TEN1_MOUSE
ID TEN1_MOUSE Reviewed; 2731 AA.
AC Q9WTS4; Q8CAT1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Teneurin-1;
DE Short=Ten-1;
DE AltName: Full=Protein Odd Oz/ten-m homolog 1;
DE AltName: Full=Tenascin-M1;
DE Short=Ten-m1;
DE AltName: Full=Teneurin transmembrane protein 1;
DE Contains:
DE RecName: Full=Ten-1 intracellular domain;
DE Short=IDten-1;
DE Short=Ten-1 ICD;
DE Contains:
DE RecName: Full=Teneurin C-terminal-associated peptide;
DE Short=TCPA-1;
DE AltName: Full=Ten-1 extracellular domain;
DE Short=Ten-1 ECD;
GN Name=Tenm1; Synonyms=Odz1, Tnm1;
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], SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
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 [4]
RP TISSUE SPECIFICITY.
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 [5]
RP FUNCTION OF ISOFORM 2 IN CELL PROLIFERATION, AND TISSUE SPECIFICITY.
RX PubMed=15710242; DOI=10.1016/j.molbrainres.2004.10.019;
RA Wang L., Rotzinger S., Al Chawaf A., Elias C.F., Barsyte-Lovejoy D.,
RA Qian X., Wang N.C., De Cristofaro A., Belsham D., Bittencourt J.C.,
RA Vaccarino F., Lovejoy D.A.;
RT "Teneurin proteins possess a carboxy terminal sequence with neuromodulatory
RT activity.";
RL Brain Res. Mol. Brain Res. 133:253-265(2005).
RN [6]
RP INTERACTION WITH MBD1 AND SORBS1.
RX PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
RA Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
RA Chiquet-Ehrismann R.;
RT "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin
RT resulting in subcellular codistribution and translocation to the nuclear
RT matrix.";
RL Exp. Cell Res. 305:122-132(2005).
RN [7]
RP FUNCTION OF ISOFORM 2 IN CELL SURVIVAL.
RX PubMed=17900539; DOI=10.1016/j.brainres.2007.07.087;
RA Trubiani G., Al Chawaf A., Belsham D.D., Barsyte-Lovejoy D., Lovejoy D.A.;
RT "Teneurin carboxy (C)-terminal associated peptide-1 inhibits alkalosis-
RT associated necrotic neuronal death by stimulating superoxide dismutase and
RT catalase activity in immortalized mouse hypothalamic cells.";
RL Brain Res. 1176:27-36(2007).
RN [8]
RP FUNCTION OF ISOFORM 2 IN AXON GROWTH.
RX PubMed=17174479; DOI=10.1016/j.neuroscience.2006.09.062;
RA Al Chawaf A., St Amant K., Belsham D., Lovejoy D.A.;
RT "Regulation of neurite growth in immortalized mouse hypothalamic neurons
RT and rat hippocampal primary cultures by teneurin C-terminal-associated
RT peptide-1.";
RL Neuroscience 144:1241-1254(2007).
RN [9]
RP FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
RX PubMed=17644218; DOI=10.1016/j.peptides.2007.05.014;
RA Al Chawaf A., Xu K., Tan L., Vaccarino F.J., Lovejoy D.A., Rotzinger S.;
RT "Corticotropin-releasing factor (CRF)-induced behaviors are modulated by
RT intravenous administration of teneurin C-terminal associated peptide-1
RT (TCAP-1).";
RL Peptides 28:1406-1415(2007).
RN [10]
RP FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
RX PubMed=18082275; DOI=10.1016/j.bbr.2007.10.032;
RA Tan L.A., Xu K., Vaccarino F.J., Lovejoy D.A., Rotzinger S.;
RT "Repeated intracerebral teneurin C-terminal associated peptide (TCAP)-1
RT injections produce enduring changes in behavioral responses to
RT corticotropin-releasing factor (CRF) in rat models of anxiety.";
RL Behav. Brain Res. 188:195-200(2008).
RN [11]
RP FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
RX PubMed=19428634; DOI=10.1016/j.bbr.2009.02.013;
RA Tan L.A., Xu K., Vaccarino F.J., Lovejoy D.A., Rotzinger S.;
RT "Teneurin C-terminal associated peptide (TCAP)-1 attenuates corticotropin-
RT releasing factor (CRF)-induced c-Fos expression in the limbic system and
RT modulates anxiety behavior in male Wistar rats.";
RL Behav. Brain Res. 201:198-206(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-109 AND SER-116, AND
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 [13]
RP FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
RX PubMed=20883474; DOI=10.1111/j.1476-5381.2010.01055.x;
RA Kupferschmidt D.A., Lovejoy D.A., Rotzinger S., Erb S.;
RT "Teneurin C-terminal associated peptide-1 blocks the effects of
RT corticotropin-releasing factor on reinstatement of cocaine seeking and on
RT cocaine-induced behavioural sensitization.";
RL Br. J. Pharmacol. 162:574-583(2011).
RN [14]
RP FUNCTION OF ISOFORM 2 IN AXON MORPHOLOGY.
RX PubMed=21411044; DOI=10.1016/j.physbeh.2011.03.015;
RA Tan L.A., Al Chawaf A., Vaccarino F.J., Boutros P.C., Lovejoy D.A.;
RT "Teneurin C-terminal associated peptide (TCAP)-1 modulates dendritic
RT morphology in hippocampal neurons and decreases anxiety-like behaviors in
RT rats.";
RL Physiol. Behav. 104:199-204(2011).
RN [15]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23026563; DOI=10.1016/j.mcn.2012.09.006;
RA Chand D., Casatti C.A., de Lannoy L., Song L., Kollara A.,
RA Barsyte-Lovejoy D., Brown T.J., Lovejoy D.A.;
RT "C-terminal processing of the teneurin proteins: Independent actions of a
RT teneurin C-terminal associated peptide in hippocampal cells.";
RL Mol. Cell. Neurosci. 52:38-50(2013).
RN [16]
RP FUNCTION OF ISOFORM 2 IN REORGANIZATION OF CYTOSKELETON, AND SUBCELLULAR
RP LOCATION (ISOFORM 2).
RX PubMed=22698694; DOI=10.1016/j.neuroscience.2012.05.069;
RA Chand D., Song L., deLannoy L., Barsyte-Lovejoy D., Ackloo S.,
RA Boutros P.C., Evans K., Belsham D.D., Lovejoy D.A.;
RT "C-Terminal region of teneurin-1 co-localizes with dystroglycan and
RT modulates cytoskeletal organization through an extracellular signal-
RT regulated kinase-dependent stathmin- and filamin A-mediated mechanism in
RT hippocampal cells.";
RL Neuroscience 219:255-270(2012).
RN [17]
RP FUNCTION OF ISOFORM 2 IN BDNF INHIBITION, AND SUBCELLULAR LOCATION (ISOFORM
RP 2).
RX PubMed=22209827; DOI=10.1016/j.regpep.2011.12.003;
RA Ng T., Chand D., Song L., Al Chawaf A., Watson J.D., Boutros P.C.,
RA Belsham D.D., Lovejoy D.A.;
RT "Identification of a novel brain derived neurotrophic factor (BDNF)-
RT inhibitory factor: regulation of BDNF by teneurin C-terminal associated
RT peptide (TCAP)-1 in immortalized embryonic mouse hypothalamic cells.";
RL Regul. Pept. 174:79-89(2012).
RN [18]
RP INTERACTION WITH HINT1.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. May function as a
CC cellular signal transducer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Teneurin C-terminal-associated peptide]: Plays a role in the
CC regulation of neuroplasticity in the limbic system. Mediates a rapid
CC reorganization of actin- and tubulin-based cytoskeleton elements with
CC an increase in dendritic arborization and spine density formation of
CC neurons in the hippocampus and amygdala. Induces BDNF transcription
CC inhibition in neurons. Activates the mitogen-activated protein (MAP)
CC kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK)
CC cascade. Acts also as a bioactive neuroprotective peptide on limbic
CC neurons of the brain and regulates stress-induced behavior: attenuates
CC alkalosis-associated necrotic cell death and the effects of
CC corticotropin-releasing factor (CRF) on c-fos/FOS induction and on the
CC reinstatement of cocaine seeking. {ECO:0000269|PubMed:15710242,
CC ECO:0000269|PubMed:17174479, ECO:0000269|PubMed:17644218,
CC ECO:0000269|PubMed:17900539, ECO:0000269|PubMed:18082275,
CC ECO:0000269|PubMed:19428634, ECO:0000269|PubMed:20883474,
CC ECO:0000269|PubMed:21411044, ECO:0000269|PubMed:22209827,
CC ECO:0000269|PubMed:22698694}.
CC -!- FUNCTION: [Ten-1 intracellular domain]: Induces gene transcription
CC activation. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either TENM2 or
CC TENM3. May also form heterodimer with TENM4. Ten-1 ICD interacts with
CC SORBS1 (via third SH3 domain). Interacts with MBD1 isoform 2
CC (PubMed:15777793). Ten-1 ICD interacts with HINT1 (PubMed:31088288).
CC {ECO:0000269|PubMed:10225957, ECO:0000269|PubMed:15777793,
CC ECO:0000269|PubMed:31088288}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:23026563}; Single-pass membrane protein
CC {ECO:0000269|PubMed:23026563}. Note=Colocalizes with isoform 2 at the
CC plasma membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Cell membrane. Secreted
CC {ECO:0000305}. Note=Transported to the cell membrane and probably
CC secreted to function as an autocrine or paracrine signaling molecule.
CC The lack of a hydrophobic segment sequence suggests that isoform 2 is
CC released by damaged cells or is secreted by a mechanism differing from
CC that used for other secretory proteins.
CC -!- SUBCELLULAR LOCATION: [Ten-1 intracellular domain]: Nucleus
CC {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Teneurin C-terminal-associated peptide]: Nucleus
CC {ECO:0000305}. Cytoplasm. Cell membrane. Note=Colocalizes with isoform
CC 1 at the plasma membrane. Colocalizes with the dystroglycan complex at
CC the cell membrane in hippocampal cells. Binds hippocampal cell
CC membranes and is incorporated in the cytoplasm by endocytosis in a
CC caveoli-dependent manner. Upon cell internalization is transported
CC arround and in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WTS4-1; Sequence=Displayed;
CC Name=2; Synonyms=TCAP-1;
CC IsoId=Q9WTS4-2; Sequence=VSP_045018;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the brain.
CC Isoform 2 is expressed in the granular layer of the dentate gyrus and
CC the pyramidal layer (Py) of the CA1, CA2 and CA3 of the hippocampus (at
CC protein level). Expressed in the cortex, thalamus, CA1, CA2, CA3,
CC dentate gyrus and granular layer of the hippocampus. Weakly expressed
CC in kidney, testis and lung. {ECO:0000269|PubMed:10225957,
CC ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:15710242,
CC ECO:0000269|PubMed:23026563}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 and isoform 2 are expressed in
CC hippocampal cells at 14 dpc (at protein level).
CC {ECO:0000269|PubMed:23026563}.
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 -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains
CC for intracellular SH3-containing proteins.
CC -!- PTM: [Isoform 2]: Once secreted, may also be cleaved to give rise to
CC the TCAP-1 form. {ECO:0000269|PubMed:23026563}.
CC -!- PTM: [Teneurin C-terminal-associated peptide]: Derives from the plasma
CC membrane form by proteolytic processing. Further proteolytic cleavage
CC may generate 11.9 and 4.7 kDa bioactive peptides.
CC {ECO:0000269|PubMed:23026563}.
CC -!- MISCELLANEOUS: [Teneurin C-terminal-associated peptide]: Binds to the
CC plasma membrane and may be internalized by a receptor- and caveolae-
CC mediated endocytosis manner to reach cytosolic compartments in a
CC dynamin-dependent manner. {ECO:0000305|PubMed:23026563}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AB025410; BAA77396.1; -; mRNA.
DR EMBL; AK037897; BAC29893.1; -; mRNA.
DR CCDS; CCDS40953.1; -. [Q9WTS4-1]
DR RefSeq; NP_035985.2; NM_011855.4. [Q9WTS4-1]
DR RefSeq; XP_011249307.1; XM_011251005.2. [Q9WTS4-1]
DR RefSeq; XP_011249308.1; XM_011251006.2. [Q9WTS4-1]
DR RefSeq; XP_011249309.1; XM_011251007.2. [Q9WTS4-1]
DR RefSeq; XP_017173972.1; XM_017318483.1. [Q9WTS4-1]
DR RefSeq; XP_017173973.1; XM_017318484.1. [Q9WTS4-1]
DR SMR; Q9WTS4; -.
DR BioGRID; 204824; 3.
DR IntAct; Q9WTS4; 1.
DR MINT; Q9WTS4; -.
DR STRING; 10090.ENSMUSP00000110711; -.
DR GlyConnect; 2755; 3 N-Linked glycans (3 sites).
DR GlyGen; Q9WTS4; 14 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q9WTS4; -.
DR PhosphoSitePlus; Q9WTS4; -.
DR CPTAC; non-CPTAC-4065; -.
DR MaxQB; Q9WTS4; -.
DR PaxDb; Q9WTS4; -.
DR PRIDE; Q9WTS4; -.
DR ProteomicsDB; 262867; -. [Q9WTS4-1]
DR ProteomicsDB; 262868; -. [Q9WTS4-2]
DR Antibodypedia; 482; 115 antibodies from 25 providers.
DR DNASU; 23963; -.
DR Ensembl; ENSMUST00000016294; ENSMUSP00000016294; ENSMUSG00000016150. [Q9WTS4-1]
DR Ensembl; ENSMUST00000115059; ENSMUSP00000110711; ENSMUSG00000016150. [Q9WTS4-1]
DR GeneID; 23963; -.
DR KEGG; mmu:23963; -.
DR UCSC; uc009tbc.1; mouse. [Q9WTS4-1]
DR CTD; 10178; -.
DR MGI; MGI:1345185; Tenm1.
DR VEuPathDB; HostDB:ENSMUSG00000016150; -.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_0_0_1; -.
DR InParanoid; Q9WTS4; -.
DR OMA; MPTRCQT; -.
DR PhylomeDB; Q9WTS4; -.
DR TreeFam; TF316833; -.
DR BioGRID-ORCS; 23963; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tenm1; mouse.
DR PRO; PR:Q9WTS4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WTS4; protein.
DR Bgee; ENSMUSG00000016150; Expressed in substantia nigra and 115 other tissues.
DR ExpressionAtlas; Q9WTS4; baseline and differential.
DR Genevisible; Q9WTS4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 3.
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 Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW Cytoplasm; Cytoskeleton; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Neuropeptide; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Secreted; Stress response; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..2731
FT /note="Teneurin-1"
FT /id="PRO_0000259499"
FT CHAIN 1..?
FT /note="Ten-1 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421007"
FT CHAIN 2602..2731
FT /note="Teneurin C-terminal-associated peptide"
FT /id="PRO_0000421008"
FT TOPO_DOM 1..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..2731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..318
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 527..558
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 559..590
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 591..623
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 624..656
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 657..690
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 691..720
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 721..752
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 760..795
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1193..1218
FT /note="NHL 1"
FT REPEAT 1298..1342
FT /note="NHL 2"
FT REPEAT 1357..1408
FT /note="NHL 3"
FT REPEAT 1420..1464
FT /note="NHL 4"
FT REPEAT 1487..1530
FT /note="NHL 5"
FT REPEAT 1540..1559
FT /note="YD 1"
FT REPEAT 1576..1596
FT /note="YD 2"
FT REPEAT 1614..1638
FT /note="YD 3"
FT REPEAT 1639..1660
FT /note="YD 4"
FT REPEAT 1661..1681
FT /note="YD 5"
FT REPEAT 1851..1870
FT /note="YD 6"
FT REPEAT 1871..1891
FT /note="YD 7"
FT REPEAT 1892..1910
FT /note="YD 8"
FT REPEAT 1911..1931
FT /note="YD 9"
FT REPEAT 1939..1955
FT /note="YD 10"
FT REPEAT 1956..1975
FT /note="YD 11"
FT REPEAT 1976..1995
FT /note="YD 12"
FT REPEAT 1998..2018
FT /note="YD 13"
FT REPEAT 2021..2041
FT /note="YD 14"
FT REPEAT 2091..2111
FT /note="YD 15"
FT REPEAT 2119..2139
FT /note="YD 16"
FT REPEAT 2159..2179
FT /note="YD 17"
FT REPEAT 2180..2200
FT /note="YD 18"
FT REPEAT 2202..2222
FT /note="YD 19"
FT REPEAT 2234..2254
FT /note="YD 20"
FT REPEAT 2256..2276
FT /note="YD 21"
FT REPEAT 2302..2319
FT /note="YD 22"
FT REPEAT 2320..2343
FT /note="YD 23"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..65
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT MOTIF 290..297
FT /note="Required for interaction with SORBS1 (Ten-1 ICD
FT form)"
FT /evidence="ECO:0000250"
FT COMPBIAS 21..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2601..2602
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKZ4"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 531..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 535..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 548..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 566..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 579..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 595..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 613..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 627..638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 632..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 665..678
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 680..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 694..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 711..720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 725..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 729..740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..774
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 768..783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 785..794
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..2613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045018"
SQ SEQUENCE 2731 AA; 305795 MW; 9129FA4CFE4A7770 CRC64;
MEQTDCKPYQ PLSKVKHEMD LAYTSSSDES EDGRKPRQSF NSRETLHEYN QELRRNYNSQ
SRKRKDVEKS TQEIEFCETP PTLCSGYHTD MHSVSRHGYQ LEMGSDVDTE TEGAASPDHA
LRMWIRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGENG FKFSPVCCDM EAPADSAQDM
QSSPHNQFTF RPLPPPPPPP HACTCARKPP PTVDSLQRRS MTTRSQPSPA APAPPTSTQD
SVHLHNSWVL NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF
SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ PVGQIYANGI
SNGNPGTESM DTTYSPIGGR VSDKSEKKVF QKGRAIDTGE VDIGAQVMQT IPPGLFWRFQ
ITIHHPIYLK FNISLAKDSL LGIYGRRNIP PTHTQFDFVK LMDGKQLVKQ DSKSSDDIQH
SPRNLILTSL QETGFIEYMD QGPWYLAFYN DGKKMEQVFV LTTAIEIMDD CSTNCNGNGE
CISGHCHCFP GFLGPDCARD SCPVLCGGNG EYEKGHCVCR NGWKGPECDV PEEQCIDPTC
FGHGTCIMGV CICVPGYKGE ICEEEDCLDP MCSSHGICVK GECHCSTGWG GVNCETPLPI
CQEQCSGHGT FLLDTGVCSC DPKWTGSDCS TELCTMECGS HGVCSRGICQ CEEGWVGPTC
EERSCHSHCA EHGQCKDGKC ECSPGWEGDH CTIAHYLDAV RDGCPGLCFG NGRCTLDQNG
WHCVCQVGWS GTGCNIVMEM LCGDNLDNDG DGLTDCVDPD CCQQSNCYVS PLCQGSPDPL
DLIQQSQPLF SQHTSRLFYD RIKFLIGKDS THVVPQDISF DSRRACVIRG QVVAVDGTPL
VGVNVSFLHH SDYGFTISRQ DGSFDLVAIG GISVVLIFDR SPFLSEKRTL WLPWNQFIVV
EKVIMQRIVA DAPSCDISNF ISPNPIVLPS PLTSFGGSCP ERGTIVPELQ VVQEEIPIPS
SFVRLSYLSS RTPGYKTLLR ILLTHSTIPV GMIKVHLTVS VEGRLTQKWF PAAINLVYTF
AWNKTDIYGQ KVWGLAEALV SVGYEYEMCP EFILWEQRTV VLQGFEMDAS NLGGWSLNKH
HIFNPQSGII HKGNGENMFI SQQPPVIATI MGNGHQRSVA CTNCNGPAHN NKLFAPVALA
SGPDGSVYVG DFNFVRRIFP SGNSVSILEL RNRDTRHSTS PAHKYYLAMD PMSESLYLSD
TNTRKVYKLK SLVETKDLSK NFEVVAGTGD QCLPFDQSHC GDGGKASEAS LNSPRGITVD
RHGFIYFVDG TMIRRIDENA VITTVIGSNG LTSTQPLSCD SGMDITQVRL EWPTDLAVNP
MDNSLYVLDN NIVLQISENR RVRIIAGRPI HCQVPGIDHF LVSKVAIHST LESARAISVS
HSGLLFIAET DERKVNRIQQ VTTNGEISII AGAPTDCDCK IDPNCDCFSG DGGYAKDAKM
KAPSSLAVSP DGTLYVADLG NVRIRTISKN QAHLNDMNLY EIASPADQEL YQFTVNGTHL
HTMNLITRDY VYNFTYNAEG DLGAITSSNG NSVHIRRDAG GMPLWLVVPG GQVYWLTISS
NGVLKRVSAQ GYNLALMTYP GNTGLLATKS NENGWTTVYE YDPEGHLTNA TFPTGEVSSF
HSDLEKLTKV ALDTSNRENV LMSTNLTATS TIYILKQENT QSTYRVSPDG SLRVTFASGM
EINLSSEPHI LAGAVNPTLG KCNISLPGEH NANLIEWRQR KEQNKGNVSA FERRLRAHNR
NLLSIDFDHM TRTGKIYDDH RKFTLRILYD QTGRPILWSP VSRYNEVNIT YSPSGLVTFI
QRGTWNEKME YDQSGKIISR TWADGKIWSY TYLEKSVMLL LHSQRRYIFE YDQSDCLLSV
TMPSMVRHSL QTMLSVGYYR NIYTPPDSST SFIQDYSRDG RLLQTLHLGT GRRVLYKYTK
QARLSEILYD TTQVTLTYEE SSGVIKTIHL MHDGFICTIR YRQTGPLIGR QIFRFSEEGL
VNARFDYSYN NFRVTSMQAV INETPLPIDL YRYVDVSGRT EQFGKFSVIN YDLNQVITTT
VMKHTKIFNA NGQVIEVQYE ILKAIAYWMT IQYDNMGRMV ICDIRVGVDA NITRYFYEYD
ADGQLQTVSV NDKIQWRYSY DLNGNINLLS HGNSARLTPL RYDLRDRITR LGEIQYKMDE
DGFLRQRGND IFEYNSNGLL QKAYNKVSGW TVQYYYDGLG RRVASKSSLG QHLQFFYADL
ANPIRVTHLY NHTSAEITSL YYDLQGHLIA MELSSGEEYY VACDNMGTPL AVFSSRGQVI
KEILYTPYGD IYHDTYPDFE VIIGFHGGLY DFLTKLVHLG QRDYDVVAGR WTTPNHHIWK
QLNLLPKPFN LYSFENNYPV GKIQDVAKYT TDIGTWLELF GFQLHNVLPG FPKPELENME
LTYELLQLQT KTQEWDPGKM ILGIQCELQK QLRNFISLDQ LPMTPQYNEG RCLEGGKQPR
FAAVPSVFGK GIKFAIKEGI VTADIIGVAN EDSRRLAAIL NNAHYLENLH FTIEGRDTHY
FIKLGSLEED LVLIGNTGGR RILENGVNVT VSQMTSVLNG RTRRFADIQL QHGALCFNIR
YGTTVEEEKN HVLEMARQRA VAQAWTQEQR RLQEGEEGTR VWTEGEKQQL LGTGRVQGYD
GYFVLSVEQY LELSDSANNI HFMRQSEIGR R
