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Q9WTS4

- TEN1_MOUSE

UniProt

Q9WTS4 - TEN1_MOUSE

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Protein

Teneurin-1

Gene

Tenm1

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).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
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 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 324324CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei325 – 34521HelicalSequence AnalysisAdd
BLAST
Topological domaini346 – 27312386ExtracellularSequence AnalysisAdd
BLAST

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
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-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

MaxQBiQ9WTS4.
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

BgeeiQ9WTS4.
CleanExiMM_ODZ1.
ExpressionAtlasiQ9WTS4. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119131.
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

        10         20         30         40         50
MEQTDCKPYQ PLSKVKHEMD LAYTSSSDES EDGRKPRQSF NSRETLHEYN
60 70 80 90 100
QELRRNYNSQ SRKRKDVEKS TQEIEFCETP PTLCSGYHTD MHSVSRHGYQ
110 120 130 140 150
LEMGSDVDTE TEGAASPDHA LRMWIRGMKS EHSSCLSSRA NSALSLTDTD
160 170 180 190 200
HERKSDGENG FKFSPVCCDM EAPADSAQDM QSSPHNQFTF RPLPPPPPPP
210 220 230 240 250
HACTCARKPP PTVDSLQRRS MTTRSQPSPA APAPPTSTQD SVHLHNSWVL
260 270 280 290 300
NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF
310 320 330 340 350
SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ
360 370 380 390 400
PVGQIYANGI SNGNPGTESM DTTYSPIGGR VSDKSEKKVF QKGRAIDTGE
410 420 430 440 450
VDIGAQVMQT IPPGLFWRFQ ITIHHPIYLK FNISLAKDSL LGIYGRRNIP
460 470 480 490 500
PTHTQFDFVK LMDGKQLVKQ DSKSSDDIQH SPRNLILTSL QETGFIEYMD
510 520 530 540 550
QGPWYLAFYN DGKKMEQVFV LTTAIEIMDD CSTNCNGNGE CISGHCHCFP
560 570 580 590 600
GFLGPDCARD SCPVLCGGNG EYEKGHCVCR NGWKGPECDV PEEQCIDPTC
610 620 630 640 650
FGHGTCIMGV CICVPGYKGE ICEEEDCLDP MCSSHGICVK GECHCSTGWG
660 670 680 690 700
GVNCETPLPI CQEQCSGHGT FLLDTGVCSC DPKWTGSDCS TELCTMECGS
710 720 730 740 750
HGVCSRGICQ CEEGWVGPTC EERSCHSHCA EHGQCKDGKC ECSPGWEGDH
760 770 780 790 800
CTIAHYLDAV RDGCPGLCFG NGRCTLDQNG WHCVCQVGWS GTGCNIVMEM
810 820 830 840 850
LCGDNLDNDG DGLTDCVDPD CCQQSNCYVS PLCQGSPDPL DLIQQSQPLF
860 870 880 890 900
SQHTSRLFYD RIKFLIGKDS THVVPQDISF DSRRACVIRG QVVAVDGTPL
910 920 930 940 950
VGVNVSFLHH SDYGFTISRQ DGSFDLVAIG GISVVLIFDR SPFLSEKRTL
960 970 980 990 1000
WLPWNQFIVV EKVIMQRIVA DAPSCDISNF ISPNPIVLPS PLTSFGGSCP
1010 1020 1030 1040 1050
ERGTIVPELQ VVQEEIPIPS SFVRLSYLSS RTPGYKTLLR ILLTHSTIPV
1060 1070 1080 1090 1100
GMIKVHLTVS VEGRLTQKWF PAAINLVYTF AWNKTDIYGQ KVWGLAEALV
1110 1120 1130 1140 1150
SVGYEYEMCP EFILWEQRTV VLQGFEMDAS NLGGWSLNKH HIFNPQSGII
1160 1170 1180 1190 1200
HKGNGENMFI SQQPPVIATI MGNGHQRSVA CTNCNGPAHN NKLFAPVALA
1210 1220 1230 1240 1250
SGPDGSVYVG DFNFVRRIFP SGNSVSILEL RNRDTRHSTS PAHKYYLAMD
1260 1270 1280 1290 1300
PMSESLYLSD TNTRKVYKLK SLVETKDLSK NFEVVAGTGD QCLPFDQSHC
1310 1320 1330 1340 1350
GDGGKASEAS LNSPRGITVD RHGFIYFVDG TMIRRIDENA VITTVIGSNG
1360 1370 1380 1390 1400
LTSTQPLSCD SGMDITQVRL EWPTDLAVNP MDNSLYVLDN NIVLQISENR
1410 1420 1430 1440 1450
RVRIIAGRPI HCQVPGIDHF LVSKVAIHST LESARAISVS HSGLLFIAET
1460 1470 1480 1490 1500
DERKVNRIQQ VTTNGEISII AGAPTDCDCK IDPNCDCFSG DGGYAKDAKM
1510 1520 1530 1540 1550
KAPSSLAVSP DGTLYVADLG NVRIRTISKN QAHLNDMNLY EIASPADQEL
1560 1570 1580 1590 1600
YQFTVNGTHL HTMNLITRDY VYNFTYNAEG DLGAITSSNG NSVHIRRDAG
1610 1620 1630 1640 1650
GMPLWLVVPG GQVYWLTISS NGVLKRVSAQ GYNLALMTYP GNTGLLATKS
1660 1670 1680 1690 1700
NENGWTTVYE YDPEGHLTNA TFPTGEVSSF HSDLEKLTKV ALDTSNRENV
1710 1720 1730 1740 1750
LMSTNLTATS TIYILKQENT QSTYRVSPDG SLRVTFASGM EINLSSEPHI
1760 1770 1780 1790 1800
LAGAVNPTLG KCNISLPGEH NANLIEWRQR KEQNKGNVSA FERRLRAHNR
1810 1820 1830 1840 1850
NLLSIDFDHM TRTGKIYDDH RKFTLRILYD QTGRPILWSP VSRYNEVNIT
1860 1870 1880 1890 1900
YSPSGLVTFI QRGTWNEKME YDQSGKIISR TWADGKIWSY TYLEKSVMLL
1910 1920 1930 1940 1950
LHSQRRYIFE YDQSDCLLSV TMPSMVRHSL QTMLSVGYYR NIYTPPDSST
1960 1970 1980 1990 2000
SFIQDYSRDG RLLQTLHLGT GRRVLYKYTK QARLSEILYD TTQVTLTYEE
2010 2020 2030 2040 2050
SSGVIKTIHL MHDGFICTIR YRQTGPLIGR QIFRFSEEGL VNARFDYSYN
2060 2070 2080 2090 2100
NFRVTSMQAV INETPLPIDL YRYVDVSGRT EQFGKFSVIN YDLNQVITTT
2110 2120 2130 2140 2150
VMKHTKIFNA NGQVIEVQYE ILKAIAYWMT IQYDNMGRMV ICDIRVGVDA
2160 2170 2180 2190 2200
NITRYFYEYD ADGQLQTVSV NDKIQWRYSY DLNGNINLLS HGNSARLTPL
2210 2220 2230 2240 2250
RYDLRDRITR LGEIQYKMDE DGFLRQRGND IFEYNSNGLL QKAYNKVSGW
2260 2270 2280 2290 2300
TVQYYYDGLG RRVASKSSLG QHLQFFYADL ANPIRVTHLY NHTSAEITSL
2310 2320 2330 2340 2350
YYDLQGHLIA MELSSGEEYY VACDNMGTPL AVFSSRGQVI KEILYTPYGD
2360 2370 2380 2390 2400
IYHDTYPDFE VIIGFHGGLY DFLTKLVHLG QRDYDVVAGR WTTPNHHIWK
2410 2420 2430 2440 2450
QLNLLPKPFN LYSFENNYPV GKIQDVAKYT TDIGTWLELF GFQLHNVLPG
2460 2470 2480 2490 2500
FPKPELENME LTYELLQLQT KTQEWDPGKM ILGIQCELQK QLRNFISLDQ
2510 2520 2530 2540 2550
LPMTPQYNEG RCLEGGKQPR FAAVPSVFGK GIKFAIKEGI VTADIIGVAN
2560 2570 2580 2590 2600
EDSRRLAAIL NNAHYLENLH FTIEGRDTHY FIKLGSLEED LVLIGNTGGR
2610 2620 2630 2640 2650
RILENGVNVT VSQMTSVLNG RTRRFADIQL QHGALCFNIR YGTTVEEEKN
2660 2670 2680 2690 2700
HVLEMARQRA VAQAWTQEQR RLQEGEEGTR VWTEGEKQQL LGTGRVQGYD
2710 2720 2730
GYFVLSVEQY LELSDSANNI HFMRQSEIGR R
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9WTS4.

Proteomic databases

MaxQBi Q9WTS4.
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 ENSGT00760000119131.
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

Bgeei Q9WTS4.
CleanExi MM_ODZ1.
ExpressionAtlasi Q9WTS4. baseline and differential.
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 ]
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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: October 29, 2014
This is version 96 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