TEN1_HUMAN
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 03-AUG-2022, entry version 167.
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. 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 (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 CCDS; CCDS55488.1; -. [Q9UKZ4-2]
DR RefSeq; NP_001156750.1; NM_001163278.1. [Q9UKZ4-2]
DR RefSeq; NP_001156751.1; NM_001163279.1.
DR RefSeq; NP_055068.2; NM_014253.3. [Q9UKZ4-1]
DR RefSeq; XP_011529532.1; XM_011531230.2. [Q9UKZ4-2]
DR RefSeq; XP_016884703.1; XM_017029214.1. [Q9UKZ4-1]
DR SMR; Q9UKZ4; -.
DR BioGRID; 115477; 18.
DR IntAct; Q9UKZ4; 4.
DR MINT; Q9UKZ4; -.
DR STRING; 9606.ENSP00000403954; -.
DR TCDB; 9.B.87.1.19; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 1795; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UKZ4; 13 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9UKZ4; -.
DR PhosphoSitePlus; Q9UKZ4; -.
DR BioMuta; TENM1; -.
DR DMDM; 117949792; -.
DR EPD; Q9UKZ4; -.
DR MassIVE; Q9UKZ4; -.
DR PaxDb; Q9UKZ4; -.
DR PeptideAtlas; Q9UKZ4; -.
DR PRIDE; Q9UKZ4; -.
DR ProteomicsDB; 84918; -. [Q9UKZ4-1]
DR ProteomicsDB; 84919; -. [Q9UKZ4-2]
DR Antibodypedia; 482; 115 antibodies from 25 providers.
DR DNASU; 10178; -.
DR Ensembl; ENST00000371130.7; ENSP00000360171.3; ENSG00000009694.13. [Q9UKZ4-1]
DR Ensembl; ENST00000422452.2; ENSP00000403954.2; ENSG00000009694.13. [Q9UKZ4-2]
DR GeneID; 10178; -.
DR KEGG; hsa:10178; -.
DR UCSC; uc004euj.4; human. [Q9UKZ4-1]
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 neXtProt; NX_Q9UKZ4; -.
DR OpenTargets; ENSG00000009694; -.
DR Orphanet; 88620; Isolated congenital anosmia.
DR PharmGKB; PA31904; -.
DR VEuPathDB; HostDB:ENSG00000009694; -.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_0_0_1; -.
DR InParanoid; Q9UKZ4; -.
DR OMA; MPTRCQT; -.
DR OrthoDB; 7516at2759; -.
DR PhylomeDB; Q9UKZ4; -.
DR TreeFam; TF316833; -.
DR PathwayCommons; Q9UKZ4; -.
DR SignaLink; Q9UKZ4; -.
DR BioGRID-ORCS; 10178; 6 hits in 704 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 153 other tissues.
DR Genevisible; Q9UKZ4; HS.
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:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; 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:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; 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: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; 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 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; 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 21..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar 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 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
