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Q9WTS4

- TEN1_MOUSE

UniProt

Q9WTS4 - TEN1_MOUSE

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Protein
Teneurin-1
Gene
Tenm1, Odz1, Tnm1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer By similarity.10 Publications
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.10 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2601 – 26022Cleavage Inferred

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

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; Single-pass membrane protein
Note: Colocalizes with isoform 2 at the plasma membrane.4 Publications
Isoform 2 : Cytoplasm. Cell membrane. Secreted Inferred
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.4 Publications
Chain Ten-1 intracellular domain : Nucleus By similarity. Nucleus speckle By similarity. Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity 4 Publications
Chain Teneurin C-terminal-associated peptide : Nucleus Inferred. 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.4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 324324Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei325 – 34521Helical; Reviewed prediction
Add
BLAST
Topological domaini346 – 27312386Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular region 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
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27312731Teneurin-1
PRO_0000259499Add
BLAST
Chaini1 – ?Ten-1 intracellular domain By similarityPRO_0000421007
Chaini2602 – 2731130Teneurin C-terminal-associated peptide
PRO_0000421008Add
BLAST

Amino acid modifications

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

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.

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 2.3 Publications

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Contains 8 EGF-like domains.
Contains 5 NHL repeats.
Contains 23 YD repeats.

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.
VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 94 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

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