TEN3_MOUSE
ID TEN3_MOUSE Reviewed; 2715 AA.
AC Q9WTS6; A0A2K9QKY6; A0A2K9QKZ0; A0A2K9QL01; A0A2K9QL03; A0A2K9QL04;
AC A0A2K9QL11; A0A2K9QL36; A0A2K9QL87; Q3UVR9; Q3UX72; Q80TD2; Q8BSL5; Q9CSV2;
AC Q9JLC1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 23-FEB-2022, entry version 134.
DE RecName: Full=Teneurin-3 {ECO:0000303|PubMed:29414938};
DE Short=Ten-3 {ECO:0000303|PubMed:29414938};
DE AltName: Full=Protein Odd Oz/ten-m homolog 3 {ECO:0000303|PubMed:10225957, ECO:0000303|PubMed:10625539};
DE AltName: Full=Tenascin-M3 {ECO:0000303|PubMed:23028443};
DE Short=Ten-m3 {ECO:0000303|PubMed:23028443};
DE AltName: Full=Teneurin transmembrane protein 3 {ECO:0000303|PubMed:23028443};
GN Name=Tenm3 {ECO:0000312|MGI:MGI:1345183};
GN Synonyms=Kiaa1455 {ECO:0000303|PubMed:12693553},
GN Odz3 {ECO:0000303|PubMed:10225957, ECO:0000303|PubMed:10625539},
GN Tnm3 {ECO:0000303|PubMed:23028443};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1B1), AND DOMAIN.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT "Mouse ten-m/Odz is a new family of dimeric type II transmembrane proteins
RT expressed in many tissues.";
RL J. Cell Biol. 145:563-577(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 354-2715 (ISOFORM A0B0).
RX PubMed=10625539; DOI=10.1006/dbio.1999.9532;
RA Ben-Zur T., Feige E., Motro B., Wides R.;
RT "The mammalian Odz gene family: homologs of a Drosophila pair-rule gene
RT with expression implying distinct yet overlapping developmental roles.";
RL Dev. Biol. 217:107-120(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 707-1248 (A0B0; A0B1; A1B0; A1B1; A2B0; A2B1;
RP A3B0 AND A3B1), FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29414938; DOI=10.1038/nature25463;
RA Berns D.S., DeNardo L.A., Pederick D.T., Luo L.;
RT "Teneurin-3 controls topographic circuit assembly in the hippocampus.";
RL Nature 554:328-333(2018).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 871-2715 (ISOFORM A0B0), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1640-2715 (ISOFORM A1B1).
RC STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-2715 (ISOFORM A1B1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP HOMODIMERIZATION, AND HETERODIMERIZATION.
RX PubMed=12000766; DOI=10.1074/jbc.m203722200;
RA Feng K., Zhou X.H., Oohashi T., Morgelin M., Lustig A., Hirakawa S.,
RA Ninomiya Y., Engel J., Rauch U., Fassler R.;
RT "All four members of the Ten-m/Odz family of transmembrane proteins form
RT dimers.";
RL J. Biol. Chem. 277:26128-26135(2002).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12915301; DOI=10.1016/s1567-133x(03)00087-5;
RA Zhou X.H., Brandau O., Feng K., Oohashi T., Ninomiya Y., Rauch U.,
RA Fassler R.;
RT "The murine Ten-m/Odz genes show distinct but overlapping expression
RT patterns during development and in adult brain.";
RL Gene Expr. Patterns 3:397-405(2003).
RN [8]
RP FUNCTION IN AXON GUIDANCE, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17803360; DOI=10.1371/journal.pbio.0050241;
RA Leamey C.A., Merlin S., Lattouf P., Sawatari A., Zhou X., Demel N.,
RA Glendining K.A., Oohashi T., Sur M., Fassler R.;
RT "Ten_m3 regulates eye-specific patterning in the mammalian visual pathway
RT and is required for binocular vision.";
RL PLoS Biol. 5:E241-E241(2007).
RN [9]
RP FUNCTION IN CELL ADHESION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17478416; DOI=10.1093/cercor/bhm031;
RA Leamey C.A., Glendining K.A., Kreiman G., Kang N.D., Wang K.H., Fassler R.,
RA Sawatari A., Tonegawa S., Sur M.;
RT "Differential gene expression between sensory neocortical areas: potential
RT roles for Ten_m3 and Bcl6 in patterning visual and somatosensory
RT pathways.";
RL Cereb. Cortex 18:53-66(2008).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380 AND ASN-2140.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION IN CELL DIFFERENTIATION, AND TISSUE SPECIFICITY.
RX PubMed=20636325; DOI=10.1111/j.1469-7580.2010.01267.x;
RA Murakami T., Fukunaga T., Takeshita N., Hiratsuka K., Abiko Y.,
RA Yamashiro T., Takano-Yamamoto T.;
RT "Expression of Ten-m/Odz3 in the fibrous layer of mandibular condylar
RT cartilage during postnatal growth in mice.";
RL J. Anat. 217:236-244(2010).
RN [13]
RP FUNCTION IN AXON GUIDANCE, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=23028443; DOI=10.1371/journal.pone.0043083;
RA Dharmaratne N., Glendining K.A., Young T.R., Tran H., Sawatari A.,
RA Leamey C.A.;
RT "Ten-m3 is required for the development of topography in the ipsilateral
RT retinocollicular pathway.";
RL PLoS ONE 7:E43083-E43083(2012).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22499796; DOI=10.1093/cercor/bhs030;
RA Merlin S., Horng S., Marotte L.R., Sur M., Sawatari A., Leamey C.A.;
RT "Deletion of Ten-m3 induces the formation of eye dominance domains in mouse
RT visual cortex.";
RL Cereb. Cortex 23:763-774(2013).
RN [15]
RP FUNCTION.
RX PubMed=25406022; DOI=10.1111/ejn.12767;
RA Tran H., Sawatari A., Leamey C.A.;
RT "The glycoprotein Ten-m3 mediates topography and patterning of
RT thalamostriatal projections from the parafascicular nucleus in mice.";
RL Eur. J. Neurosci. 41:55-68(2015).
CC -!- FUNCTION: Involved in neural development by regulating the
CC establishment of proper connectivity within the nervous system
CC (PubMed:17478416, PubMed:17803360, PubMed:23028443, PubMed:25406022,
CC PubMed:22499796, PubMed:29414938). Acts in both pre- and postsynaptic
CC neurons in the hippocampus to control the assembly of a precise
CC topographic projection: required in both CA1 and subicular neurons for
CC the precise targeting of proximal CA1 axons to distal subiculum,
CC probably by promoting homophilic cell adhesion (PubMed:29414938).
CC Promotes homophilic adhesion in a splicing isoform-dependent manner:
CC most isoforms (isoform-type A and type-B) can mediate homophilic
CC interaction (PubMed:29414938). Promotes axon guidance
CC (PubMed:23028443). Required for proper dendrite morphogenesis and axon
CC targeting in the vertebrate visual system, thereby playing a key role
CC in the development of the visual pathway (PubMed:17803360,
CC PubMed:23028443, PubMed:25406022, PubMed:22499796). Regulates the
CC formation in ipsilateral retinal mapping to both the dorsal lateral
CC geniculate nucleus (dLGN) and the superior colliculus (SC)
CC (PubMed:17803360, PubMed:23028443). May also be involved in the
CC differentiation of the fibroblast-like cells in the superficial layer
CC of mandibular condylar cartilage into chondrocytes (PubMed:20636325).
CC {ECO:0000269|PubMed:17478416, ECO:0000269|PubMed:17803360,
CC ECO:0000269|PubMed:20636325, ECO:0000269|PubMed:22499796,
CC ECO:0000269|PubMed:23028443, ECO:0000269|PubMed:25406022,
CC ECO:0000269|PubMed:29414938}.
CC -!- SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell
CC adhesion (PubMed:29414938, PubMed:12000766). Most isoforms (isoform-
CC type A and type-B) can mediate homophilic interaction
CC (PubMed:29414938). Heterodimer with either TENM1 or TENM2
CC (PubMed:12000766). May also form heterodimer with TENM4
CC (PubMed:12000766). Isoform A0B0: Does not form homodimer to mediate
CC homophilic cell adhesion. Isoform A0B0: Heterodimer with ADGRL3
CC (PubMed:29414938). {ECO:0000269|PubMed:12000766,
CC ECO:0000269|PubMed:29414938}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29414938,
CC ECO:0000305|PubMed:17478416}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17478416}. Cell projection, axon
CC {ECO:0000269|PubMed:17478416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=8 different isoforms are produced by the inclusion or
CC exclusion of 'exon 12' and 'exon 20' (at splice sites A and B,
CC respectively). The different isoforms probably mediate a combination
CC of specific homophilic and/or heterophilic interactions.
CC {ECO:0000269|PubMed:29414938};
CC Name=A1B1 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-1; Sequence=Displayed;
CC Name=A0B0 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-2; Sequence=VSP_021402, VSP_021403;
CC Name=A0B1 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-3; Sequence=VSP_021402;
CC Name=A1B0 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-4; Sequence=VSP_059562;
CC Name=A2B1 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-5; Sequence=VSP_059560;
CC Name=A2B0 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-6; Sequence=VSP_059560, VSP_059562;
CC Name=A3B1 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-7; Sequence=VSP_059561;
CC Name=A3B0 {ECO:0000303|PubMed:29414938};
CC IsoId=Q9WTS6-8; Sequence=VSP_059561, VSP_059562;
CC -!- TISSUE SPECIFICITY: In brain, expressed in highly specific regions of
CC the postnatal brain: expressed in restricted domains of the developing
CC hippocampal region, including proximal CA1, distal subiculum, and
CC medial entorhinal cortex (at protein level) (PubMed:29414938).
CC Expression matches with topographic connectivity between entorhinal
CC cortex, CA1, and subiculum (at protein level) (PubMed:29414938). Also
CC specifically expressed in subregions of the presubiculum,
CC parasubiculum, medial mammillary nucleus and anteroventral thalamic
CC nucleus that are topographically connected with subiculum or entorhinal
CC cortex (at protein level) (PubMed:29414938). Expressed in neurons of
CC the developing visual pathway (at protein level). Expressed in the
CC dorsal and ventral lateral geniculate nucleus (dLGN and vLGN) and optic
CC tract at birth. Expressed in ipsilateral retinal axons of terminal
CC zones (TZs) in the developing superior colliculus (SC) throughout the
CC first postnatal week. Expressed in the layer V of the visual caudal
CC cortex. Expressed in the femoral and mandibular condylar cartilages.
CC Strongly expressed in fibrous and proliferating chondrocytes. Poorly
CC expressed in mature chondrocytes. Not expressed in hypertrophic
CC chondrocytes (PubMed:12915301, PubMed:17478416, PubMed:17803360,
CC PubMed:20636325, PubMed:23028443). {ECO:0000269|PubMed:12915301,
CC ECO:0000269|PubMed:17478416, ECO:0000269|PubMed:17803360,
CC ECO:0000269|PubMed:20636325, ECO:0000269|PubMed:23028443,
CC ECO:0000269|PubMed:29414938}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the neural plate at 7.5 dpc.
CC Expressed in the forebrain and telencephalon at 8.5 dpc. Expressed in
CC the diencephalon, spinal cord and midbrain at 12.5 dpc. Expressed in
CC the retinal ganglion cell (RGC) layer and the dorsal lateral geniculate
CC nucleus (dLGN) at 16 dpc. Expressed in ipsilateral retinal axons of
CC terminal zones (TZs) in the developing superior colliculus (SC) at 16
CC dpc, onward. {ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:17803360,
CC ECO:0000269|PubMed:23028443}.
CC -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines
CC might enable the formation of intermolecular disulfide bonds.
CC {ECO:0000305|PubMed:10225957}.
CC -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains
CC for intracellular SH3-containing proteins.
CC {ECO:0000305|PubMed:10225957}.
CC -!- DISRUPTION PHENOTYPE: Mice show impair binocular vision, consistent
CC with altered ipsilateral retinal neuron projections both into the
CC ventrolateral region of the lateral geniculate nucleus (dLGN) and the
CC superior colliculus (SC) (PubMed:17803360, PubMed:23028443). The
CC distribution of ipsilateral drive in V1 is altered, leading to an
CC expanded but visuotopically misaligned binocular zone
CC (PubMed:22499796). Conditional knockout mice lacking Tenm3 in CA1
CC neurons display proximal CA1 axons spread throughout the entire
CC subiculum, instead of projecting only to distal regions
CC (PubMed:29414938). When Tenm3 is absent from a subset of distal
CC subicular cells, Tenm3-containing proximal CA1 axons do not target
CC Tenm3 and instead innervate nearby Tenm3 regions (PubMed:29414938).
CC {ECO:0000269|PubMed:17803360, ECO:0000269|PubMed:22499796,
CC ECO:0000269|PubMed:23028443, ECO:0000269|PubMed:29414938}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025412; BAA77398.1; -; mRNA.
DR EMBL; AF195418; AAF28316.1; -; mRNA.
DR EMBL; MG387139; AUQ44320.1; -; mRNA.
DR EMBL; MG387140; AUQ44321.1; -; mRNA.
DR EMBL; MG387141; AUQ44322.1; -; mRNA.
DR EMBL; MG387142; AUQ44323.1; -; mRNA.
DR EMBL; MG387143; AUQ44324.1; -; mRNA.
DR EMBL; MG387144; AUQ44325.1; -; mRNA.
DR EMBL; MG387145; AUQ44326.1; -; mRNA.
DR EMBL; MG387146; AUQ44327.1; -; mRNA.
DR EMBL; AK011924; BAB27919.1; -; mRNA.
DR EMBL; AK031268; BAC27329.1; -; mRNA.
DR EMBL; AK122513; BAC65795.1; -; mRNA.
DR EMBL; AK135844; BAE22691.1; ALT_INIT; mRNA.
DR EMBL; AK136994; BAE23200.1; -; mRNA.
DR CCDS; CCDS22303.1; -. [Q9WTS6-1]
DR CCDS; CCDS85538.1; -. [Q9WTS6-2]
DR PDB; 6FAY; EM; 3.80 A; A=845-2715.
DR PDBsum; 6FAY; -.
DR SMR; Q9WTS6; -.
DR IntAct; Q9WTS6; 1.
DR STRING; 10090.ENSMUSP00000140141; -.
DR GlyConnect; 2431; 3 N-Linked glycans (2 sites). [Q9WTS6-2]
DR GlyConnect; 2757; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9WTS6; 17 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9WTS6; -.
DR PhosphoSitePlus; Q9WTS6; -.
DR MaxQB; Q9WTS6; -.
DR PaxDb; Q9WTS6; -.
DR PRIDE; Q9WTS6; -.
DR ProteomicsDB; 258991; -. [Q9WTS6-1]
DR ProteomicsDB; 258992; -. [Q9WTS6-2]
DR MGI; MGI:1345183; Tenm3.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; Q9WTS6; -.
DR PhylomeDB; Q9WTS6; -.
DR ChiTaRS; Tenm3; mouse.
DR PRO; PR:Q9WTS6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WTS6; protein.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:1903385; P:regulation of homophilic cell adhesion; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR027691; Ten-3/4.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF65; PTHR11219:SF65; 1.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 2.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2715
FT /note="Teneurin-3"
FT /id="PRO_0000259506"
FT TOPO_DOM 1..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..2715
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..309
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 514..545
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 546..576
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 578..610
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 611..642
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 644..677
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 678..709
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 710..739
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 740..783
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1181..1209
FT /note="NHL 1"
FT REPEAT 1216..1260
FT /note="NHL 2"
FT REPEAT 1286..1330
FT /note="NHL 3"
FT REPEAT 1347..1387
FT /note="NHL 4"
FT REPEAT 1418..1445
FT /note="NHL 5"
FT REPEAT 1474..1517
FT /note="NHL 6"
FT REPEAT 1527..1546
FT /note="YD 1"
FT REPEAT 1563..1583
FT /note="YD 2"
FT REPEAT 1626..1645
FT /note="YD 3"
FT REPEAT 1646..1668
FT /note="YD 4"
FT REPEAT 1839..1858
FT /note="YD 5"
FT REPEAT 1880..1898
FT /note="YD 6"
FT REPEAT 1899..1919
FT /note="YD 7"
FT REPEAT 1926..1943
FT /note="YD 8"
FT REPEAT 1944..1965
FT /note="YD 9"
FT REPEAT 1966..1983
FT /note="YD 10"
FT REPEAT 1986..2006
FT /note="YD 11"
FT REPEAT 2009..2029
FT /note="YD 12"
FT REPEAT 2037..2056
FT /note="YD 13"
FT REPEAT 2062..2079
FT /note="YD 14"
FT REPEAT 2080..2106
FT /note="YD 15"
FT REPEAT 2108..2121
FT /note="YD 16"
FT REPEAT 2122..2145
FT /note="YD 17"
FT REPEAT 2148..2168
FT /note="YD 18"
FT REPEAT 2169..2189
FT /note="YD 19"
FT REPEAT 2191..2211
FT /note="YD 20"
FT REPEAT 2223..2243
FT /note="YD 21"
FT REPEAT 2245..2265
FT /note="YD 22"
FT REPEAT 2291..2332
FT /note="YD 23"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 2280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 518..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 522..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 535..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 553..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 566..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 587..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 619..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 632..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 652..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 667..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 681..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 685..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..707
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 712..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 716..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 729..738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 752..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 756..771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 773..782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 741..749
FT /note="Missing (in isoform A0B0 and isoform A0B1)"
FT /evidence="ECO:0000269|PubMed:29414938,
FT ECO:0000303|PubMed:10625539, ECO:0000303|PubMed:16141072"
FT /id="VSP_021402"
FT VAR_SEQ 749
FT /note="K -> KDKIGYK (in isoform A2B1 and isoform A2B0)"
FT /evidence="ECO:0000269|PubMed:29414938"
FT /id="VSP_059560"
FT VAR_SEQ 749
FT /note="K -> KADKIGYK (in isoform A3B1 and isoform A3B0)"
FT /evidence="ECO:0000269|PubMed:29414938"
FT /id="VSP_059561"
FT VAR_SEQ 1219..1226
FT /note="RNKDFRHS -> S (in isoform A1B0, isoform A2B0 and
FT isoform A3B0)"
FT /evidence="ECO:0000269|PubMed:29414938"
FT /id="VSP_059562"
FT VAR_SEQ 1219..1225
FT /note="Missing (in isoform A0B0)"
FT /evidence="ECO:0000303|PubMed:10625539,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021403"
FT CONFLICT 1632..1637
FT /note="LLATKS -> AFSHQK (in Ref. 4; BAE22691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1640
FT /note="T -> S (in Ref. 4; BAE23200)"
FT /evidence="ECO:0000305"
FT CONFLICT 2332
FT /note="T -> I (in Ref. 2; AAF28316 and 4; BAE23200/
FT BAC65795)"
FT /evidence="ECO:0000305"
FT CONFLICT 2482
FT /note="Missing (in Ref. 4; BAC27329)"
FT /evidence="ECO:0000305"
FT CONFLICT 2636
FT /note="I -> L (in Ref. 4; BAB27919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2715 AA; 303066 MW; 598F46A77334C2E1 CRC64;
MDVKERRPYC SLTKSRREKE RRYTNSSADN EECRVPTQKS YSSSETLKAF DHDYSRLLYG
NRVKDLVHRE ADEYTRQGQN FTLRQLGVCE SATRRGVAFC AEMGLPHRGY SISAGSDADT
ENEAVMSPEH AMRLWGRGVK SGRSSCLSSR SNSALTLTDT EHENRSDSES EQPSNNPGQP
TLQPLPPSHK QHPAQHHPSI TSLNRNSLTN RRNQSPAPPA ALPAELQTTP ESVQLQDSWV
LGSNVPLESR HFLFKTGTGT TPLFSTATPG YTMASGSVYS PPTRPLPRNT LSRSAFKFKK
SSKYCSWRCT ALCAVGVSVL LAILLSYFIA MHLFGLNWHL QQTENDTFEN GKVNSDTVPT
NTVSLPSGDN GKLGGFTHEN NTIDSGELDI GRRAIQEVPP GIFWRSQLFI DQPQFLKFNI
SLQKDALIGV YGRKGLPPSH TQYDFVELLD GSRLIAREQR NLVESERAGR QARSVSLHEA
GFIQYLDSGI WHLAFYNDGK NPEQVSFNTI VIESVVECPR NCHGNGECVS GTCHCFPGFL
GPDCSRAACP VLCSGNGQYS KGRCLCFSGW KGTECDVPTT QCIDPQCGGR GICIMGSCAC
NSGYKGENCE EADCLDPGCS NHGVCIHGEC HCNPGWGGSN CEILKTMCAD QCSGHGTYLQ
ESGSCTCDPN WTGPDCSNEI CSVDCGSHGV CMGGSCRCEE GWTGPACNQR ACHPRCAEHG
TCKDGKCECS QGWNGEHCTI AHYLDKIVKE GCPGLCNSNG RCTLDQNGWH CVCQPGWRGA
GCDVAMETLC TDSKDNEGDG LIDCMDPDCC LQSSCQNQPY CRGLPDPQDI ISQSLQTPSQ
QAAKSFYDRI SFLIGSDSTH VLPGESPFNK SLASVIRGQV LTADGTPLIG VNVSFLHYSE
YGYTITRQDG MFDLVANGGA SLTLVFERSP FLTQYHTVWI PWNVFYVMDT LVMKKEENDI
PSCDLSGFVR PSPIIVSSPL STFFRSSPED SPIIPETQVL HEETTIPGTD LKLSYLSSRA
AGYKSVLKIT MTQAVIPFNL MKVHLMVAVV GRLFQKWFPA SPNLAYTFIW DKTDAYNQKV
YGLSEAVVSV GYEYESCLDL TLWEKRTAVL QGYELDASNM GGWTLDKHHV LDVQNGILYK
GNGENQFISQ QPPVVSSIMG NGRRRSISCP SCNGQADGNK LLAPVALACG IDGSLYVGDF
NYVRRIFPSG NVTSVLELRN KDFRHSSNPA HRYYLATDPV TGDLYVSDTN TRRIYRPKSL
TGAKDLTKNA EVVAGTGEQC LPFDEARCGD GGKAVEATLM SPKGMAIDKN GLIYFVDGTM
IRKVDQNGII STLLGSNDLT SARPLTCDTS MHISQVRLEW PTDLAINPMD NSIYVLDNNV
VLQITENRQV RIAAGRPMHC QVPGVEYPVG KHAVQTTLES ATAIAVSYSG VLYITETDEK
KINRIRQVTT DGEISLVAGI PSECDCKNDA NCDCYQSGDG YAKDAKLNAP SSLAASPDGT
LYIADLGNIR IRAVSKNKPL LNSMNFYEVA SPTDQELYIF DINGTHQYTV SLVTGDYLYN
FSYSNDNDVT AVTDSNGNTL RIRRDPNRMP VRVVSPDNQV IWLTIGTNGC LKSMTAQGLE
LVLFTYHGNS GLLATKSDET GWTTFFDYDS EGRLTNVTFP TGVVTNLHGD MDKAITVDIE
SSSREEDVSI TSNLSSIDSF YTMVQDQLRN SYQIGYDGSL RIFYASGLDS HYQTEPHVLA
GTANPTVAKR NMTLPGENGQ NLVEWRFRKE QAQGKVNVFG RKLRVNGRNL LSVDFDRTTK
TEKIYDDHRK FLLRIAYDTS GHPTLWLPSS KLMAVNVTYS STGQIASIQR GTTSEKVDYD
SQGRIVSRVF ADGKTWSYTY LEKSMVLLLH SQRQYIFEYD MWDRLSAITM PSVARHTMQT
IRSIGYYRNI YNPPESNASI ITDYNEEGLL LQTAFLGTSR RVLFKYRRQT RLSEILYDST
RVSFTYDETA GVLKTVNLQS DGFICTIRYR QIGPLIDRQI FRFSEDGMVN ARFDYSYDNS
FRVTSMQGVI NETPLPIDLY QFDDISGKVE QFGKFGVIYY DINQIISTAV MTYTKHFDAH
GRIKEIQYEI FRSLMYWITI QYDNMGRVTK REIKIGPFAN TTKYAYEYDV DGQLQTVYLN
EKIMWRYNYD LNGNLHLLNP SSSARLTPLR YDLRDRITRL GDVQYRLDED GFLRQRGTEI
FEYSSKGLLT RVYSKGSGWT VIYRYDGLGR RVSSKTSLGQ HLQFFYADLT YPTRITHVYN
HSSSEITSLY YDLQGHLFAM EISSGDEFYI ASDNTGTPLA VFSSNGLMLK QTQYTAYGEI
YFDSNVDFQL VIGFHGGLYD PLTKLIHFGE RDYDILAGRW TTPDIEIWKR IGKDPAPFNL
YMFRNNNPAS KIHDVKDYIT DVNSWLVTFG FHLHNAIPGF PVPKFDLTEP SYELVKSQQW
EDVPPIFGVQ QQVARQAKAF LSLGKMAEVQ VSRRKAGAEQ SWLWFATVKS LIGKGVMLAV
SQGRVQTNVL NIANEDCIKV AAVLNNAFYL ENLHFTIEGK DTHYFIKTTT PESDLGTLRL
TSGRKALENG INVTVSQSTT VVNGRTRRFA DVEMQFGALA LHVRYGMTLD EEKARILEQA
RQRALARAWA REQQRVRDGE EGARLWTEGE KRQLLSAGKV QGYDGYYVLS VEQYPELADS
ANNIQFLRQS EIGKR
