Detail Information for IndEnz0002013674
IED ID IndEnz0002013674
Enzyme Type ID protease013674
Protein Name Teneurin-1
Ten-1
Protein Odd Oz/ten-m homolog 1
Tenascin-M1
Ten-m1
Teneurin transmembrane protein 1

Cleaved into: Ten-1 intracellular domain
IDten-1
Ten-1 ICD
; Teneurin C-terminal-associated peptide
TCPA-1
Ten-1 extracellular domain
Ten-1 ECD
Gene Name Tenm1 Odz1 Tnm1
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MEQTDCKPYQPLSKVKHEMDLAYTSSSDESEDGRKPRQSFNSRETLHEYNQELRRNYNSQSRKRKDVEKSTQEIEFCETPPTLCSGYHTDMHSVSRHGYQLEMGSDVDTETEGAASPDHALRMWIRGMKSEHSSCLSSRANSALSLTDTDHERKSDGENGFKFSPVCCDMEAPADSAQDMQSSPHNQFTFRPLPPPPPPPHACTCARKPPPTVDSLQRRSMTTRSQPSPAAPAPPTSTQDSVHLHNSWVLNSNIPLETRHFLFKHGSGSSAIFSAASQNYPLTSNTVYSPPPRPLPRSTFSRPAFTFNKPYRCCNWKCTALSATAITVTLALLLAYVIAVHLFGLTWQLQPVGQIYANGISNGNPGTESMDTTYSPIGGRVSDKSEKKVFQKGRAIDTGEVDIGAQVMQTIPPGLFWRFQITIHHPIYLKFNISLAKDSLLGIYGRRNIPPTHTQFDFVKLMDGKQLVKQDSKSSDDIQHSPRNLILTSLQETGFIEYMDQGPWYLAFYNDGKKMEQVFVLTTAIEIMDDCSTNCNGNGECISGHCHCFPGFLGPDCARDSCPVLCGGNGEYEKGHCVCRNGWKGPECDVPEEQCIDPTCFGHGTCIMGVCICVPGYKGEICEEEDCLDPMCSSHGICVKGECHCSTGWGGVNCETPLPICQEQCSGHGTFLLDTGVCSCDPKWTGSDCSTELCTMECGSHGVCSRGICQCEEGWVGPTCEERSCHSHCAEHGQCKDGKCECSPGWEGDHCTIAHYLDAVRDGCPGLCFGNGRCTLDQNGWHCVCQVGWSGTGCNIVMEMLCGDNLDNDGDGLTDCVDPDCCQQSNCYVSPLCQGSPDPLDLIQQSQPLFSQHTSRLFYDRIKFLIGKDSTHVVPQDISFDSRRACVIRGQVVAVDGTPLVGVNVSFLHHSDYGFTISRQDGSFDLVAIGGISVVLIFDRSPFLSEKRTLWLPWNQFIVVEKVIMQRIVADAPSCDISNFISPNPIVLPSPLTSFGGSCPERGTIVPELQVVQEEIPIPSSFVRLSYLSSRTPGYKTLLRILLTHSTIPVGMIKVHLTVSVEGRLTQKWFPAAINLVYTFAWNKTDIYGQKVWGLAEALVSVGYEYEMCPEFILWEQRTVVLQGFEMDASNLGGWSLNKHHIFNPQSGIIHKGNGENMFISQQPPVIATIMGNGHQRSVACTNCNGPAHNNKLFAPVALASGPDGSVYVGDFNFVRRIFPSGNSVSILELRNRDTRHSTSPAHKYYLAMDPMSESLYLSDTNTRKVYKLKSLVETKDLSKNFEVVAGTGDQCLPFDQSHCGDGGKASEASLNSPRGITVDRHGFIYFVDGTMIRRIDENAVITTVIGSNGLTSTQPLSCDSGMDITQVRLEWPTDLAVNPMDNSLYVLDNNIVLQISENRRVRIIAGRPIHCQVPGIDHFLVSKVAIHSTLESARAISVSHSGLLFIAETDERKVNRIQQVTTNGEISIIAGAPTDCDCKIDPNCDCFSGDGGYAKDAKMKAPSSLAVSPDGTLYVADLGNVRIRTISKNQAHLNDMNLYEIASPADQELYQFTVNGTHLHTMNLITRDYVYNFTYNAEGDLGAITSSNGNSVHIRRDAGGMPLWLVVPGGQVYWLTISSNGVLKRVSAQGYNLALMTYPGNTGLLATKSNENGWTTVYEYDPEGHLTNATFPTGEVSSFHSDLEKLTKVALDTSNRENVLMSTNLTATSTIYILKQENTQSTYRVSPDGSLRVTFASGMEINLSSEPHILAGAVNPTLGKCNISLPGEHNANLIEWRQRKEQNKGNVSAFERRLRAHNRNLLSIDFDHMTRTGKIYDDHRKFTLRILYDQTGRPILWSPVSRYNEVNITYSPSGLVTFIQRGTWNEKMEYDQSGKIISRTWADGKIWSYTYLEKSVMLLLHSQRRYIFEYDQSDCLLSVTMPSMVRHSLQTMLSVGYYRNIYTPPDSSTSFIQDYSRDGRLLQTLHLGTGRRVLYKYTKQARLSEILYDTTQVTLTYEESSGVIKTIHLMHDGFICTIRYRQTGPLIGRQIFRFSEEGLVNARFDYSYNNFRVTSMQAVINETPLPIDLYRYVDVSGRTEQFGKFSVINYDLNQVITTTVMKHTKIFNANGQVIEVQYEILKAIAYWMTIQYDNMGRMVICDIRVGVDANITRYFYEYDADGQLQTVSVNDKIQWRYSYDLNGNINLLSHGNSARLTPLRYDLRDRITRLGEIQYKMDEDGFLRQRGNDIFEYNSNGLLQKAYNKVSGWTVQYYYDGLGRRVASKSSLGQHLQFFYADLANPIRVTHLYNHTSAEITSLYYDLQGHLIAMELSSGEEYYVACDNMGTPLAVFSSRGQVIKEILYTPYGDIYHDTYPDFEVIIGFHGGLYDFLTKLVHLGQRDYDVVAGRWTTPNHHIWKQLNLLPKPFNLYSFENNYPVGKIQDVAKYTTDIGTWLELFGFQLHNVLPGFPKPELENMELTYELLQLQTKTQEWDPGKMILGIQCELQKQLRNFISLDQLPMTPQYNEGRCLEGGKQPRFAAVPSVFGKGIKFAIKEGIVTADIIGVANEDSRRLAAILNNAHYLENLHFTIEGRDTHYFIKLGSLEEDLVLIGNTGGRRILENGVNVTVSQMTSVLNGRTRRFADIQLQHGALCFNIRYGTTVEEEKNHVLEMARQRAVAQAWTQEQRRLQEGEEGTRVWTEGEKQQLLGTGRVQGYDGYFVLSVEQYLELSDSANNIHFMRQSEIGRR
Enzyme Length 2731
Uniprot Accession Number Q9WTS4
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; FUNCTION: [Teneurin C-terminal-associated peptide]: Plays a role in the regulation of neuroplasticity in the limbic system. Mediates a rapid reorganization of actin- and tubulin-based cytoskeleton elements with an increase in dendritic arborization and spine density formation of neurons in the hippocampus and amygdala. Induces BDNF transcription inhibition in neurons. Activates the mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade. Acts also as a bioactive neuroprotective peptide on limbic neurons of the brain and regulates stress-induced behavior: attenuates alkalosis-associated necrotic cell death and the effects of corticotropin-releasing factor (CRF) on c-fos/FOS induction and on the reinstatement of cocaine seeking. {ECO:0000269|PubMed:15710242, ECO:0000269|PubMed:17174479, ECO:0000269|PubMed:17644218, ECO:0000269|PubMed:17900539, ECO:0000269|PubMed:18082275, ECO:0000269|PubMed:19428634, ECO:0000269|PubMed:20883474, ECO:0000269|PubMed:21411044, ECO:0000269|PubMed:22209827, ECO:0000269|PubMed:22698694}.; FUNCTION: [Ten-1 intracellular domain]: Induces gene transcription activation. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (3); Compositional bias (2); Disulfide bond (22); Domain (9); Glycosylation (14); Modified residue (4); Motif (2); Region (2); Repeat (28); Site (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell membrane;Cleavage on pair of basic residues;Cytoplasm;Cytoskeleton;Disulfide bond;EGF-like domain;Glycoprotein;Membrane;Neuropeptide;Nucleus;Phosphoprotein;Reference proteome;Repeat;Repressor;Secreted;Stress response;Transcription;Transcription regulation;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23026563}; Single-pass membrane protein {ECO:0000269|PubMed:23026563}. Note=Colocalizes with isoform 2 at the plasma membrane.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Cell membrane. Secreted {ECO:0000305}. Note=Transported to the cell membrane and probably secreted to function as an autocrine or paracrine signaling molecule. The lack of a hydrophobic segment sequence suggests that isoform 2 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.; SUBCELLULAR LOCATION: [Ten-1 intracellular domain]: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.; SUBCELLULAR LOCATION: [Teneurin C-terminal-associated peptide]: Nucleus {ECO:0000305}. Cytoplasm. Cell membrane. Note=Colocalizes with isoform 1 at the plasma membrane. Colocalizes with the dystroglycan complex at the cell membrane in hippocampal cells. Binds hippocampal cell membranes and is incorporated in the cytoplasm by endocytosis in a caveoli-dependent manner. Upon cell internalization is transported arround and in the nucleus.
Modified Residue MOD_RES 105; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 109; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 116; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2586; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKZ4
Post Translational Modification PTM: [Isoform 2]: Once secreted, may also be cleaved to give rise to the TCAP-1 form. {ECO:0000269|PubMed:23026563}.; PTM: [Teneurin C-terminal-associated peptide]: Derives from the plasma membrane form by proteolytic processing. Further proteolytic cleavage may generate 11.9 and 4.7 kDa bioactive peptides. {ECO:0000269|PubMed:23026563}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10341219; 12466851; 14681479; 16919471; 21651764; 21677750; 27040985; 27720483; 27798109; 28558017;
Motif MOTIF 62..65; /note=Nuclear localization signal (NLS); /evidence=ECO:0000250; MOTIF 290..297; /note=Required for interaction with SORBS1 (Ten-1 ICD form); /evidence=ECO:0000250
Gene Encoded By
Mass 305,795
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda