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Q9WTS4

- TEN1_MOUSE

UniProt

Q9WTS4 - TEN1_MOUSE

Protein

Teneurin-1

Gene

Tenm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer By similarity.By similarity
    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.10 Publications
    Ten-1 intracellular domain: Induces gene transcription activation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei2601 – 26022CleavageCurated

    GO - Molecular functioni

    1. protein heterodimerization activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. neuropeptide signaling pathway Source: UniProtKB-KW
    2. positive regulation of actin filament polymerization Source: UniProtKB
    3. positive regulation of filopodium assembly Source: UniProtKB
    4. positive regulation of intracellular protein transport Source: UniProtKB
    5. positive regulation of MAP kinase activity Source: UniProtKB
    6. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    9. response to stress Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Neuropeptide, Repressor

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Teneurin-1
    Short name:
    Ten-1
    Alternative name(s):
    Protein Odd Oz/ten-m homolog 1
    Tenascin-M1
    Short name:
    Ten-m1
    Teneurin transmembrane protein 1
    Cleaved into the following 2 chains:
    Ten-1 intracellular domain
    Short name:
    IDten-1
    Short name:
    Ten-1 ICD
    Alternative name(s):
    Ten-1 extracellular domain
    Short name:
    Ten-1 ECD
    Gene namesi
    Name:Tenm1
    Synonyms:Odz1, Tnm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1345185. Tenm1.

    Subcellular locationi

    Isoform 1 : Cell membrane 1 Publication; Single-pass membrane protein 1 Publication
    Note: Colocalizes with isoform 2 at the plasma membrane.
    Isoform 2 : Cytoplasm. Cell membrane. Secreted Curated
    Note: Transported to the cell membrane and probably secreted to function as an autocrine or paracrine signaling molecule. The lack of a hydrophobic segment sequence suggests that isoform 2 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.
    Chain Ten-1 intracellular domain : Nucleus By similarity. Nucleus speckle By similarity. Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity
    Chain Teneurin C-terminal-associated peptide : Nucleus Curated. Cytoplasm. Cell membrane
    Note: Colocalizes with isoform 1 at the plasma membrane. Colocalizes with the dystroglycan complex at the cell membrane in hippocampal cells. Binds hippocampal cell membranes and is incorporated in the cytoplasm by endocytosis in a caveoli-dependent manner. Upon cell internalization is transported arround and in the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. extracellular region Source: UniProtKB
    5. Golgi apparatus Source: UniProtKB
    6. integral component of plasma membrane Source: MGI
    7. nuclear matrix Source: UniProtKB
    8. nuclear speck Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27312731Teneurin-1PRO_0000259499Add
    BLAST
    Chaini1 – ?Ten-1 intracellular domainBy similarityPRO_0000421007
    Chaini2602 – 2731130Teneurin C-terminal-associated peptidePRO_0000421008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi531 ↔ 541PROSITE-ProRule annotation
    Disulfide bondi535 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi548 ↔ 557PROSITE-ProRule annotation
    Disulfide bondi566 ↔ 577PROSITE-ProRule annotation
    Disulfide bondi579 ↔ 588PROSITE-ProRule annotation
    Disulfide bondi595 ↔ 606PROSITE-ProRule annotation
    Disulfide bondi600 ↔ 611PROSITE-ProRule annotation
    Disulfide bondi613 ↔ 622PROSITE-ProRule annotation
    Disulfide bondi627 ↔ 638PROSITE-ProRule annotation
    Disulfide bondi632 ↔ 643PROSITE-ProRule annotation
    Disulfide bondi645 ↔ 654PROSITE-ProRule annotation
    Disulfide bondi665 ↔ 678PROSITE-ProRule annotation
    Disulfide bondi680 ↔ 689PROSITE-ProRule annotation
    Disulfide bondi694 ↔ 704PROSITE-ProRule annotation
    Disulfide bondi698 ↔ 709PROSITE-ProRule annotation
    Disulfide bondi711 ↔ 720PROSITE-ProRule annotation
    Disulfide bondi725 ↔ 735PROSITE-ProRule annotation
    Disulfide bondi729 ↔ 740PROSITE-ProRule annotation
    Disulfide bondi742 ↔ 751PROSITE-ProRule annotation
    Disulfide bondi764 ↔ 774PROSITE-ProRule annotation
    Disulfide bondi768 ↔ 783PROSITE-ProRule annotation
    Disulfide bondi785 ↔ 794PROSITE-ProRule annotation
    Glycosylationi904 – 9041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1083 – 10831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1556 – 15561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1573 – 15731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1669 – 16691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1705 – 17051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1743 – 17431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1787 – 17871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1848 – 18481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2151 – 21511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2291 – 22911N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2586 – 25861PhosphoserineBy similarity
    Glycosylationi2608 – 26081N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Isoform 2: Once secreted, may also be cleaved to give rise to the TCAP-1 form.1 Publication
    Teneurin C-terminal-associated peptide: Derives from the plasma membrane form by proteolytic processing. Further proteolytic cleavage may generate 11.9 and 4.7 kDa bioactive peptides.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9WTS4.
    PRIDEiQ9WTS4.

    PTM databases

    PhosphoSiteiQ9WTS4.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in the brain. Isoform 2 is expressed in the granular layer of the dentate gyrus and the pyramidal layer (Py) of the CA1, CA2 and CA3 of the hippocampus (at protein level). Expressed in the cortex, thalamus, CA1, CA2, CA3, dentate gyrus and granular layer of the hippocampus. Weakly expressed in kidney, testis and lung.4 Publications

    Developmental stagei

    Isoform 1 and isoform 2 are expressed in hippocampal cells at 14 dpc (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9WTS4.
    BgeeiQ9WTS4.
    CleanExiMM_ODZ1.
    GenevestigatoriQ9WTS4.

    Interactioni

    Subunit structurei

    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 isoform 2.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTS4.
    SMRiQ9WTS4. Positions 529-840, 1311-1340.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 324324CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini346 – 27312386ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei325 – 34521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 318318Teneurin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini527 – 55832EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini559 – 59032EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini591 – 62333EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini624 – 65633EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini657 – 69034EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini691 – 72030EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini721 – 75232EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini760 – 79536EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati1193 – 121826NHL 1Add
    BLAST
    Repeati1298 – 134245NHL 2Add
    BLAST
    Repeati1357 – 140852NHL 3Add
    BLAST
    Repeati1420 – 146445NHL 4Add
    BLAST
    Repeati1487 – 153044NHL 5Add
    BLAST
    Repeati1540 – 155920YD 1Add
    BLAST
    Repeati1576 – 159621YD 2Add
    BLAST
    Repeati1614 – 163825YD 3Add
    BLAST
    Repeati1639 – 166022YD 4Add
    BLAST
    Repeati1661 – 168121YD 5Add
    BLAST
    Repeati1851 – 187020YD 6Add
    BLAST
    Repeati1871 – 189121YD 7Add
    BLAST
    Repeati1892 – 191019YD 8Add
    BLAST
    Repeati1911 – 193121YD 9Add
    BLAST
    Repeati1939 – 195517YD 10Add
    BLAST
    Repeati1956 – 197520YD 11Add
    BLAST
    Repeati1976 – 199520YD 12Add
    BLAST
    Repeati1998 – 201821YD 13Add
    BLAST
    Repeati2021 – 204121YD 14Add
    BLAST
    Repeati2091 – 211121YD 15Add
    BLAST
    Repeati2119 – 213921YD 16Add
    BLAST
    Repeati2159 – 217921YD 17Add
    BLAST
    Repeati2180 – 220021YD 18Add
    BLAST
    Repeati2202 – 222221YD 19Add
    BLAST
    Repeati2234 – 225421YD 20Add
    BLAST
    Repeati2256 – 227621YD 21Add
    BLAST
    Repeati2302 – 231918YD 22Add
    BLAST
    Repeati2320 – 234324YD 23Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi62 – 654Nuclear localization signal (NLS)By similarity
    Motifi290 – 2978Required for interaction with SORBS1 (Ten-1 ICD form)By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 2009Poly-Pro

    Domaini

    EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.
    Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins.

    Sequence similaritiesi

    Belongs to the tenascin family. Teneurin subfamily.Curated
    Contains 8 EGF-like domains.PROSITE-ProRule annotation
    Contains 5 NHL repeats.Curated
    Contains 1 teneurin N-terminal domain.PROSITE-ProRule annotation
    Contains 23 YD repeats.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG323120.
    GeneTreeiENSGT00660000095277.
    HOGENOMiHOG000231701.
    HOVERGENiHBG080306.
    InParanoidiQ9WTS4.
    OMAiIAYWMTI.
    OrthoDBiEOG7H791C.
    PhylomeDBiQ9WTS4.
    TreeFamiTF316833.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009471. Ten_N.
    IPR027688. TENM1.
    IPR028916. Tox-GHH_dom.
    IPR006530. YD.
    [Graphical view]
    PANTHERiPTHR11219:SF7. PTHR11219:SF7. 1 hit.
    PfamiPF12661. hEGF. 1 hit.
    PF06484. Ten_N. 2 hits.
    PF15636. Tox-GHH. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 7 hits.
    [Graphical view]
    TIGRFAMsiTIGR01643. YD_repeat_2x. 3 hits.
    PROSITEiPS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS51361. TENEURIN_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WTS4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEQTDCKPYQ PLSKVKHEMD LAYTSSSDES EDGRKPRQSF NSRETLHEYN     50
    QELRRNYNSQ SRKRKDVEKS TQEIEFCETP PTLCSGYHTD MHSVSRHGYQ 100
    LEMGSDVDTE TEGAASPDHA LRMWIRGMKS EHSSCLSSRA NSALSLTDTD 150
    HERKSDGENG FKFSPVCCDM EAPADSAQDM QSSPHNQFTF RPLPPPPPPP 200
    HACTCARKPP PTVDSLQRRS MTTRSQPSPA APAPPTSTQD SVHLHNSWVL 250
    NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF 300
    SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ 350
    PVGQIYANGI SNGNPGTESM DTTYSPIGGR VSDKSEKKVF QKGRAIDTGE 400
    VDIGAQVMQT IPPGLFWRFQ ITIHHPIYLK FNISLAKDSL LGIYGRRNIP 450
    PTHTQFDFVK LMDGKQLVKQ DSKSSDDIQH SPRNLILTSL QETGFIEYMD 500
    QGPWYLAFYN DGKKMEQVFV LTTAIEIMDD CSTNCNGNGE CISGHCHCFP 550
    GFLGPDCARD SCPVLCGGNG EYEKGHCVCR NGWKGPECDV PEEQCIDPTC 600
    FGHGTCIMGV CICVPGYKGE ICEEEDCLDP MCSSHGICVK GECHCSTGWG 650
    GVNCETPLPI CQEQCSGHGT FLLDTGVCSC DPKWTGSDCS TELCTMECGS 700
    HGVCSRGICQ CEEGWVGPTC EERSCHSHCA EHGQCKDGKC ECSPGWEGDH 750
    CTIAHYLDAV RDGCPGLCFG NGRCTLDQNG WHCVCQVGWS GTGCNIVMEM 800
    LCGDNLDNDG DGLTDCVDPD CCQQSNCYVS PLCQGSPDPL DLIQQSQPLF 850
    SQHTSRLFYD RIKFLIGKDS THVVPQDISF DSRRACVIRG QVVAVDGTPL 900
    VGVNVSFLHH SDYGFTISRQ DGSFDLVAIG GISVVLIFDR SPFLSEKRTL 950
    WLPWNQFIVV EKVIMQRIVA DAPSCDISNF ISPNPIVLPS PLTSFGGSCP 1000
    ERGTIVPELQ VVQEEIPIPS SFVRLSYLSS RTPGYKTLLR ILLTHSTIPV 1050
    GMIKVHLTVS VEGRLTQKWF PAAINLVYTF AWNKTDIYGQ KVWGLAEALV 1100
    SVGYEYEMCP EFILWEQRTV VLQGFEMDAS NLGGWSLNKH HIFNPQSGII 1150
    HKGNGENMFI SQQPPVIATI MGNGHQRSVA CTNCNGPAHN NKLFAPVALA 1200
    SGPDGSVYVG DFNFVRRIFP SGNSVSILEL RNRDTRHSTS PAHKYYLAMD 1250
    PMSESLYLSD TNTRKVYKLK SLVETKDLSK NFEVVAGTGD QCLPFDQSHC 1300
    GDGGKASEAS LNSPRGITVD RHGFIYFVDG TMIRRIDENA VITTVIGSNG 1350
    LTSTQPLSCD SGMDITQVRL EWPTDLAVNP MDNSLYVLDN NIVLQISENR 1400
    RVRIIAGRPI HCQVPGIDHF LVSKVAIHST LESARAISVS HSGLLFIAET 1450
    DERKVNRIQQ VTTNGEISII AGAPTDCDCK IDPNCDCFSG DGGYAKDAKM 1500
    KAPSSLAVSP DGTLYVADLG NVRIRTISKN QAHLNDMNLY EIASPADQEL 1550
    YQFTVNGTHL HTMNLITRDY VYNFTYNAEG DLGAITSSNG NSVHIRRDAG 1600
    GMPLWLVVPG GQVYWLTISS NGVLKRVSAQ GYNLALMTYP GNTGLLATKS 1650
    NENGWTTVYE YDPEGHLTNA TFPTGEVSSF HSDLEKLTKV ALDTSNRENV 1700
    LMSTNLTATS TIYILKQENT QSTYRVSPDG SLRVTFASGM EINLSSEPHI 1750
    LAGAVNPTLG KCNISLPGEH NANLIEWRQR KEQNKGNVSA FERRLRAHNR 1800
    NLLSIDFDHM TRTGKIYDDH RKFTLRILYD QTGRPILWSP VSRYNEVNIT 1850
    YSPSGLVTFI QRGTWNEKME YDQSGKIISR TWADGKIWSY TYLEKSVMLL 1900
    LHSQRRYIFE YDQSDCLLSV TMPSMVRHSL QTMLSVGYYR NIYTPPDSST 1950
    SFIQDYSRDG RLLQTLHLGT GRRVLYKYTK QARLSEILYD TTQVTLTYEE 2000
    SSGVIKTIHL MHDGFICTIR YRQTGPLIGR QIFRFSEEGL VNARFDYSYN 2050
    NFRVTSMQAV INETPLPIDL YRYVDVSGRT EQFGKFSVIN YDLNQVITTT 2100
    VMKHTKIFNA NGQVIEVQYE ILKAIAYWMT IQYDNMGRMV ICDIRVGVDA 2150
    NITRYFYEYD ADGQLQTVSV NDKIQWRYSY DLNGNINLLS HGNSARLTPL 2200
    RYDLRDRITR LGEIQYKMDE DGFLRQRGND IFEYNSNGLL QKAYNKVSGW 2250
    TVQYYYDGLG RRVASKSSLG QHLQFFYADL ANPIRVTHLY NHTSAEITSL 2300
    YYDLQGHLIA MELSSGEEYY VACDNMGTPL AVFSSRGQVI KEILYTPYGD 2350
    IYHDTYPDFE VIIGFHGGLY DFLTKLVHLG QRDYDVVAGR WTTPNHHIWK 2400
    QLNLLPKPFN LYSFENNYPV GKIQDVAKYT TDIGTWLELF GFQLHNVLPG 2450
    FPKPELENME LTYELLQLQT KTQEWDPGKM ILGIQCELQK QLRNFISLDQ 2500
    LPMTPQYNEG RCLEGGKQPR FAAVPSVFGK GIKFAIKEGI VTADIIGVAN 2550
    EDSRRLAAIL NNAHYLENLH FTIEGRDTHY FIKLGSLEED LVLIGNTGGR 2600
    RILENGVNVT VSQMTSVLNG RTRRFADIQL QHGALCFNIR YGTTVEEEKN 2650
    HVLEMARQRA VAQAWTQEQR RLQEGEEGTR VWTEGEKQQL LGTGRVQGYD 2700
    GYFVLSVEQY LELSDSANNI HFMRQSEIGR R 2731
    Length:2,731
    Mass (Da):305,795
    Last modified:November 1, 1999 - v1
    Checksum:i9129FA4CFE4A7770
    GO
    Isoform 2 (identifier: Q9WTS4-2) [UniParc]FASTAAdd to Basket

    Also known as: TCAP-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2613: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:118
    Mass (Da):13,705
    Checksum:i69AF60B26B80DB7E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 26132613Missing in isoform 2. CuratedVSP_045018Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025410 mRNA. Translation: BAA77396.1.
    AK037897 mRNA. Translation: BAC29893.1.
    CCDSiCCDS40953.1. [Q9WTS4-1]
    RefSeqiNP_035985.2. NM_011855.4. [Q9WTS4-1]
    XP_006541552.1. XM_006541489.1. [Q9WTS4-1]
    XP_006541553.1. XM_006541490.1. [Q9WTS4-1]
    UniGeneiMm.327698.

    Genome annotation databases

    EnsembliENSMUST00000016294; ENSMUSP00000016294; ENSMUSG00000016150. [Q9WTS4-1]
    ENSMUST00000115059; ENSMUSP00000110711; ENSMUSG00000016150. [Q9WTS4-1]
    GeneIDi23963.
    KEGGimmu:23963.
    UCSCiuc009tbc.1. mouse. [Q9WTS4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025410 mRNA. Translation: BAA77396.1 .
    AK037897 mRNA. Translation: BAC29893.1 .
    CCDSi CCDS40953.1. [Q9WTS4-1 ]
    RefSeqi NP_035985.2. NM_011855.4. [Q9WTS4-1 ]
    XP_006541552.1. XM_006541489.1. [Q9WTS4-1 ]
    XP_006541553.1. XM_006541490.1. [Q9WTS4-1 ]
    UniGenei Mm.327698.

    3D structure databases

    ProteinModelPortali Q9WTS4.
    SMRi Q9WTS4. Positions 529-840, 1311-1340.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9WTS4.

    Proteomic databases

    PaxDbi Q9WTS4.
    PRIDEi Q9WTS4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016294 ; ENSMUSP00000016294 ; ENSMUSG00000016150 . [Q9WTS4-1 ]
    ENSMUST00000115059 ; ENSMUSP00000110711 ; ENSMUSG00000016150 . [Q9WTS4-1 ]
    GeneIDi 23963.
    KEGGi mmu:23963.
    UCSCi uc009tbc.1. mouse. [Q9WTS4-1 ]

    Organism-specific databases

    CTDi 10178.
    MGIi MGI:1345185. Tenm1.

    Phylogenomic databases

    eggNOGi NOG323120.
    GeneTreei ENSGT00660000095277.
    HOGENOMi HOG000231701.
    HOVERGENi HBG080306.
    InParanoidi Q9WTS4.
    OMAi IAYWMTI.
    OrthoDBi EOG7H791C.
    PhylomeDBi Q9WTS4.
    TreeFami TF316833.

    Miscellaneous databases

    NextBioi 303821.
    PROi Q9WTS4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WTS4.
    Bgeei Q9WTS4.
    CleanExi MM_ODZ1.
    Genevestigatori Q9WTS4.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009471. Ten_N.
    IPR027688. TENM1.
    IPR028916. Tox-GHH_dom.
    IPR006530. YD.
    [Graphical view ]
    PANTHERi PTHR11219:SF7. PTHR11219:SF7. 1 hit.
    Pfami PF12661. hEGF. 1 hit.
    PF06484. Ten_N. 2 hits.
    PF15636. Tox-GHH. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 7 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01643. YD_repeat_2x. 3 hits.
    PROSITEi PS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS51361. TENEURIN_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse ten-m/Odz is a new family of dimeric type II transmembrane proteins expressed in many tissues."
      Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T., Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.
      J. Cell Biol. 145:563-577(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Thymus.
    3. "All four members of the Ten-m/Odz family of transmembrane proteins form dimers."
      Feng K., Zhou X.H., Oohashi T., Morgelin M., Lustig A., Hirakawa S., Ninomiya Y., Engel J., Rauch U., Fassler R.
      J. Biol. Chem. 277:26128-26135(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, HETERODIMERIZATION.
    4. "The murine Ten-m/Odz genes show distinct but overlapping expression patterns during development and in adult brain."
      Zhou X.H., Brandau O., Feng K., Oohashi T., Ninomiya Y., Rauch U., Fassler R.
      Gene Expr. Patterns 3:397-405(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    5. Cited for: FUNCTION OF ISOFORM 2 IN CELL PROLIFERATION, TISSUE SPECIFICITY.
    6. "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin resulting in subcellular codistribution and translocation to the nuclear matrix."
      Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D., Chiquet-Ehrismann R.
      Exp. Cell Res. 305:122-132(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD1 AND SORBS1.
    7. "Teneurin carboxy (C)-terminal associated peptide-1 inhibits alkalosis-associated necrotic neuronal death by stimulating superoxide dismutase and catalase activity in immortalized mouse hypothalamic cells."
      Trubiani G., Al Chawaf A., Belsham D.D., Barsyte-Lovejoy D., Lovejoy D.A.
      Brain Res. 1176:27-36(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN CELL SURVIVAL.
    8. "Regulation of neurite growth in immortalized mouse hypothalamic neurons and rat hippocampal primary cultures by teneurin C-terminal-associated peptide-1."
      Al Chawaf A., St Amant K., Belsham D., Lovejoy D.A.
      Neuroscience 144:1241-1254(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN AXON GROWTH.
    9. "Corticotropin-releasing factor (CRF)-induced behaviors are modulated by intravenous administration of teneurin C-terminal associated peptide-1 (TCAP-1)."
      Al Chawaf A., Xu K., Tan L., Vaccarino F.J., Lovejoy D.A., Rotzinger S.
      Peptides 28:1406-1415(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
    10. "Repeated intracerebral teneurin C-terminal associated peptide (TCAP)-1 injections produce enduring changes in behavioral responses to corticotropin-releasing factor (CRF) in rat models of anxiety."
      Tan L.A., Xu K., Vaccarino F.J., Lovejoy D.A., Rotzinger S.
      Behav. Brain Res. 188:195-200(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
    11. "Teneurin C-terminal associated peptide (TCAP)-1 attenuates corticotropin-releasing factor (CRF)-induced c-Fos expression in the limbic system and modulates anxiety behavior in male Wistar rats."
      Tan L.A., Xu K., Vaccarino F.J., Lovejoy D.A., Rotzinger S.
      Behav. Brain Res. 201:198-206(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
    12. "Teneurin C-terminal associated peptide-1 blocks the effects of corticotropin-releasing factor on reinstatement of cocaine seeking and on cocaine-induced behavioural sensitization."
      Kupferschmidt D.A., Lovejoy D.A., Rotzinger S., Erb S.
      Br. J. Pharmacol. 162:574-583(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN STRESS RESPONSE.
    13. "Teneurin C-terminal associated peptide (TCAP)-1 modulates dendritic morphology in hippocampal neurons and decreases anxiety-like behaviors in rats."
      Tan L.A., Al Chawaf A., Vaccarino F.J., Boutros P.C., Lovejoy D.A.
      Physiol. Behav. 104:199-204(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN AXON MORPHOLOGY.
    14. "C-terminal processing of the teneurin proteins: Independent actions of a teneurin C-terminal associated peptide in hippocampal cells."
      Chand D., Casatti C.A., de Lannoy L., Song L., Kollara A., Barsyte-Lovejoy D., Brown T.J., Lovejoy D.A.
      Mol. Cell. Neurosci. 52:38-50(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    15. "C-Terminal region of teneurin-1 co-localizes with dystroglycan and modulates cytoskeletal organization through an extracellular signal-regulated kinase-dependent stathmin- and filamin A-mediated mechanism in hippocampal cells."
      Chand D., Song L., deLannoy L., Barsyte-Lovejoy D., Ackloo S., Boutros P.C., Evans K., Belsham D.D., Lovejoy D.A.
      Neuroscience 219:255-270(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN REORGANIZATION OF CYTOSKELETON, SUBCELLULAR LOCATION (ISOFORM 2).
    16. "Identification of a novel brain derived neurotrophic factor (BDNF)-inhibitory factor: regulation of BDNF by teneurin C-terminal associated peptide (TCAP)-1 in immortalized embryonic mouse hypothalamic cells."
      Ng T., Chand D., Song L., Al Chawaf A., Watson J.D., Boutros P.C., Belsham D.D., Lovejoy D.A.
      Regul. Pept. 174:79-89(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 2 IN BDNF INHIBITION, SUBCELLULAR LOCATION (ISOFORM 2).

    Entry informationi

    Entry nameiTEN1_MOUSE
    AccessioniPrimary (citable) accession number: Q9WTS4
    Secondary accession number(s): Q8CAT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3