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Database: UniProt
Entry: TEN1_CHICK
LinkDB: TEN1_CHICK
Original site: TEN1_CHICK 
ID   TEN1_CHICK              Reviewed;        2705 AA.
AC   Q9W6V6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   19-FEB-2014, entry version 83.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10341219;
RA   Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S.,
RA   Chiquet-Ehrismann R.;
RT   "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene
RT   ten-m, is a neuronal protein with a novel type of heparin-binding
RT   domain.";
RL   J. Cell Sci. 112:2019-2032(1999).
RN   [2]
RP   PROTEOLYTIC PROCESSING, FUNCTION OF TEN-1 ICD, INTERACTION WITH MBD1
RP   AND SORBS1, AND SUBCELLULAR LOCATION.
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
RT   CAP/ponsin resulting in subcellular codistribution and translocation
RT   to the nuclear matrix.";
RL   Exp. Cell Res. 305:122-132(2005).
RN   [3]
RP   PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   MUTAGENESIS OF 62-ARG--LYS-65.
RX   PubMed=18366734; DOI=10.1186/1471-213X-8-30;
RA   Kenzelmann D., Chiquet-Ehrismann R., Leachman N.T., Tucker R.P.;
RT   "Teneurin-1 is expressed in interconnected regions of the developing
RT   brain and is processed in vivo.";
RL   BMC Dev. Biol. 8:30-30(2008).
CC   -!- FUNCTION: Involved in neural development, regulating the
CC       establishment of proper connectivity within the nervous system.
CC       May function as a cellular signal transducer (By similarity).
CC   -!- FUNCTION: Teneurin C-terminal-associated peptide: Plays a role in
CC       the regulation of neuroplasticity in the limbic system. Mediates a
CC       rapid reorganization of actin- and tubulin-based cytoskeleton
CC       elements with an increase in dendritic arborization and spine
CC       density formation of neurons in the hippocampus and amygdala.
CC       Induces BDNF transcription inhibition in neurons. Activates the
CC       mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular
CC       signal-regulated kinase (ERK) cascade (By similarity).
CC   -!- FUNCTION: Ten-1 intracellular domain: Induces gene transcription
CC       activation.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with other
CC       teneurins (By similarity). Ten-1 ICD interacts with SORBS1 (via
CC       third SH3 domain). Interacts with MBD1 isoform 2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC   -!- SUBCELLULAR LOCATION: Ten-1 intracellular domain: Nucleus. Nucleus
CC       speckle. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Colocalizes
CC       with SORBS1 in the nucleus and to the cell periphery. Colocalizes
CC       with MBD1 and PML in foci associated with the nuclear matrix.
CC   -!- SUBCELLULAR LOCATION: Teneurin C-terminal-associated peptide:
CC       Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the neurons of the developing
CC       visual system and in fetal brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed in mitral cell, glomerular layer of
CC       the olfactory bulb, hippocampus, posteromedial cortex piriformis,
CC       nucleus rotundu, laminae 2 and 5 within the inner plexiform layer
CC       of the retina, stratum griseum, nucleus laminaris and
CC       magnocellularis in the hindbrain and Purkinje cells at embryonic
CC       day (E) 17 (at protein level). At E14, it is concentrated in the
CC       retina, the optic tectum and in specific nuclei in the dorsal
CC       diencephalon, it is concentrated in the stratum griseum centrale.
CC       Expression is seen in diencephalon, concentrated in the rotund
CC       nucleus and in the neighboring ovoid nucleus. Similar expression
CC       patterns are seen at E17.
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- PTM: Teneurin C-terminal-associated peptide: Derives from the
CC       plasma membrane form by proteolytic processing. Further
CC       proteolytic cleavage may be generated (By similarity).
CC   -!- PTM: Ten-1 intracellular domain: Derives from the plasma membrane
CC       form by proteolytic cleavage and translocates to the nucleus.
CC   -!- MISCELLANEOUS: Teneurin C-terminal-associated peptide: Binds to
CC       the plasma membrane and may be internalized by a receptor- and
CC       caveolae-mediated endocytosis manner to reach cytosolic
CC       compartments in a dynamin-dependent manner (By similarity).
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
CC   -!- SIMILARITY: Contains 1 teneurin N-terminal domain.
CC   -!- SIMILARITY: Contains 23 YD repeats.
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DR   EMBL; AJ238613; CAB43098.1; -; mRNA.
DR   RefSeq; NP_990193.1; NM_204862.1.
DR   UniGene; Gga.4323; -.
DR   ProteinModelPortal; Q9W6V6; -.
DR   MINT; MINT-1342396; -.
DR   STRING; 9031.ENSGALP00000031671; -.
DR   PaxDb; Q9W6V6; -.
DR   GeneID; 395668; -.
DR   KEGG; gga:395668; -.
DR   CTD; 395668; -.
DR   eggNOG; NOG323120; -.
DR   HOGENOM; HOG000231701; -.
DR   HOVERGEN; HBG080306; -.
DR   NextBio; 20815740; -.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; IDA: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 from RNA polymerase III promoter; ISS:UniProtKB.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 3.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR027688; TENM1.
DR   InterPro; IPR006530; YD.
DR   PANTHER; PTHR11219:SF7; PTHR11219:SF7; 1.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF06484; Ten_N; 2.
DR   SMART; SM00181; EGF; 6.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 2.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cleavage on pair of basic residues; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Neuropeptide; Nucleus; Reference proteome;
KW   Repeat; Repressor; Stress response; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN         1   2705       Teneurin-1.
FT                                /FTId=PRO_0000259500.
FT   CHAIN         1      ?       Ten-1 intracellular domain.
FT                                /FTId=PRO_0000421009.
FT   CHAIN      2576   2705       Teneurin C-terminal-associated peptide
FT                                (By similarity).
FT                                /FTId=PRO_0000421010.
FT   TOPO_DOM      1    305       Cytoplasmic (Potential).
FT   TRANSMEM    306    326       Helical; (Potential).
FT   TOPO_DOM    327   2705       Extracellular (Potential).
FT   DOMAIN        1    299       Teneurin N-terminal.
FT   DOMAIN      509    540       EGF-like 1.
FT   DOMAIN      541    572       EGF-like 2.
FT   DOMAIN      573    605       EGF-like 3.
FT   DOMAIN      606    638       EGF-like 4.
FT   DOMAIN      639    672       EGF-like 5.
FT   DOMAIN      673    702       EGF-like 6.
FT   DOMAIN      703    734       EGF-like 7.
FT   DOMAIN      735    769       EGF-like 8.
FT   REPEAT     1167   1192       NHL 1.
FT   REPEAT     1202   1246       NHL 2.
FT   REPEAT     1272   1316       NHL 3.
FT   REPEAT     1331   1382       NHL 4.
FT   REPEAT     1461   1504       NHL 5.
FT   REPEAT     1514   1533       YD 1.
FT   REPEAT     1550   1570       YD 2.
FT   REPEAT     1588   1612       YD 3.
FT   REPEAT     1613   1634       YD 4.
FT   REPEAT     1635   1655       YD 5.
FT   REPEAT     1825   1844       YD 6.
FT   REPEAT     1845   1865       YD 7.
FT   REPEAT     1866   1884       YD 8.
FT   REPEAT     1885   1905       YD 9.
FT   REPEAT     1913   1929       YD 10.
FT   REPEAT     1930   1949       YD 11.
FT   REPEAT     1950   1969       YD 12.
FT   REPEAT     1972   1992       YD 13.
FT   REPEAT     1995   2015       YD 14.
FT   REPEAT     2065   2085       YD 15.
FT   REPEAT     2093   2113       YD 16.
FT   REPEAT     2133   2153       YD 17.
FT   REPEAT     2154   2174       YD 18.
FT   REPEAT     2176   2196       YD 19.
FT   REPEAT     2208   2228       YD 20.
FT   REPEAT     2230   2250       YD 21.
FT   REPEAT     2276   2293       YD 22.
FT   REPEAT     2294   2317       YD 23.
FT   MOTIF        62     65       Nuclear localization signal (NLS).
FT   MOTIF       271    278       Required for interaction with SORBS1
FT                                (Ten-1 ICD form).
FT   COMPBIAS    173    181       Poly-Pro.
FT   SITE       2575   2576       Cleavage (Probable).
FT   CARBOHYD    414    414       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    878    878       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1057   1057       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1530   1530       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1547   1547       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1643   1643       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1679   1679       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1737   1737       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1761   1761       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1822   1822       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2125   2125       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2265   2265       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2582   2582       N-linked (GlcNAc...) (Potential).
FT   DISULFID    513    523       By similarity.
FT   DISULFID    517    528       By similarity.
FT   DISULFID    530    539       By similarity.
FT   DISULFID    548    559       By similarity.
FT   DISULFID    561    570       By similarity.
FT   DISULFID    577    588       By similarity.
FT   DISULFID    582    593       By similarity.
FT   DISULFID    595    604       By similarity.
FT   DISULFID    609    620       By similarity.
FT   DISULFID    614    625       By similarity.
FT   DISULFID    627    636       By similarity.
FT   DISULFID    647    660       By similarity.
FT   DISULFID    662    671       By similarity.
FT   DISULFID    676    686       By similarity.
FT   DISULFID    680    691       By similarity.
FT   DISULFID    693    702       By similarity.
FT   DISULFID    707    717       By similarity.
FT   DISULFID    711    722       By similarity.
FT   DISULFID    724    733       By similarity.
FT   DISULFID    738    748       By similarity.
FT   DISULFID    742    757       By similarity.
FT   DISULFID    759    768       By similarity.
FT   MUTAGEN      62     65       RKRK->AAAA: Inhibits translocation to the
FT                                nucleus (Ten-1 ICD form).
SQ   SEQUENCE   2705 AA;  302388 MW;  230F03D1999037D2 CRC64;
     MEQMDCKPYQ PLSKVKHEVD LTYTSSSDES EDGRKQRQSY DSRETLNEYS QELRLNYNSQ
     SRKRKNTDQS TQDMEFCETP HILCSGYQTD LHGVSEHSYP LEVGSDVDTE TEGGASPDHA
     LRMWMRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGEND MPGSPHNQFT FRPLPPPPPP
     PHACTCTRKP PPAADSLQRR SMTTRSQPSP AAPTPPTSTQ DSVHLHNSWV LNSNIPLETR
     HFLFKHGSGS SAIFSAASQN YPLTSNTVYS PPPRPLPRNT FSRPAFTFSK PYRCCNWKCT
     ALSATAITVT LALLLAYVIA VHLFGLTWQL QPVEGQLYEN GVSKGNKGAE STDTTYSPIG
     GKVSDKTEKK VFQKGRAIDT GEVEIGAQVM QTIPPGLFWR FQITIHHPVY LKFNISLAKD
     SLLGIYGRRN IPPTHTQFDF VKLMDGKQLI KQEPKNSEEP QQAPRNLILT SLQETGFIEY
     MDQGAWHMAF YNDGKKVEQV FVLTTAIEVL DDCSTNCNGN GECISGHCHC FPGFLGPDCA
     KDSCPVLCSG NGEYEKGHCV CRNGWKGPEC DVPEEQCIDP TCFGHGTCIM GVCICVPGYK
     GEICEEEDCL DPMCSGHGVC VQGECHCSAG WGGVNCETSL PICQEHCSGH GTFLLDVGLC
     SCEPQWTGSD CSTELCTLDC GSHGVCSRGI CQCEEGWVGP TCEERTCHSH CAEHGQCKDG
     KCECSPGWEG DHCTIDGCPG LCYGNGRCTL DQNGWHCVCQ VGWSGSGCNV VMEMACGDNL
     DNDGDGLTDC VDPDCCQQNN CYASPLCQGS PDPLDLIQHS QPPFSQHPPR LFYDRIRFLI
     GKESTHVIPG DISFESRRAS VIRGQVVAID GTPLVGVNVS FLHHDEYGYT ISRQDGSFDL
     VAVGGISVTL VFDRSPFISE KRTLWLSWNR FVIVDKVVMQ RAESDIPSCD VSSFISPNPI
     VLPSPLTAFG GSCPERGTVI PELQVVQEEI PIPSSFVKLS YLSSRTPGYK TLLRVILTHT
     TIPSGMTKVH LIIAVEGRLL QKWFPAAANL VYTFAWNKTD IYGQKVSGLA EAMVSVGYEY
     ETCPDFILWE KRTVILQGFE MDASNLGGWS INKHHVLNPQ SGIVHKGNGE NMFISQQPPV
     ISTMMGNGHQ RSVSCSNCNG LALNSKLFAP VALTSGPDGS VYIGDFNFVR RIFPSGNSIG
     ILELRNRDTR HSTSPAHKYY LAVDPVSESL YLSDTNTRRV YKAKSLIETK DLAKNVDVVA
     GTGDQCLPFD QSHCGDGGKA SEASLNSPRG ITIDKHGFIY FVDGTMIRKI DENGMITTII
     GSNGLTSTQP LSCDSGMDIT QVRLEWPTDL TVNPLDNSLY VLDNNIVLQI SESRRVRIIA
     GRPIHCQVPG IDHFIVSKVA IHSTLESARA IAVSHSGIPY IRETDERKIN RIQQVTTNGE
     ISIIAGAPSD CDCKIDPNCD CFSGDGGYAK DAKLKAPSSL AVSPDDTLYV ADLGNIRIRA
     VSRNKAHLSD TNMYEIASPA DQELYQFTIN GTHLHTLNLI TRDYIYNFTY SGEGDVATIT
     SSNGNSVHIR RDTSGLPLWV VVPGGQVYWL TISSNGVLKR VYAQGYNLAL MTYPGNTGLL
     ATKSDENGWT TVYEYDSDGH LTNATFPTGE VSSFHSDVEK LTRVELDTSN RENMVTATNF
     SATSTIYTLK QDNTQNIYRV SPDGSLRVTF ASGMEITLNT EPHILAGVVS PTLGKCNISL
     PGEHNSNLIE WRQRREQTKG NISTFERRLR AHNRNLLSID FDHVTRTGKI YDDHRKFTLR
     IMYDQTGRPV LWSPISKYNE VNITYSHSGL VTYIQRGTWT EKMEYDPSGN IISRTWADGK
     IWSYTYLEKS VMLLLHSQRR YIFEYDQSDY LLSVTMPSMV RHALQTMLSV GYYRNIYTPP
     DSGAAFIQDV TRDGRLLQTL YPGTGRRVLY KYSKQSRLSE ILYDTTQVTF TYEESSGVIK
     TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD YSYNNFRVTS MQAMINETPL
     PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK IFSANGQVIE VQYEILKSIA
     YWMTIQYDNM GRMVICDIRV GVDANITRYF YEYDRDGQLQ TVSVNDKTQW RYSYDLNGNI
     NLLSHGNSAR LTPLRYDLRD RITRLGEIQY KMDEDGFLRQ RGNEIFEYNS NGLLNKAYNK
     VSGWTVQYCY DGLGRRVASK SSLGQHLQFF YADLSNPIRV THLYNHSSSE ITSLYYDLQG
     HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT PYGEIYQDTN PDFQVVIGFH
     GGLYDSLTKL VHLGQRDYDV IAGRWTTPNH HIWKHLNAVP QPFNLYSFEN NYPVGRIQDV
     AKYTTDIGSW LELFGFQLHN VLPGFPKPEI EALETTYELL QLQTKTQEWD PGKTILGIQC
     ELQKQLRNFI SLDQLPMTPR YSDGKCYEGV KQPRFAAIPS VFGKGIKFAI KDGIVTADII
     GVANEDSRRI AAILNNAHYL ENLHFTIEGR DTHYFIKLGS LEEDLSLIGN TGGRRILENG
     VNVTVSQMTS VINGRTRRFA DIQLQHGALC FNVRYGTTVE EEKNHVLEVA RQRAVAQAWT
     KEQRRLQEGE EGIRAWTDGE KQQLLNTGRV QGYDGYFVLS VEQYLELSDS ANNIHFMRQS
     EIGRR
//
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