Q9W7R4 · TEN3_DANRE
- ProteinTeneurin-3
- Genetenm3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2694 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Involved in neural development by regulating the establishment of proper connectivity within the nervous system (PubMed:24183672, PubMed:27374343).
Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion (By similarity).
Required by retinal ganglion cells for acquisition of their correct morphological and functional connectivity, thereby playing a key role in the development of the visual pathway (PubMed:24183672, PubMed:27374343).
Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion (By similarity).
Required by retinal ganglion cells for acquisition of their correct morphological and functional connectivity, thereby playing a key role in the development of the visual pathway (PubMed:24183672, PubMed:27374343).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | membrane | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Molecular Function | cell adhesion molecule binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | dendrite guidance | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | neuron development | |
Biological Process | positive regulation of neuron projection development | |
Biological Process | regulation of homophilic cell adhesion | |
Biological Process | retinal ganglion cell axon guidance | |
Biological Process | signal transduction | |
Biological Process | visual perception |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTeneurin-3
- Short namesTen-3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ9W7R4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-312 | Cytoplasmic | ||||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSGDSEDCRVPTQKSYSSSETLKAFDHDSSRLLYGGHVKEMVHREADEYSRQGQNFNLRQLGICEPATRRGLAFCAEMGMPSSLSSPSVTEHSHSQPPSPNLHDNQSSILSNATTQAVQDSDSEEEYTAVLYRPVTQPAPSHSCNEQPSNQHQQGQSTLPPVPPPHKQQPSVTALNHNSLSSRRNVSPAPPAALPAELQTTPESVPLQDSWVLGSNVPLESRHFLFKTGTGTTPLFSTATPGYTMATGAVYSPPTRPLPRNTLSRSAFKFKKSSKYCSWRCTALSAM | ||||||
Transmembrane | 313-333 | Helical | ||||
Sequence: AVSILLSVLLCYCIAMHLFGL | ||||||
Topological domain | 334-2694 | Extracellular | ||||
Sequence: NWQLQETEGYAFENGQVKSDSTATNAVTALSTENKVYFQENNTIDTGEVDVGRRAVQDVPPGTFWRTQLFIDQPQSLKFNISVQRGALVGVYGRKGLPPTHTQYDFVELLDGSRLIAKEKRGLVEVEGAARKARSVNVHEAEFIRFLDSGTWHLAFYNDGKNAEQVSYNTIIIDTLTECPHNCHGNGDCRTGTCHCFPGFLGPDCSRAACPVLCSGNGQYSRGRCLCYSGWKGTECDVPSNQCIDIHCSGHGICIMGTCACNTGYKGDNCEEVDCLDPSCSSHGVCIHGECHCNPGWGGNNCEILKTMCPDQCSGHGTYQTESGTCTCDTNWTGPDCSIEVCAVDCGSHGVCIGGSCRCEEGWTGSVCDLKACHPRCTEHGTCKDGKCECHQGWTGEHCTVEGCPGLCNSNGRCTLDQNGWHCVCQPGWRGAGCDVAMETLCADGKDNEGDGLVDCMDPDCCLQSSCQTQPFCRGSPDPIDIISQNQPASPQQAAQSFYQQISFLTGPESTHVINGENPFNRSLVSIIRGQVLTADGTPLIGVNVSFVHYPDHGYTITRQDGMFDILANGGASLTLSFERAPFLTQFRTVWIPWNVFYVMDTLVMKKEENDIPSCDLSGFIRPSPLIVATPLSTFFRSSPENGPIIPETQVLQEETAIPGSDLNLMYLSSRAAGYRPVLKVTMTQATIPFNLMKVHLMVAVVGRLFQKWFPAEPNLSYTFIWDKTDAYNQRVYGLSEAVVSVGFEYESCLDLILWEKRTAILQGYELDASNMGGWTLDKHHVLDVQNGILYKGNGENVFVSQQPPVISTIMGNGRRRSISCPSCNGQADGNKLLAPVALACGSDGSLFVGDFNYIRRIFPSGNVTSVMELSNNPAHRYYLATDPMTGQLYVSDTNSRRIFRPKALTGTKELLQNAEVVAGTGEQCLPFDEARCGDGGKATEALLLGPKGIAVDKNGFIYFVDGTMIRKVDRNGIISTLLGSNDLTSARPLTCDNSMHIGQVRLEWPTDLAINPMDNSIYVLDNNVVLQITENRQVRIVAGRPMHCQVPGIEYTMGKRAIQTTLEGATAISLSYSGVLYIAETDEKKINRIRQVSTDGEISHLAGAPSDCDCKNDANCDCYQTGDGYAKDARLNAPSSLVVSPDGTLYVADLGNIRIRAIRHNRPPQGSSGLFEVASPASQELYVFDSNGTHQYTMSLVTGDYKYNFSYSNEDDVTAVTDSSGNTLRVRRDPNRMPVRIVAPDNQVIWLTIGTNGGLKTLTAQGQELVLFTYHGNSGLLATKSIQIGWTTFYDYDSEGRLTNVTFPTGVITSLIGEMDRALTVDIETSGRDDDVSITTNLSSIDSFYTLVQDQLRNSYQVGYDNSMRVIYANGMDSHFQTEPHILAGASNPTVARRNMTLPGENGQNLVEWRFRKEQNRGKVVVFGRKLRVNGRNLLSVDYDRSLRTEKIYDDHRKFLLKIVYDASGHPTLWVPSSKLMSVNLTYSSTGQVTSLQRGPTTERVEYDSQGRIVSRTFADAKIWSYTYLDKSMVLLLHSQRQYIFDYDLQDRLSAITMPSVARHTMQTIRSVGYYRNIYNPPESNASVTVDYSEDGQLLRVAHLGTGRRVLYKYRRQNKLSEILYDSTRVSFTYDETAGVLKTVNLQSEGFICSIRYRQIGPLVDRQIFRFSEDGMVNARFDYTYDNSFRVTSMQGVINETPLPIDLYQFDDISGKVEQFGKFGVIYYDINQIISTAVMTYTKHFDVHGRIKEIQYEIFRSLMYWITIQYDNMGRVTKREIKIGPFANTTKYGYEYDVDGQLQTVYLNEKMMWRYNYDLNGNLHLLNPGNSARLTPLRYDLRDRITRLGDVQYRMDEDGFLRQRGAEIFEYNSKGLLVRVHSKASGWTIQYRYDGLGRRLASRNSLGQHLQFFYADLNYPTRITHVYNHSSSEITSLYYDLQGHLFAMEISSGEEFYIACDNTGTPLAVFSSNGLLLKQVQYTAYGEIYFDSNPDFQLVIGFHGGLYDPLTRLLHFGERDYDIQAGRWTTPDISTWTRVGKDPAPFNLYMFRNNNPISKIHEVKEYVTDVNIWLVTFGFHLHNVIPGFPIPKFDLTQPSLEMRKSQLWDDLPSISGVQQEVMRQAKAFLSFERMPEIQLSRRRSSREKPWLWFATVKSLIGKGVMLAITSKGQVATNALNIANEDCIKVATVLNNAFYLEDLHFTVEGRDTHYFIKTSLPESDLGALRLTSGRKSLENGVNVTVSQSTTVVNGRTRRFADVELQYGALALHVRYGMTLDEEKARVLEQARQRALSSAWAREQQRVRDGEEGVRLWTEGEKRQLLSSGKVLGYDGYYVLSVEQYPELADSANNVQFLRQSEIGKR |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Morpholino knockdown of the protein causes retinal ganglion cell dendrite stratification defects within the inner plexiform layer, as well as mistargeting of dendritic processes into outer portions of the retina.
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000259507 | 1-2694 | Teneurin-3 | |||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSGDSEDCRVPTQKSYSSSETLKAFDHDSSRLLYGGHVKEMVHREADEYSRQGQNFNLRQLGICEPATRRGLAFCAEMGMPSSLSSPSVTEHSHSQPPSPNLHDNQSSILSNATTQAVQDSDSEEEYTAVLYRPVTQPAPSHSCNEQPSNQHQQGQSTLPPVPPPHKQQPSVTALNHNSLSSRRNVSPAPPAALPAELQTTPESVPLQDSWVLGSNVPLESRHFLFKTGTGTTPLFSTATPGYTMATGAVYSPPTRPLPRNTLSRSAFKFKKSSKYCSWRCTALSAMAVSILLSVLLCYCIAMHLFGLNWQLQETEGYAFENGQVKSDSTATNAVTALSTENKVYFQENNTIDTGEVDVGRRAVQDVPPGTFWRTQLFIDQPQSLKFNISVQRGALVGVYGRKGLPPTHTQYDFVELLDGSRLIAKEKRGLVEVEGAARKARSVNVHEAEFIRFLDSGTWHLAFYNDGKNAEQVSYNTIIIDTLTECPHNCHGNGDCRTGTCHCFPGFLGPDCSRAACPVLCSGNGQYSRGRCLCYSGWKGTECDVPSNQCIDIHCSGHGICIMGTCACNTGYKGDNCEEVDCLDPSCSSHGVCIHGECHCNPGWGGNNCEILKTMCPDQCSGHGTYQTESGTCTCDTNWTGPDCSIEVCAVDCGSHGVCIGGSCRCEEGWTGSVCDLKACHPRCTEHGTCKDGKCECHQGWTGEHCTVEGCPGLCNSNGRCTLDQNGWHCVCQPGWRGAGCDVAMETLCADGKDNEGDGLVDCMDPDCCLQSSCQTQPFCRGSPDPIDIISQNQPASPQQAAQSFYQQISFLTGPESTHVINGENPFNRSLVSIIRGQVLTADGTPLIGVNVSFVHYPDHGYTITRQDGMFDILANGGASLTLSFERAPFLTQFRTVWIPWNVFYVMDTLVMKKEENDIPSCDLSGFIRPSPLIVATPLSTFFRSSPENGPIIPETQVLQEETAIPGSDLNLMYLSSRAAGYRPVLKVTMTQATIPFNLMKVHLMVAVVGRLFQKWFPAEPNLSYTFIWDKTDAYNQRVYGLSEAVVSVGFEYESCLDLILWEKRTAILQGYELDASNMGGWTLDKHHVLDVQNGILYKGNGENVFVSQQPPVISTIMGNGRRRSISCPSCNGQADGNKLLAPVALACGSDGSLFVGDFNYIRRIFPSGNVTSVMELSNNPAHRYYLATDPMTGQLYVSDTNSRRIFRPKALTGTKELLQNAEVVAGTGEQCLPFDEARCGDGGKATEALLLGPKGIAVDKNGFIYFVDGTMIRKVDRNGIISTLLGSNDLTSARPLTCDNSMHIGQVRLEWPTDLAINPMDNSIYVLDNNVVLQITENRQVRIVAGRPMHCQVPGIEYTMGKRAIQTTLEGATAISLSYSGVLYIAETDEKKINRIRQVSTDGEISHLAGAPSDCDCKNDANCDCYQTGDGYAKDARLNAPSSLVVSPDGTLYVADLGNIRIRAIRHNRPPQGSSGLFEVASPASQELYVFDSNGTHQYTMSLVTGDYKYNFSYSNEDDVTAVTDSSGNTLRVRRDPNRMPVRIVAPDNQVIWLTIGTNGGLKTLTAQGQELVLFTYHGNSGLLATKSIQIGWTTFYDYDSEGRLTNVTFPTGVITSLIGEMDRALTVDIETSGRDDDVSITTNLSSIDSFYTLVQDQLRNSYQVGYDNSMRVIYANGMDSHFQTEPHILAGASNPTVARRNMTLPGENGQNLVEWRFRKEQNRGKVVVFGRKLRVNGRNLLSVDYDRSLRTEKIYDDHRKFLLKIVYDASGHPTLWVPSSKLMSVNLTYSSTGQVTSLQRGPTTERVEYDSQGRIVSRTFADAKIWSYTYLDKSMVLLLHSQRQYIFDYDLQDRLSAITMPSVARHTMQTIRSVGYYRNIYNPPESNASVTVDYSEDGQLLRVAHLGTGRRVLYKYRRQNKLSEILYDSTRVSFTYDETAGVLKTVNLQSEGFICSIRYRQIGPLVDRQIFRFSEDGMVNARFDYTYDNSFRVTSMQGVINETPLPIDLYQFDDISGKVEQFGKFGVIYYDINQIISTAVMTYTKHFDVHGRIKEIQYEIFRSLMYWITIQYDNMGRVTKREIKIGPFANTTKYGYEYDVDGQLQTVYLNEKMMWRYNYDLNGNLHLLNPGNSARLTPLRYDLRDRITRLGDVQYRMDEDGFLRQRGAEIFEYNSKGLLVRVHSKASGWTIQYRYDGLGRRLASRNSLGQHLQFFYADLNYPTRITHVYNHSSSEITSLYYDLQGHLFAMEISSGEEFYIACDNTGTPLAVFSSNGLLLKQVQYTAYGEIYFDSNPDFQLVIGFHGGLYDPLTRLLHFGERDYDIQAGRWTTPDISTWTRVGKDPAPFNLYMFRNNNPISKIHEVKEYVTDVNIWLVTFGFHLHNVIPGFPIPKFDLTQPSLEMRKSQLWDDLPSISGVQQEVMRQAKAFLSFERMPEIQLSRRRSSREKPWLWFATVKSLIGKGVMLAITSKGQVATNALNIANEDCIKVATVLNNAFYLEDLHFTVEGRDTHYFIKTSLPESDLGALRLTSGRKSLENGVNVTVSQSTTVVNGRTRRFADVELQYGALALHVRYGMTLDEEKARVLEQARQRALSSAWAREQQRVRDGEEGVRLWTEGEKRQLLSSGKVLGYDGYYVLSVEQYPELADSANNVQFLRQSEIGKR | ||||||
Glycosylation | 374 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 413 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 512↔522 | |||||
Sequence: CPHNCHGNGDC | ||||||
Disulfide bond | 516↔527 | |||||
Sequence: CHGNGDCRTGTC | ||||||
Disulfide bond | 529↔538 | |||||
Sequence: CFPGFLGPDC | ||||||
Disulfide bond | 547↔558 | |||||
Sequence: CSGNGQYSRGRC | ||||||
Disulfide bond | 560↔569 | |||||
Sequence: CYSGWKGTEC | ||||||
Disulfide bond | 576↔587 | |||||
Sequence: CIDIHCSGHGIC | ||||||
Disulfide bond | 581↔592 | |||||
Sequence: CSGHGICIMGTC | ||||||
Disulfide bond | 594↔603 | |||||
Sequence: CNTGYKGDNC | ||||||
Disulfide bond | 608↔619 | |||||
Sequence: CLDPSCSSHGVC | ||||||
Disulfide bond | 613↔624 | |||||
Sequence: CSSHGVCIHGEC | ||||||
Disulfide bond | 626↔635 | |||||
Sequence: CNPGWGGNNC | ||||||
Disulfide bond | 646↔659 | |||||
Sequence: CSGHGTYQTESGTC | ||||||
Disulfide bond | 661↔670 | |||||
Sequence: CDTNWTGPDC | ||||||
Glycosylation | 664 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 675↔685 | |||||
Sequence: CAVDCGSHGVC | ||||||
Disulfide bond | 679↔690 | |||||
Sequence: CGSHGVCIGGSC | ||||||
Disulfide bond | 692↔701 | |||||
Sequence: CEEGWTGSVC | ||||||
Disulfide bond | 706↔716 | |||||
Sequence: CHPRCTEHGTC | ||||||
Disulfide bond | 710↔721 | |||||
Sequence: CTEHGTCKDGKC | ||||||
Disulfide bond | 723↔732 | |||||
Sequence: CHQGWTGEHC | ||||||
Disulfide bond | 737↔747 | |||||
Sequence: CPGLCNSNGRC | ||||||
Disulfide bond | 741↔756 | |||||
Sequence: CNSNGRCTLDQNGWHC | ||||||
Disulfide bond | 758↔767 | |||||
Sequence: CQPGWRGAGC | ||||||
Glycosylation | 854 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 877 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1048 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1196 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1521 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1538 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1634 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1671 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1729 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1814 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1915 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2571 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed by retinal ganglion cells and their presynaptic amacrine and postsynaptic tectal cell targets.
Developmental stage
Expressed at the notochord and the somite around tailbud stage. At 14 hours post-fertilization (hpf), expressed in the somites, notochord, and the brain. Found in the rhombomere 3 (r3) and r5. Expressed in the optic vesicles and a region covering the caudal diencephalon and the mesencephalon with the strongest expression at its most anterior part. Mesodermal expression is observed in both forming and formed somites. In forming and newly formed somites, transcripts are distributed evenly. In contrast, distribution in somites located on more anterior trunk seems to be uneven, strongest in the ventral, intermediate in the dorsal, and weakest in the medial parts. At 23 hpf, there is no expression in the medial parts of somites. Expression in somites fades away by 36 hpf. At 20 hpf, additional expression is detected in the pharyngeal arches.
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked; to mediate homophilic cell adhesion.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Basic and acidic residues | ||||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSG | ||||||
Region | 1-45 | Disordered | ||||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSGDSEDCRVPTQKSYSSSE | ||||||
Domain | 1-306 | Teneurin N-terminal | ||||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSGDSEDCRVPTQKSYSSSETLKAFDHDSSRLLYGGHVKEMVHREADEYSRQGQNFNLRQLGICEPATRRGLAFCAEMGMPSSLSSPSVTEHSHSQPPSPNLHDNQSSILSNATTQAVQDSDSEEEYTAVLYRPVTQPAPSHSCNEQPSNQHQQGQSTLPPVPPPHKQQPSVTALNHNSLSSRRNVSPAPPAALPAELQTTPESVPLQDSWVLGSNVPLESRHFLFKTGTGTTPLFSTATPGYTMATGAVYSPPTRPLPRNTLSRSAFKFKKSSKYCSWRC | ||||||
Compositional bias | 30-45 | Polar residues | ||||
Sequence: SEDCRVPTQKSYSSSE | ||||||
Region | 106-132 | Disordered | ||||
Sequence: PSSLSSPSVTEHSHSQPPSPNLHDNQS | ||||||
Region | 161-198 | Disordered | ||||
Sequence: TQPAPSHSCNEQPSNQHQQGQSTLPPVPPPHKQQPSVT | ||||||
Compositional bias | 163-182 | Polar residues | ||||
Sequence: PAPSHSCNEQPSNQHQQGQS | ||||||
Domain | 508-539 | EGF-like 1 | ||||
Sequence: TLTECPHNCHGNGDCRTGTCHCFPGFLGPDCS | ||||||
Domain | 540-570 | EGF-like 2 | ||||
Sequence: RAACPVLCSGNGQYSRGRCLCYSGWKGTECD | ||||||
Domain | 572-604 | EGF-like 3 | ||||
Sequence: PSNQCIDIHCSGHGICIMGTCACNTGYKGDNCE | ||||||
Domain | 605-636 | EGF-like 4 | ||||
Sequence: EVDCLDPSCSSHGVCIHGECHCNPGWGGNNCE | ||||||
Domain | 638-671 | EGF-like 5 | ||||
Sequence: LKTMCPDQCSGHGTYQTESGTCTCDTNWTGPDCS | ||||||
Domain | 672-703 | EGF-like 6 | ||||
Sequence: IEVCAVDCGSHGVCIGGSCRCEEGWTGSVCDL | ||||||
Domain | 704-733 | EGF-like 7 | ||||
Sequence: KACHPRCTEHGTCKDGKCECHQGWTGEHCT | ||||||
Domain | 734-768 | EGF-like 8 | ||||
Sequence: VEGCPGLCNSNGRCTLDQNGWHCVCQPGWRGAGCD | ||||||
Repeat | 1166-1192 | NHL 1 | ||||
Sequence: LLAPVALACGSDGSLFVGDFNYIRRIF | ||||||
Repeat | 1194-1238 | NHL 2 | ||||
Sequence: SGNVTSVMELSNNPAHRYYLATDPMTGQLYVSDTNSRRIFRPKAL | ||||||
Repeat | 1264-1308 | NHL 3 | ||||
Sequence: ARCGDGGKATEALLLGPKGIAVDKNGFIYFVDGTMIRKVDRNGII | ||||||
Repeat | 1325-1365 | NHL 4 | ||||
Sequence: CDNSMHIGQVRLEWPTDLAINPMDNSIYVLDNNVVLQITEN | ||||||
Repeat | 1452-1495 | NHL 5 | ||||
Sequence: CYQTGDGYAKDARLNAPSSLVVSPDGTLYVADLGNIRIRAIRHN | ||||||
Repeat | 1505-1524 | YD 1 | ||||
Sequence: FEVASPASQELYVFDSNGTH | ||||||
Repeat | 1541-1561 | YD 2 | ||||
Sequence: YSNEDDVTAVTDSSGNTLRVR | ||||||
Repeat | 1604-1623 | YD 3 | ||||
Sequence: YHGNSGLLATKSIQIGWTTF | ||||||
Repeat | 1624-1646 | YD 4 | ||||
Sequence: YDYDSEGRLTNVTFPTGVITSLI | ||||||
Repeat | 1817-1836 | YD 5 | ||||
Sequence: YSSTGQVTSLQRGPTTERVE | ||||||
Repeat | 1858-1876 | YD 6 | ||||
Sequence: YLDKSMVLLLHSQRQYIFD | ||||||
Repeat | 1877-1897 | YD 7 | ||||
Sequence: YDLQDRLSAITMPSVARHTMQ | ||||||
Repeat | 1904-1921 | YD 8 | ||||
Sequence: YYRNIYNPPESNASVTVD | ||||||
Repeat | 1922-1943 | YD 9 | ||||
Sequence: YSEDGQLLRVAHLGTGRRVLYK | ||||||
Repeat | 1944-1961 | YD 10 | ||||
Sequence: YRRQNKLSEILYDSTRVS | ||||||
Repeat | 1964-1984 | YD 11 | ||||
Sequence: YDETAGVLKTVNLQSEGFICS | ||||||
Repeat | 1987-2007 | YD 12 | ||||
Sequence: YRQIGPLVDRQIFRFSEDGMV | ||||||
Repeat | 2015-2034 | YD 13 | ||||
Sequence: YDNSFRVTSMQGVINETPLP | ||||||
Repeat | 2040-2057 | YD 14 | ||||
Sequence: FDDISGKVEQFGKFGVIY | ||||||
Repeat | 2058-2084 | YD 15 | ||||
Sequence: YDINQIISTAVMTYTKHFDVHGRIKEI | ||||||
Repeat | 2086-2099 | YD 16 | ||||
Sequence: YEIFRSLMYWITIQ | ||||||
Repeat | 2100-2123 | YD 17 | ||||
Sequence: YDNMGRVTKREIKIGPFANTTKYG | ||||||
Repeat | 2126-2146 | YD 18 | ||||
Sequence: YDVDGQLQTVYLNEKMMWRYN | ||||||
Repeat | 2147-2167 | YD 19 | ||||
Sequence: YDLNGNLHLLNPGNSARLTPL | ||||||
Repeat | 2169-2189 | YD 20 | ||||
Sequence: YDLRDRITRLGDVQYRMDEDG | ||||||
Repeat | 2201-2221 | YD 21 | ||||
Sequence: YNSKGLLVRVHSKASGWTIQY | ||||||
Repeat | 2223-2243 | YD 22 | ||||
Sequence: YDGLGRRLASRNSLGQHLQFF | ||||||
Repeat | 2269-2310 | YD 23 | ||||
Sequence: YDLQGHLFAMEISSGEEFYIACDNTGTPLAVFSSNGLLLKQV |
Sequence similarities
Belongs to the tenascin family. Teneurin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9W7R4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,694
- Mass (Da)300,669
- Last updated2018-04-25 v2
- Checksum65C41528CC4B4A10
Q9W7R4-2
- Name2
- Differences from canonical
- 1-104: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q0D280 | Q0D280_DANRE | tenm3 | 189 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Basic and acidic residues | ||||
Sequence: MDVKERRPYCSLTKSRREKERRYTGSSG | ||||||
Alternative sequence | VSP_059563 | 1-104 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 30-45 | Polar residues | ||||
Sequence: SEDCRVPTQKSYSSSE | ||||||
Compositional bias | 163-182 | Polar residues | ||||
Sequence: PAPSHSCNEQPSNQHQQGQS | ||||||
Sequence conflict | 781 | in Ref. 1; BAA81892 | ||||
Sequence: N → S | ||||||
Sequence conflict | 813 | in Ref. 1; BAA81892 | ||||
Sequence: I → F | ||||||
Sequence conflict | 892 | in Ref. 1; BAA81892 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 1210 | in Ref. 1; BAA81892 | ||||
Sequence: R → G | ||||||
Sequence conflict | 1880-1884 | in Ref. 1; BAA81892 | ||||
Sequence: QDRLS → HGKQI | ||||||
Sequence conflict | 2520 | in Ref. 1; BAA81892 | ||||
Sequence: A → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB026979 EMBL· GenBank· DDBJ | BAA81892.1 EMBL· GenBank· DDBJ | mRNA | ||
BX005481 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX322797 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX324137 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX324208 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |