TEN1_HUMAN » Teneurin-1

TEN1_HUMAN » Teneurin-1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
TEN1_HUMAN » Teneurin-1 » Ten-1; Protein Odd Oz/ten-m homolog 1;Tenascin-M1;Ten-m1; Teneurin transmembrane protein 1;
Hydrophobic Thickness 39.2 ± 1.6 Å
Tilt Angle 0 ± 1°
ΔGtransfer -43.6 kcal/mol
ΔGfold -21.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology In
TM Segments 320-347 (317-347)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 13-179, Teneurin Intracellular Region

AA: 168-317, Teneurin Intracellular Region

AA: 2641-2718, GHH signature containing HNH/Endo VII superfamily nuclease toxin

UniProt annotation for TEN1_HUMAN » Teneurin-1
FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity).

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 (By similarity).

FUNCTION: Ten-1 intracellular domain: Induces gene transcription activation.

SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either TENM2 or TENM3. May also form heterodimer with TENM4. Ten-1 ICD interacts with SORBS1 (via third SH3 domain). Interacts with MBD1 (By similarity).

TISSUE SPECIFICITY: Expressed in fetal brain.

DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.

DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins.

MISCELLANEOUS: Teneurin C-terminal-associated peptide: Binds to the plasma membrane and may be internalized by a receptor- and caveolae-mediated endocytosis manner to reach cytosolic compartments in a dynamin-dependent manner.

UniProt features for TEN1_HUMAN » Teneurin-1
CHAIN 1 2725 Teneurin-1.
CHAIN 1 ? Ten-1 intracellular domain (By similarity).
CHAIN 2596 2725 Teneurin C-terminal-associated peptide (By similarity).
DOMAIN 1 318 Teneurin N-terminal.
DOMAIN 528 559 EGF-like 1.
DOMAIN 560 591 EGF-like 2.
DOMAIN 592 624 EGF-like 3.
DOMAIN 625 657 EGF-like 4.
DOMAIN 658 691 EGF-like 5.
DOMAIN 692 721 EGF-like 6.
DOMAIN 722 753 EGF-like 7.
DOMAIN 761 796 EGF-like 8.
REPEAT 1194 1219 NHL 1.
REPEAT 1292 1336 NHL 2.
REPEAT 1351 1402 NHL 3.
REPEAT 1414 1458 NHL 4.
REPEAT 1481 1524 NHL 5.
REPEAT 1534 1553 YD 1.
REPEAT 1570 1590 YD 2.
REPEAT 1608 1632 YD 3.
REPEAT 1633 1654 YD 4.
REPEAT 1655 1675 YD 5.
REPEAT 1845 1864 YD 6.
REPEAT 1865 1885 YD 7.
REPEAT 1886 1904 YD 8.
REPEAT 1905 1925 YD 9.
REPEAT 1933 1949 YD 10.
REPEAT 1950 1969 YD 11.
REPEAT 1970 1989 YD 12.
REPEAT 1992 2012 YD 13.
REPEAT 2015 2035 YD 14.
REPEAT 2085 2105 YD 15.
REPEAT 2113 2133 YD 16.
REPEAT 2153 2173 YD 17.
REPEAT 2174 2194 YD 18.
REPEAT 2196 2216 YD 19.
REPEAT 2228 2248 YD 20.
REPEAT 2250 2270 YD 21.
REPEAT 2296 2313 YD 22.
REPEAT 2314 2337 YD 23.
MOTIF 62 65 Nuclear localization signal (NLS) (By similarity).
MOTIF 290 297 Required for interaction with SORBS1 (Ten-1 ICD form) (By similarity).
SITE 2595 2596 Cleavage (Probable).
DISULFID 532 542 By similarity.
DISULFID 536 547 By similarity.
DISULFID 549 558 By similarity.
DISULFID 567 578 By similarity.
DISULFID 580 589 By similarity.
DISULFID 596 607 By similarity.
DISULFID 601 612 By similarity.
DISULFID 614 623 By similarity.
DISULFID 628 639 By similarity.
DISULFID 633 644 By similarity.
DISULFID 646 655 By similarity.
DISULFID 666 679 By similarity.
DISULFID 681 690 By similarity.
DISULFID 695 705 By similarity.
DISULFID 699 710 By similarity.
DISULFID 712 721 By similarity.
DISULFID 726 736 By similarity.
DISULFID 730 741 By similarity.
DISULFID 743 752 By similarity.
DISULFID 765 775 By similarity.
DISULFID 769 784 By similarity.
DISULFID 786 795 By similarity.
Amino Acid Sequence for TEN1_HUMAN » Teneurin-1
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