cite journal | vauthors=Baumgartner S, Chiquet-Ehrismann R | title = Tena, a Drosophila gene related to tenascin, shows selective transcript localization | journal = Mechanisms of Development | volume = 40 | issue = 3 | pages = 165–76 | date = March 1993 | pmid = 7684246 | doi = 10.1016/0925-4773(93)90074-8 | s2cid = 38892756 }}</ref><ref name="pmid7514504">{{cite journal | vauthors=Levine A, Bashan-Ahrend A, Budai-Hadrian O, Gartenberg D, Menasherow S, Wides R | title = odd Oz: A novel Drosophila pair rule gene | journal = Cell | volume = 77 | issue = 4 | pages = 587–98 | date = May 1994 | pmid = 7514504 | doi = 10.1016/0092-8674(94)90220-8| s2cid = 32035939 }}</ref><ref name="pmid10341219">{{cite journal | vauthors=Minet AD, Rubin BP, Tucker RP, Baumgartner S, Chiquet-Ehrismann R | title = Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain | journal = Journal of Cell Science | volume = 112 | issue = Pt 12 | pages = 2019–32 | date = June 1999 | doi = 10.1242/jcs.112.12.2019 | pmid = 10341219| url = https://lup.lub.lu.se/record/17313ef0-1fb0-4eba-bf26-d19df57fcd82 | url-access = subscription }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TENM3 teneurin transmembrane protein 3| url = https://www.ncbi.nlm.nih.gov/gene/55714| access-date = 2017-10-22}}</ref> Ten-m3 is a ~300 kDa type II transmembrane glycoprotein that is a member of the teneurin/Ten-m/Odz family. The teneurin family currently consists of four members: Ten-m1-Ten-m4. Ten-ms are conserved across both vertebrate and invertebrate species. They are expressed in distinct, but often interconnected, areas of the developing nervous system and in some non-neural tissues. Like the Ten-m family, Ten-m3 plays a critical role in regulating connectivity of the nervous system, particularly in axon pathfinding and synaptic organisation in the motor and visual system.<ref name="pmid16406038">{{cite journal | vauthors=Tucker RP, Chiquet-Ehrismann R | title = Teneurins: A conserved family of transmembrane proteins involved in intercellular signaling during development | journal = Developmental Biology | volume = 290 | issue = 2 | pages = 237–45 | date = February 2006 | pmid = 16406038 | doi = 10.1016/j.ydbio.2005.11.038| doi-access = free }}</ref><ref name="pmid18723111">{{cite journal | vauthors=Young TR, Leamey CA | title = Teneurins: Important regulators of neural circuitry | journal = International Journal of Biochemistry & Cell Biology | volume = 41 | issue = 5 | pages = 990–3 | date = May 2009 | pmid = 18723111 | doi = 10.1016/j.biocel.2008.06.014}}</ref> Mutation in the ''TENM3''/''ODZ3'' gene in humans has been associated with the eye condition, microphthalmia.<ref name="pmid22766609">{{cite journal | vauthors=Aldahmesh MA, Mohammed JY, Al-Hazzaa S, Alkuraya FS | title = Homozygous null mutation in ODZ3 causes microphthalmia in humans | journal = Genetics in Medicine | volume = 14 | issue = 11 | pages = 900–4 | date = November 2012 | pmid = 22766609 | doi = 10.1038/gim.2012.71| doi-access = free }}</ref>

==History== Teneurin protein was first identified and characterised in ''Drosophila'' by Baumgartner and Chiquet-Ehrismann in early 1990s.<ref name="pmid7684246"/> They were looking for the invertebrate homologue of the extracellular matrix glycoprotein tenascin-C to learn more about its structure and function. The embryonic ''Drosophila'' cDNA library was screened using polymerase chain reaction (PCR) and a primer derived from the EGF-like repeats region of chicken tenascin-C protein. Two novel molecules containing similar tenascin-like repeats were identified, which were named Ten-a for "tenascin-like molecule accessory" and Ten-m for "tenascin-like molecule major".<ref name="pmid7684246"/><ref name="pmid16406038"/> Around the same time, Levine et al.<ref name="pmid7514504"/> also identified Ten-m in ''Drosophila'' by screening for tyrosine phosphorylation on cDNA using monoclonal antibodies. However, they named this gene ''odd Oz'' (''Odz'') after the oddless pair-rule phenotype displayed in ''Odz'' mutant embryos, where every odd-numbered body segment was deleted. Since discovery of teneurins in ''Drosophila'', many other laboratories have independently described the Ten-a and Ten-m/Odz homolog proteins in different vertebrates. However, various names were assigned to these vertebrate homologs, which complicated the nomenclature of teneurin proteins.<ref name="pmid16406038"/> The proteins were called Ten-ms in zebrafish,<ref name="pmid10495292">{{cite journal | vauthors=Mieda M, Kikuchi Y, Hirate Y, Aoki M, Okamoto H | title = Compartmentalized expression of zebrafish ten-m3 and ten-m4, homologues of the Drosophila ten(m)/odd Oz gene, in the central nervous system | journal = Mechanisms of Development | volume = 87 | issue = 1 | pages = 223–7 | date = September 1999 | pmid = 10495292 | doi = 10.1016/S0925-4773(99)00155-0| doi-access = }}</ref> teneurins in chicken,<ref name="pmid10588872">{{cite journal | vauthors=Rubin BP, Tucker RP, Martin D, Chiquet-Ehrismann R | title = Teneurins: A Novel Family of Neuronal Cell Surface Proteins in Vertebrates, Homologous to the Drosophila Pair-Rule Gene Product Ten-m | journal = Developmental Biology | volume = 216 | issue = 1 | pages = 195–209 | date = December 1999 | pmid = 10588872 | doi = 10.1006/dbio.1999.9503| doi-access = free }}</ref> Ten-m1-4, Odz1-4, Ten-m/Odz1-4, DOC4 in mouse,<ref name="pmid10225957">{{cite journal | vauthors=Oohashi T, Zhou XH, Feng K, Richter B, Mörgelin M, Perez MT, Su WD, Chiquet-Ehrismann R, Rauch U, Fässler R | title = Mouse Ten-m/Odz Is a New Family of Dimeric Type II Transmembrane Proteins Expressed in Many Tissues | journal = The Journal of Cell Biology | volume = 145 | issue = 3 | pages = 563–77 | date = May 1999 | pmid = 10225957 | pmc = 2185078 | doi = 10.1083/jcb.145.3.563}}</ref><ref name="pmid9649432">{{cite journal | vauthors=Wang XZ, Kuroda M, Sok J, Batchvarova N, Kimmel R, Chung P, Zinszner H, Ron D | title = Identification of novel stress-induced genes downstream of chop | journal = The EMBO Journal | volume = 17 | issue = 13 | pages = 3619–30 | date = July 1998 | pmid = 9649432 | pmc = 1170698 | doi = 10.1093/emboj/17.13.3619}}</ref> neurestin in rat,<ref name="pmid10419693">{{cite journal | vauthors=Otaki JM, Firestein S | title = Neurestin: Putative Transmembrane Molecule Implicated in Neuronal Development | journal = Developmental Biology | volume = 212 | issue = 1 | pages = 165–81 | date = August 1999 | pmid = 10419693 | doi = 10.1006/dbio.1999.9310| doi-access = free }}</ref> and teneurin or Odz in human.<ref name="pmid10331952">{{cite journal | vauthors=Ben-Zur T, Wides R | title = Mapping Homologs of Drosophila odd Oz(odz):Doc4/Odz4 to Mouse Chromosome 7, Odz1 to Mouse Chromosome 11; and ODZ3 to Human Chromosome Xq25 | journal = Genomics | volume = 58 | issue = 1 | pages = 102–3 | date = May 1999 | pmid = 10331952 | doi = 10.1006/geno.1999.5798}}</ref><ref name="pmid10341219"/> The name teneurin was coined by Minet et al. in 1999<ref name="pmid10341219"/> from the original name, Ten-a, and the major site of the protein expression being in the nervous system.

==Structure== [[File:Ten-m3_Structure.png | thumb| Schematic diagram of the hypothesised structure of a pair of dimerised mouse teneurin molecules. The extracellular domain of the teneurin protein consists of a linker region, a region of EGF-like repeats with a cysteine on the second and fifth repeats for dimerisation, and a globular domain. The globular domain consists of a cysteine-rich region, five NHL repeats, 26 YD repeats and the TCAP. The intracellular domain consists of two polyproline domains, two EF-hand-like motifs and tyrosine phosphorylation sites. Adapted from.<ref name="pmid18723111"/><ref name="renamed_from_25152333_on_20171115040513">{{cite journal | vauthors=Leamey CA, Sawatari A | title = The teneurins: new players in the generation of visual topography | journal = Seminars in Cell & Developmental Biology | volume = 35 | pages = 173–9 | date = November 2014 | pmid = 25152333 | doi = 10.1016/j.semcdb.2014.08.007}}</ref>]] Like the Ten-m family, Ten-m3 is a large type II transmembrane glycoprotein that has a molecular weight of ~300 kDa and is composed of ~2800 amino acids. Teneurins are highly conserved within and between species. The primary structure, or amino acid sequence identity, of the proteins between paralogs is ~60% identical and between orthologs is ~90%, whilst between vertebrates and ''Drosophila'' or ''C. elegans'' is only 33-41% identical.<ref name="pmid16406038"/> All teneurins, especially in mouse, are type II transmembrane proteins that are composed of a large extracellular C terminal domain of ~2400 amino acid residues, a single transmembrane helical domain of ~30 hydrophobic residues and an intracellular N terminal domain of ~300-375 residues.<ref name="pmid16406038"/> The extracellular domain of the molecule can undergo dimerisation.

===Extracellular domain=== The extracellular C terminal domain is composed of a linker region, EGF-like repeats and then a globular domain. The linker region is made up of ~200 amino acid residues and is found immediately distal to the transmembrane domain. This is followed by eight phylogenetically conserved tenascin C-type EGF-like repeats, which features the uniquely conserved replacement of a single cysteine in repeats 2 and 5 in place of the original tyrosine and phenylalanine residues respectively. Since cysteines are susceptible to forming disulfide bonds, the single cysteines at the EGF-like repeats of a teneurin molecule can facilitate the homophilic and heterophilic dimerisation of teneurin family molecules.<ref name="pmid10225957"/> More distally is the globular domain consisting of a 700-800 amino acid residue region. There are 17 conserved cysteine residues, a region of NHL repeats, a region of 26 YD residue repeats, and then a teneurin C-associated peptide (TCAP). The YD repeats are rich in N-linked glycosylation and were previously only reported in the ''rhs'' element of bacteria.<ref name="pmid23688238">{{cite journal | vauthors=Beckmann J, Schubert R, Chiquet-Ehrismann R, Müller DJ | title = Deciphering teneurin domains that facilitate cellular recognition, cell-cell adhesion and neurite outgrowth using atomic force microscopy-based single-cell force spectroscopy | journal = Nano Letters | volume = 13 | issue = 6 | pages = 2937–46 | date = June 2013 | pmid = 23688238 | doi = 10.1021/nl4013248| bibcode = 2013NanoL..13.2937B | doi-access = free | hdl = 20.500.11850/73745 | hdl-access = free }}</ref><ref name="pmid11054571">{{cite journal | vauthors=Minet AD, Chiquet-Ehrismann R | title = Phylogenetic analysis of teneurin genes and comparison to the rearrangement hot spot elements of E. coli | journal = Gene | volume = 257 | issue = 1 | pages = 87–97 | date = October 2000 | pmid = 11054571 | doi = 10.1016/S0378-1119(00)00388-7}}</ref> The TCAP is the resulting peptide from cleaving a putative furin cleavage site found immediately on the N-terminal of TCAP. The furin cleavage site is rich in tyrosine residues and consists of 4 conserved cysteine residues. The 4 cysteine residues assist in protein folding, however, they are absent in Ten-m2 and Ten-m3. There are 41 amino acids in TCAPs, except for TCAP-3 from Ten-m3, which has 40.<ref name="pmid15158132">{{cite journal | vauthors=Qian X, Barsyte-Lovejoy D, Wang L, Chewpoy B, Gautam N, Al Chawaf A, Lovejoy DA | title = Cloning and characterization of teneurin C-terminus associated peptide (TCAP)-3 from the hypothalamus of an adult rainbow trout (Oncorhynchus mykiss) | journal = General and Comparative Endocrinology | volume = 137 | issue = 2 | pages = 205–16 | date = June 2004 | pmid = 15158132 | doi = 10.1016/j.ygcen.2004.02.007}}</ref> TCAPs show structural homology to the CRF family molecule and appears to influence neurite outgrowth and some behaviours relating to stress and anxiety.<ref name="pmid16406038"/><ref name="pmid18723111"/>

===Intracellular domain=== The N terminal intracellular domain (ICD) consists of two proline-rich regions in the half closest to the transmembrane domain, two EF-hand-like motifs near the centre, and a number of conserved tyrosine phosphorylation sites. The proline-rich stretches are typical binding sites for SH3 proteins, which can regulate intracellular teneurin signalling pathway.<ref name="pmid15777793">{{cite journal | vauthors=Nunes SM, Ferralli J, Choi K, Brown-Leudi M, Minet AD, Chiquet-Ehrismann R | title = The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin resulting in subcellular codistribution and translocation to the nuclear matrix | journal = Experimental Cell Research | volume = 305 | issue = 1 | pages = 122–32 | date = April 2005 | pmid = 15777793 | doi = 10.1016/j.yexcr.2004.12.020}}</ref>

==Interactions== Teneurins are homophilic adhesion molecules that bind specifically to other teneurin-family molecules on adjacent cells. The NHL domain on the extracellular domain of teneurins acts as a homophilic recognition site to mediate this specific binding. This interaction facilitates neurite outgrowth and the adhesion strength needed to stop outgrowth.<ref name="pmid23688238"/> The dimerisation of the extracellular domains of teneurin molecules can lead to the proteolytic cleavage of the ICD. A weak nuclear localisation signal in the ICD of Ten-m3 facilitates the translocation of the ICD into the nucleus.<ref name="pmid22045996">{{cite journal | vauthors=Tucker RP, Beckmann J, Leachman NT, Schöler J, Chiquet-Ehrismann R | title = Phylogenetic Analysis of the Teneurins: Conserved Features and Premetazoan Ancestry | journal = Molecular Biology and Evolution | volume = 29 | issue = 2 | pages = 1019–29 | date = March 2012 | pmid = 22045996 | pmc = 3278476 | doi = 10.1093/molbev/msr271}}</ref><ref name="renamed_from_25152333_on_20171115040513"/> TCAPs from the extracellular domain of a teneurin molecule can form an intercellular adhesive complex when bound to the adhesion family G-protein coupled receptor latrophilin, which is involved in gamete migration and gonadal morphology.<ref name="pmid26485751">{{cite journal | vauthors=Lovejoy DA, Pavlović T | title = Role of the teneurins, teneurin C-terminal associated peptides (TCAP) in reproduction: clinical perspectives | journal = Hormone Molecular Biology and Clinical Investigation | volume = 24 | issue = 2 | pages = 83–90 | date = November 2015 | pmid = 26485751 | doi = 10.1515/hmbci-2015-0032| s2cid = 35441943 }}</ref>

==Expression== Teneurin molecules are prominently expressed in distinctive, but often overlapping, populations of neurons, especially during embryonic development. They are also expressed in some non-neuronal tissues that regulate pattern formation and sites of cell migration. Some Ten-m3 expressions can occur in a high-to-low gradient.<ref name="pmid12915301">{{cite journal | vauthors=Zhou XH, Brandau O, Feng K, Oohashi T, Ninomiya Y, Rauch U, Fässler R | title = The murine Ten-m/Odz genes show distinct but overlapping expression patterns during development and in adult brain | journal = Gene Expression Patterns | volume = 3 | issue = 4 | pages = 397–405 | date = August 2003 | pmid = 12915301 | doi = 10.1016/S1567-133X(03)00087-5}}</ref><ref name="pmid16406038"/>

===Embryonic expression=== At day 7.5 in mouse embryonic development (E7.5), ''in situ'' hybridisation shows ''Ten-m3'' mRNA expression at the neural plate, particularly in the neural folds. At E8.5, ''Ten-m3'' is expressed at the caudal forebrain, the midbrain region and structures outside of the CNS, including the pharyngeal arches and the otic vesicles. At E9.5 and 10.5, ''Ten-m3'' expression extends from the telencephalon to the midbrain and also at the pharyngeal arches, otic vesicles, anterior somites and the limb buds. Between these stages, ''Ten-m3'' and ''Ten-m4'' are expressed in complementary patterns in the brain, suggesting a complementary function during development. At E12.5, ''Ten-m3'' is higher in the midbrain compared to the caudal diencephalon and the spinal cord. It is also co-expressed with ''Ten-m4'' in the first, second and third pharyngeal arches. At E15.5, ''Ten-m3'' is expressed in the forebrain and facial mesenchyme, but absent from the mid- and hindbrain. It is also expressed in the developing whisker pads in mouse.<ref name="pmid10495292"/><ref name="pmid12915301"/>

===Adult expression=== In a 6-week-old adult mouse, ''Ten-m3'' is co-expressed with the other three ''Ten-m'' mRNAs at the granular layer of the dentate gyrus and the stratum pyramidale of the hippocampus. It is expressed relatively weakly in the granular layer and in the stratum lacunosum moleculare, but is strongly expressed in the CA2 subfield and weakly in the CA1 subfield of the hippocampus. However, immunostaining of Ten-m3 shows weak protein expression throughout the hippocampus except for the stratum lacunosum moleculare. ''Ten-m3'' mRNA is prominently co-expressed with ''Ten-m2'' and ''Ten-m4'' in the Purkinje's cell zone of the cerebellum. Ten-m3 protein is expressed in the Purkinje's cell zone, molecular and granular layers and the white matter of the cerebellum. All Ten-m mRNAs are expressed prominently between layers II and VI of the cerebrum.<ref name="pmid12915301"/>

===Gradient expression=== The ''Ten-m3'' gene, along with ''Ten-m2'' and ''Ten-m4'', is expressed throughout the neocortex in a low rostral to high caudal and a high dorsal-medial to low ventral-lateral gradient from E15.5 to P2.<ref name="pmid16919471">{{cite journal | vauthors=Li H, Bishop KM, O'Leary DD | title = Potential target genes of EMX2 include Odz/Ten-M and other gene families with implications for cortical patterning | journal = Molecular and Cellular Neuroscience | volume = 33 | issue = 2 | pages = 136–49 | date = October 2006 | pmid = 16919471 | doi = 10.1016/j.mcn.2006.06.012| s2cid = 24032841 }}</ref> In E17 mouse, ''Ten-m3'' mRNA is expressed in the parafascicular thalamic nucleus, a subregion of the thalamus, and in the striatum in a high dorsal-caudal to low ventral-rostral gradient. Patches of this expression can still be observed in first week postnatal mice.<ref name="pmid17478416">{{cite journal | vauthors=Leamey CA, Glendining KA, Kreiman G, Kang ND, Wang KH, Fassler R, Sawatari A, Tonegawa S, Sur M | title = Differential Gene Expression between Sensory Neocortical Areas: Potential Roles for Ten_m3 and Bcl6 in Patterning Visual and Somatosensory Pathways | journal = Cerebral Cortex | volume = 18 | issue = 1 | pages = 53–66 | date = January 2008 | pmid = 17478416 | doi = 10.1093/cercor/bhm031| doi-access = free }}</ref><ref name="pmid25406022">{{cite journal | vauthors=Tran H, Sawatari A, Leamey CA | title = The glycoprotein Ten-m3 mediates topography and patterning of thalamostriatal projections from the parafascicular nucleus in mice | journal = European Journal of Neuroscience | volume = 41 | issue = 1 | pages = 55–68 | date = January 2015 | pmid = 25406022 | doi = 10.1111/ejn.12767| s2cid = 28180602 }}</ref> Similarly, there is a graded expression of Ten-m3 in the visual pathway, especially during embryonic and early postnatal development. Expression is highest in the dorsal lateral geniculate nucleus (dLGN) and superior colliculus in the region that corresponds topographically to ventral retina.<ref name="pmid17803360">{{cite journal | vauthors=Leamey CA, Merlin S, Lattouf P, Sawatari A, Zhou X, Demel N, Glendining KA, Oohashi T, Sur M, Fässler R | title = Ten_m3 regulates eye-specific patterning in the mammalian visual pathway and is required for binocular vision | journal = PLOS Biology | volume = 5 | issue = 9 | article-number = e241 | date = September 2007 | pmid = 17803360 | pmc = 1964777 | doi = 10.1371/journal.pbio.0050241 | doi-access = free }}</ref><ref name="renamed_from_25152333_on_20171115040513"/>

==Function== ===Motor skill acquisition=== Ten-m3 plays an important role during early development in directing the topographic neural projection and formation of the thalamostriatal circuitry, thus critical for motor skill acquisition. Ten-m3 molecule is the first to be reported to regulate connectivity in the thalamostriatal pathway. Ten-m3 guides some of the axon projections from dorsal regions of the parafascicular nucleus (PF) of the thalamus to dorsal regions of the striatum. This creates a high dorsal to low ventral gradient topography mapping between the two structures. In Ten-m3 null mutant mice, these projections are diffuse and project ectopically to more ventral and medial regions in the striatum. Furthermore, the null mutant mice display delayed motor skill acquisition in the accelerating rotorod task.<ref name="pmid25406022"/>

===Binocular vision=== In ''in vivo'' vertebrate studies, Ten-m3 acts as an eye-specific guidance molecule during early development. Functional binocular vision requires the correct projection of ipsilateral axons from the retina to the dorsal lateral geniculate nucleus (dLGN) and primary visual cortex (V1) and to the superior colliculus (SC). Ten-m3 facilitates the retinotopic mapping of ipsilateral axons from the ventrotemporal retinal ganglion cells, which encode visual input from the binocular visual field, to the dorsomedial dLGN and to the rostromedial SC. Immunostaining reveals a cluster of high Ten-m3 protein expression in the areas involved in this ipsilateral mapping. In Ten-m3 null mutant mice, these projections are reduced and ectopic projections are expanded ventrolaterally along the dLGN and caudomedially in the SC from both eyes. The aberrant misalignment of ipsilateral axons from both eyes result in binocular vision deficits. Ten-m3 null mutant mice performed worse than wild type (WT) in behavioural tests of binocular visual function, such as vertical placement and visual cliff test. However, inactivation of inputs from one eye (i.e. inactivate binocular vision) restored visual behaviour to a level similar to WT mice under binocular condition.<ref name="pmid17803360"/><ref name="renamed_from_25152333_on_20171115040513"/>

===Teneurin C-Associated Peptide functions=== The peptide cleaved from the C terminal of Ten-m3, TCAP-3, stimulates the production of cAMP and the proliferation of neurons. It can increase the expression of its gene at high concentrations but attenuate the expression at low concentrations.<ref name="pmid15158132"/> TCAP-1 from Ten-m1, another member of the Ten-m family, modulates stress and anxiety behaviours. TCAP-1 increases the acoustic startle response in a low-anxiety rat but decreases the response in a high anxiety rat when injected into the basolateral amygdala. It also inhibits the sensitisation of the response when injected into the lateral ventricles.<ref name="pmid15710242">{{cite journal | vauthors=Wang L, Rotzinger S, Al Chawaf A, Elias CF, Barsyte-Lovejoy D, Qian X, Wang NC, De Cristofaro A, Belsham D, Bittencourt JC, Vaccarino F, Lovejoy DA | title = Teneurin proteins possess a carboxy terminal sequence with neuromodulatory activity | journal = Molecular Brain Research | volume = 133 | issue = 2 | pages = 253–65 | date = February 2005 | pmid = 15710242 | doi = 10.1016/j.molbrainres.2004.10.019}}</ref>

==Disease Linkage== A case study reports a family with autosomal recessive colobomatous microphthalmia in two children of third-cousin parents. This developmental condition results in small-sized eyes and is associated with coloboma. PCR analysis identified the homozygous null mutation to be in the ''ODZ3'' gene, which is important for the early developing eye.<ref name="pmid22766609"/>

==References== {{reflist}}

== Further reading ==

{{refbegin | 2}} *{{Cite journal | last1 = Ben-Zur | first1 = T. | last2 = Feige | first2 = E. | last3 = Motro | first3 = B. | last4 = Wides | first4 = R. | title = The Mammalian Odz Gene Family: Homologs of a Drosophila Pair-Rule Gene with Expression Implying Distinct yet Overlapping Developmental Roles | doi = 10.1006/dbio.1999.9532 | journal = Developmental Biology | volume = 217 | issue = 1 | pages = 107–120 | year = 2000 | pmid = 10625539 | pmc = | doi-access = free }} *{{Cite journal | last1 = Strichman-Almashanu | first1 = L. Z. | last2 = Lee | first2 = R. S. | last3 = Onyango | first3 = P. O. | last4 = Perlman | first4 = E. | last5 = Flam | first5 = F. | last6 = Frieman | first6 = M. B. | last7 = Feinberg | first7 = A. P. | doi = 10.1101/gr.224102 | title = A Genome-Wide Screen for Normally Methylated Human CpG Islands That Can Identify Novel Imprinted Genes | journal = Genome Research | volume = 12 | issue = 4 | pages = 543–554 | year = 2002 | pmid = 11932239 | pmc =187522 }} *{{Cite journal | last1 = Hart | first1 = A. B. | last2 = Engelhardt | first2 = B. E. | last3 = Wardle | first3 = M. C. | last4 = Sokoloff | first4 = G. | last5 = Stephens | first5 = M. | last6 = De Wit | first6 = H. | last7 = Palmer | first7 = A. A. | editor1-last = Arking | editor1-first = Dan E | title = Genome-Wide Association Study of d-Amphetamine Response in Healthy Volunteers Identifies Putative Associations, Including Cadherin 13 (CDH13) | doi = 10.1371/journal.pone.0042646 | journal = PLOS ONE | volume = 7 | issue = 8 | article-number = e42646 | year = 2012 | pmid = 22952603 | pmc =3429486 | bibcode = 2012PLoSO...742646H | doi-access = free }} *{{Cite journal | last1 = Clark | first1 = A. G. | last2 = Glanowski | first2 = S. | last3 = Nielsen | first3 = R. | last4 = Thomas | first4 = P. D. | last5 = Kejariwal | first5 = A. | last6 = Todd | first6 = M. A. | last7 = Tanenbaum | first7 = D. M. | last8 = Civello | first8 = D. | last9 = Lu | first9 = F. | last10 = Murphy | first10 = B. | last11 = Ferriera | first11 = S. | last12 = Wang | first12 = G. | last13 = Zheng | first13 = X. | last14 = White | first14 = T. J. | last15 = Sninsky | first15 = J. J. | last16 = Adams | first16 = M. D. | last17 = Cargill | first17 = M. | title = Inferring Nonneutral Evolution from Human-Chimp-Mouse Orthologous Gene Trios | doi = 10.1126/science.1088821 | journal = Science | volume = 302 | issue = 5652 | pages = 1960–1963 | year = 2003 | pmid = 14671302 | pmc = | bibcode = 2003Sci...302.1960C | s2cid = 6682593 | url = https://semanticscholar.org/paper/2eb213b62c724a3a979ded7e8c53157335e1d094 }} *{{Cite journal | last1 = Aldahmesh | first1 = M. A. | last2 = Mohammed | first2 = J. Y. | last3 = Al-Hazzaa | first3 = S. | last4 = Alkuraya | first4 = F. S. | title = Homozygous null mutation in ODZ3 causes microphthalmia in humans | doi = 10.1038/gim.2012.71 | journal = Genetics in Medicine | volume = 14 | issue = 11 | pages = 900–904 | year = 2012 | pmid = 22766609 | pmc = | doi-access = free }} *{{Cite journal | last1 = Ben-Zur | first1 = T. | last2 = Wides | first2 = R. | doi = 10.1006/geno.1999.5798 | title = Mapping Homologs ofDrosophila odd Oz(odz):Doc4/Odz4to Mouse Chromosome 7,Odz1to Mouse Chromosome 11; and ODZ3 to Human Chromosome Xq25 | journal = Genomics | volume = 58 | issue = 1 | pages = 102–103 | year = 1999 | pmid = 10331952 | pmc = }}

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Category:Genes on human chromosome 4