ID   TEN1_HUMAN              Reviewed;        2725 AA.
AC   Q9UKZ4; B2RTR5; Q5JZ17;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   02-SEP-2026, entry version 185.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10556288; DOI=10.1093/hmg/8.13.2407;
RA   Brandau O., Schuster V., Weiss M., Hellebrand H., Fink F.M., Kreczy A.,
RA   Friedrich W., Strahm B., Niemeyer C., Belohradsky B.H., Meindl A.;
RT   "Epstein-Barr virus-negative boys with non-Hodgkin lymphoma are mutated in
RT   the SH2D1A gene, as are patients with X-linked lymphoproliferative disease
RT   (XLP).";
RL   Hum. Mol. Genet. 8:2407-2413(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=10341219; DOI=10.1242/jcs.112.12.2019;
RA   Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S., Chiquet-Ehrismann R.;
RT   "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m,
RT   is a neuronal protein with a novel type of heparin-binding domain.";
RL   J. Cell Sci. 112:2019-2032(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2580, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   VARIANTS [LARGE SCALE ANALYSIS] PHE-342; ILE-1216; VAL-1482; HIS-2235 AND
RP   PHE-2396.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [7]
RP   VARIANT ASP-174.
RX   PubMed=23092983; DOI=10.1038/tp.2012.102;
RA   Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA   Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA   Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA   Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA   Brice A., Depienne C.;
RT   "Analysis of the chromosome X exome in patients with autism spectrum
RT   disorders identified novel candidate genes, including TMLHE.";
RL   Transl. Psychiatry 2:E179-E179(2012).
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. Also acts 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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       Ten-1 ICD interacts with HINT1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WTS4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
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:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}.
CC       Note=Colocalizes with the dystroglycan complex at the cell membrane in
CC       hippocampal cells. Binds hippocampal cell membranes and is incorporated
CC       in the cytoplasm by endocytosis in a caveoli-dependent manner. Upon
CC       cell internalization is transported arround and in the nucleus (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UKZ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UKZ4-2; Sequence=VSP_043356;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal brain.
CC       {ECO:0000269|PubMed:10341219}.
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: [Teneurin C-terminal-associated peptide]: Derives from the plasma
CC       membrane form by proteolytic processing. Further proteolytic cleavage
CC       may be generated (By similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF100772; AAF04723.1; -; mRNA.
DR   EMBL; AL022718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL023878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z81008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z83823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z85995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC140783; AAI40784.1; -; mRNA.
DR   CCDS; CCDS14609.1; -. [Q9UKZ4-1]
DR   RefSeq; NP_001156750.1; NM_001163278.2. [Q9UKZ4-2]
DR   RefSeq; NP_001156751.1; NM_001163279.1.
DR   RefSeq; NP_055068.2; NM_014253.3. [Q9UKZ4-1]
DR   RefSeq; XP_016884703.1; XM_017029214.3. [Q9UKZ4-1]
DR   RefSeq; XP_054182325.1; XM_054326350.1. [Q9UKZ4-1]
DR   SMR; Q9UKZ4; -.
DR   BioGRID; 115477; 22.
DR   FunCoup; Q9UKZ4; 468.
DR   IntAct; Q9UKZ4; 5.
DR   MINT; Q9UKZ4; -.
DR   STRING; 9606.ENSP00000403954; -.
DR   TCDB; 9.B.87.1.19; the selenoprotein p receptor (selp-receptor) family.
DR   GlyConnect; Q9UKZ4; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9UKZ4; 13 sites, 2 glycans.
DR   GlyGen; Q9UKZ4; 16 sites, 15 N-linked glycans (5 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9UKZ4; -.
DR   PhosphoSitePlus; Q9UKZ4; -.
DR   BioMuta; TENM1; -.
DR   DMDM; 117949792; -.
DR   jPOST; Q9UKZ4; -.
DR   MassIVE; Q9UKZ4; -.
DR   PaxDb; 9606-ENSP00000403954; -.
DR   PeptideAtlas; Q9UKZ4; -.
DR   ProteomicsDB; 84918; -. [Q9UKZ4-1]
DR   ProteomicsDB; 84919; -. [Q9UKZ4-2]
DR   Antibodypedia; 482; 117 antibodies from 27 providers.
DR   DNASU; 10178; -.
DR   Ensembl; ENST00000371130.7; ENSP00000360171.3; ENSG00000009694.14. [Q9UKZ4-1]
DR   Ensembl; ENST00000422452.4; ENSP00000403954.4; ENSG00000009694.14. [Q9UKZ4-2]
DR   GeneID; 10178; -.
DR   KEGG; hsa:10178; -.
DR   MANE-Select; ENST00000422452.4; ENSP00000403954.4; NM_001163278.2; NP_001156750.1. [Q9UKZ4-2]
DR   UCSC; uc004euj.4; human. [Q9UKZ4-1]
DR   AGR; HGNC:8117; -.
DR   ClinPGx; PA31904; -.
DR   CTD; 10178; -.
DR   DisGeNET; 10178; -.
DR   GeneCards; TENM1; -.
DR   HGNC; HGNC:8117; TENM1.
DR   HPA; ENSG00000009694; Tissue enhanced (brain).
DR   MalaCards; TENM1; -.
DR   MIM; 300588; gene.
DR   OpenTargets; ENSG00000009694; -.
DR   Orphanet; 88620; Isolated congenital anosmia.
DR   VEuPathDB; HostDB:ENSG00000009694; -.
DR   eggNOG; KOG4659; Eukaryota.
DR   GeneTree; ENSGT01030000234566; -.
DR   HOGENOM; CLU_000229_0_0_1; -.
DR   InParanoid; Q9UKZ4; -.
DR   OMA; DNMGRMI; -.
DR   OrthoDB; 442731at2759; -.
DR   PAN-GO; Q9UKZ4; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UKZ4; -.
DR   PathwayCommons; Q9UKZ4; -.
DR   SignaLink; Q9UKZ4; -.
DR   Agora; ENSG00000009694; -.
DR   BioGRID-ORCS; 10178; 8 hits in 778 CRISPR screens.
DR   ChiTaRS; TENM1; human.
DR   GeneWiki; ODZ1; -.
DR   GenomeRNAi; 10178; -.
DR   Pharos; Q9UKZ4; Tbio.
DR   PRO; PR:Q9UKZ4; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UKZ4; protein.
DR   Bgee; ENSG00000009694; Expressed in cerebellar vermis and 155 other cell types or tissues.
DR   ExpressionAtlas; Q9UKZ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS: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; TAS:ProtInc.
DR   GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; ISS: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; ISS:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 1.
DR   FunFam; 2.180.10.10:FF:000019; Teneurin transmembrane protein 1; 1.
DR   FunFam; 2.10.25.10:FF:000016; Teneurin transmembrane protein 2; 1.
DR   FunFam; 2.10.25.10:FF:000021; Teneurin transmembrane protein 2; 2.
DR   FunFam; 2.10.25.10:FF:000013; Teneurin transmembrane protein 4; 1.
DR   FunFam; 2.120.10.30:FF:000005; Teneurin transmembrane protein 4; 1.
DR   FunFam; 2.120.10.30:FF:000006; Teneurin transmembrane protein 4; 1.
DR   FunFam; 2.10.25.10:FF:000169; teneurin-1 isoform X1; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 2.180.10.10; RHS repeat-associated core; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR057627; FN-plug_TEN1-4.
DR   InterPro; IPR056823; TEN-like_YD-shell.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR056822; TEN_NHL.
DR   InterPro; IPR056820; TEN_TTR-like.
DR   InterPro; IPR051216; Teneurin.
DR   InterPro; IPR057629; Teneurin1-4_GBD.
DR   InterPro; IPR028916; Tox-GHH_dom.
DR   InterPro; IPR006530; YD.
DR   NCBIfam; TIGR01643; YD_repeat_2x; 3.
DR   PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR   PANTHER; PTHR11219:SF7; TENEURIN-1; 1.
DR   Pfam; PF25024; EGF_TEN; 1.
DR   Pfam; PF24329; FN-plug_TEN1-4; 1.
DR   Pfam; PF23093; GBD_Tenm3; 1.
DR   Pfam; PF06484; Ten_N; 2.
DR   Pfam; PF25021; TEN_NHL; 1.
DR   Pfam; PF25023; TEN_YD-shell; 1.
DR   Pfam; PF23538; Teneurin_ABD; 1.
DR   Pfam; PF15636; Tox-GHH; 1.
DR   Pfam; PF25020; TTR_TEN1-4; 1.
DR   SMART; SM00181; EGF; 8.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
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; Proteomics identification;
KW   Reference proteome; Repeat; Repressor; Stress response; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2725
FT                   /note="Teneurin-1"
FT                   /id="PRO_0000259498"
FT   CHAIN           1..?
FT                   /note="Ten-1 intracellular domain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421005"
FT   CHAIN           2596..2725
FT                   /note="Teneurin C-terminal-associated peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421006"
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..2725
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          528..559
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          560..591
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          592..624
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          625..657
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          658..691
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          692..721
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          722..753
FT                   /note="EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          761..796
FT                   /note="EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          1194..1219
FT                   /note="NHL 1"
FT   REPEAT          1292..1336
FT                   /note="NHL 2"
FT   REPEAT          1351..1402
FT                   /note="NHL 3"
FT   REPEAT          1414..1458
FT                   /note="NHL 4"
FT   REPEAT          1481..1524
FT                   /note="NHL 5"
FT   REPEAT          1534..1553
FT                   /note="YD 1"
FT   REPEAT          1570..1590
FT                   /note="YD 2"
FT   REPEAT          1608..1632
FT                   /note="YD 3"
FT   REPEAT          1633..1654
FT                   /note="YD 4"
FT   REPEAT          1655..1675
FT                   /note="YD 5"
FT   REPEAT          1845..1864
FT                   /note="YD 6"
FT   REPEAT          1865..1885
FT                   /note="YD 7"
FT   REPEAT          1886..1904
FT                   /note="YD 8"
FT   REPEAT          1905..1925
FT                   /note="YD 9"
FT   REPEAT          1933..1949
FT                   /note="YD 10"
FT   REPEAT          1950..1969
FT                   /note="YD 11"
FT   REPEAT          1970..1989
FT                   /note="YD 12"
FT   REPEAT          1992..2012
FT                   /note="YD 13"
FT   REPEAT          2015..2035
FT                   /note="YD 14"
FT   REPEAT          2085..2105
FT                   /note="YD 15"
FT   REPEAT          2113..2133
FT                   /note="YD 16"
FT   REPEAT          2153..2173
FT                   /note="YD 17"
FT   REPEAT          2174..2194
FT                   /note="YD 18"
FT   REPEAT          2196..2216
FT                   /note="YD 19"
FT   REPEAT          2228..2248
FT                   /note="YD 20"
FT   REPEAT          2250..2270
FT                   /note="YD 21"
FT   REPEAT          2296..2313
FT                   /note="YD 22"
FT   REPEAT          2314..2337
FT                   /note="YD 23"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..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        174..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..201
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            2595..2596
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTS4"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTS4"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTS4"
FT   MOD_RES         2580
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        905
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1084
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1663
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1757
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1781
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1842
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        532..542
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        536..547
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        549..558
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        567..578
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        580..589
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        596..607
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        601..612
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        614..623
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        628..639
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        633..644
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        646..655
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        666..679
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        681..690
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        695..705
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        699..710
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        712..721
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        726..736
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        730..741
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        743..752
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        765..775
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        769..784
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        786..795
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         1231
FT                   /note="L -> LRNRDTRH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043356"
FT   VARIANT         40
FT                   /note="Y -> H (in dbSNP:rs36065191)"
FT                   /id="VAR_053792"
FT   VARIANT         174
FT                   /note="A -> D (in dbSNP:rs139486546)"
FT                   /evidence="ECO:0000269|PubMed:23092983"
FT                   /id="VAR_076255"
FT   VARIANT         342
FT                   /note="L -> F (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036596"
FT   VARIANT         371
FT                   /note="M -> T (in dbSNP:rs2213591)"
FT                   /id="VAR_053793"
FT   VARIANT         632
FT                   /note="M -> V (in dbSNP:rs16999334)"
FT                   /id="VAR_053794"
FT   VARIANT         641
FT                   /note="K -> E (in dbSNP:rs6649271)"
FT                   /id="VAR_053795"
FT   VARIANT         1216
FT                   /note="V -> I (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs137882910)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036597"
FT   VARIANT         1482
FT                   /note="F -> V (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036598"
FT   VARIANT         2235
FT                   /note="Q -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036599"
FT   VARIANT         2396
FT                   /note="L -> F (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036600"
FT   CONFLICT        261
FT                   /note="F -> S (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1135
FT                   /note="G -> D (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1628
FT                   /note="L -> P (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1908
FT                   /note="P -> S (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2133..2137
FT                   /note="MVICD -> HGNMC (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2179
FT                   /note="N -> D (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2271..2275
FT                   /note="YADLT -> VDATA (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2388..2389
FT                   /note="PN -> AY (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2611
FT                   /note="V -> L (in Ref. 1; AAF04723)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2725 AA;  305011 MW;  70F5C22BF33B5BB7 CRC64;
     MEQTDCKPYQ PLPKVKHEMD LAYTSSSDES EDGRKPRQSY NSRETLHEYN QELRMNYNSQ
     SRKRKEVEKS TQEMEFCETS HTLCSGYQTD MHSVSRHGYQ LEMGSDVDTE TEGAASPDHA
     LRMWIRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGENG FKFSPVCCDM EAQAGSTQDV
     QSSPHNQFTF RPLPPPPPPP HACTCARKPP PAADSLQRRS MTTRSQPSPA APAPPTSTQD
     SVHLHNSWVL NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF
     SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ PVEGELYANG
     VSKGNRGTES MDTTYSPIGG KVSDKSEKKV FQKGRAIDTG EVDIGAQVMQ TIPPGLFWRF
     QITIHHPIYL KFNISLAKDS LLGIYGRRNI PPTHTQFDFV KLMDGKQLVK QDSKGSDDTQ
     HSPRNLILTS LQETGFIEYM DQGPWYLAFY NDGKKMEQVF VLTTAIEIMD DCSTNCNGNG
     ECISGHCHCF PGFLGPDCAR DSCPVLCGGN GEYEKGHCVC RHGWKGPECD VPEEQCIDPT
     CFGHGTCIMG VCICVPGYKG EICEEEDCLD PMCSNHGICV KGECHCSTGW GGVNCETPLP
     VCQEQCSGHG TFLLDAGVCS CDPKWTGSDC STELCTMECG SHGVCSRGIC QCEEGWVGPT
     CEERSCHSHC TEHGQCKDGK CECSPGWEGD HCTIAHYLDA VRDGCPGLCF GNGRCTLDQN
     GWHCVCQVGW SGTGCNVVME MLCGDNLDND GDGLTDCVDP DCCQQSNCYI SPLCQGSPDP
     LDLIQQSQTL FSQHTSRLFY DRIKFLIGKD STHVIPPEVS FDSRRACVIR GQVVAIDGTP
     LVGVNVSFLH HSDYGFTISR QDGSFDLVAI GGISVILIFD RSPFLPEKRT LWLPWNQFIV
     VEKVTMQRVV SDPPSCDISN FISPNPIVLP SPLTSFGGSC PERGTIVPEL QVVQEEIPIP
     SSFVRLSYLS SRTPGYKTLL RILLTHSTIP VGMIKVHLTV AVEGRLTQKW FPAAINLVYT
     FAWNKTDIYG QKVWGLAEAL VSVGYEYETC PDFILWEQRT VVLQGFEMDA SNLGGWSLNK
     HHILNPQSGI IHKGNGENMF ISQQPPVIST IMGNGHQRSV ACTNCNGPAH NNKLFAPVAL
     ASGPDGSVYV GDFNFVRRIF PSGNSVSILE LSTSPAHKYY LAMDPVSESL YLSDTNTRKV
     YKLKSLVETK DLSKNFEVVA GTGDQCLPFD QSHCGDGGRA SEASLNSPRG ITVDRHGFIY
     FVDGTMIRKI DENAVITTVI GSNGLTSTQP LSCDSGMDIT QVRLEWPTDL AVNPMDNSLY
     VLDNNIVLQI SENRRVRIIA GRPIHCQVPG IDHFLVSKVA IHSTLESARA ISVSHSGLLF
     IAETDERKVN RIQQVTTNGE IYIIAGAPTD CDCKIDPNCD CFSGDGGYAK DAKMKAPSSL
     AVSPDGTLYV ADLGNVRIRT ISRNQAHLND MNIYEIASPA DQELYQFTVN GTHLHTLNLI
     TRDYVYNFTY NSEGDLGAIT SSNGNSVHIR RDAGGMPLWL VVPGGQVYWL TISSNGVLKR
     VSAQGYNLAL MTYPGNTGLL ATKSNENGWT TVYEYDPEGH LTNATFPTGE VSSFHSDLEK
     LTKVELDTSN RENVLMSTNL TATSTIYILK QENTQSTYRV NPDGSLRVTF ASGMEIGLSS
     EPHILAGAVN PTLGKCNISL PGEHNANLIE WRQRKEQNKG NVSAFERRLR AHNRNLLSID
     FDHITRTGKI YDDHRKFTLR ILYDQTGRPI LWSPVSRYNE VNITYSPSGL VTFIQRGTWN
     EKMEYDQSGK IISRTWADGK IWSYTYLEKS VMLLLHSQRR YIFEYDQPDC LLSVTMPSMV
     RHSLQTMLSV GYYRNIYTPP DSSTSFIQDY SRDGRLLQTL HLGTGRRVLY KYTKQARLSE
     VLYDTTQVTL TYEESSGVIK TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD
     YSYNNFRVTS MQAVINETPL PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK
     IFSANGQVIE VQYEILKAIA YWMTIQYDNV GRMVICDIRV GVDANITRYF YEYDADGQLQ
     TVSVNDKTQW RYSYDLNGNI NLLSHGKSAR LTPLRYDLRD RITRLGEIQY KMDEDGFLRQ
     RGNDIFEYNS NGLLQKAYNK ASGWTVQYYY DGLGRRVASK SSLGQHLQFF YADLTNPIRV
     THLYNHTSSE ITSLYYDLQG HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT
     PYGDIYHDTY PDFQVIIGFH GGLYDFLTKL VHLGQRDYDV VAGRWTTPNH HIWKQLNLLP
     KPFNLYSFEN NYPVGKIQDV AKYTTDIRSW LELFGFQLHN VLPGFPKPEL ENLELTYELL
     RLQTKTQEWD PGKTILGIQC ELQKQLRNFI SLDQLPMTPR YNDGRCLEGG KQPRFAAVPS
     VFGKGIKFAI KDGIVTADII GVANEDSRRL AAILNNAHYL ENLHFTIEGR DTHYFIKLGS
     LEEDLVLIGN TGGRRILENG VNVTVSQMTS VLNGRTRRFA DIQLQHGALC FNIRYGTTVE
     EEKNHVLEIA RQRAVAQAWT KEQRRLQEGE EGIRAWTEGE KQQLLSTGRV QGYDGYFVLS
     VEQYLELSDS ANNIHFMRQS EIGRR
//