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Protein

Teneurin-m

Gene

Ten-m

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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. Acts as a homophilic and heterophilic synaptic cell adhesion molecule that drives synapse assembly. Promotes bi-directional trans-synaptic signaling with Ten-a to organize neuromuscular synapses. Functions in olfactory synaptic partner matching by promoting homophilic cell adhesion between pre-synaptic olfactory receptor neurons (ORN) axons and post-synaptic projection neurons (PN) dendrites partner in the developing antennal lobe to form stable connections. Also required for peripheral axon growth cone guidance and target recognition of motor neurons.4 Publications

GO - Molecular functioni

  • filamin binding Source: FlyBase
  • identical protein binding Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: FlyBase
  • chaeta development Source: FlyBase
  • compound eye corneal lens development Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • compound eye photoreceptor development Source: FlyBase
  • cytoplasmic microtubule organization Source: UniProtKB
  • maintenance of presynaptic active zone structure Source: UniProtKB
  • motor neuron axon guidance Source: FlyBase
  • neuromuscular synaptic transmission Source: UniProtKB
  • positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
  • positive regulation of locomotion Source: UniProtKB
  • postsynaptic membrane organization Source: UniProtKB
  • presynaptic membrane organization Source: UniProtKB
  • R7 cell development Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of homotypic cell-cell adhesion Source: UniProtKB
  • regulation of terminal button organization Source: UniProtKB
  • sensory perception of pain Source: FlyBase
  • synapse organization Source: UniProtKB
  • synaptic growth at neuromuscular junction Source: FlyBase
  • synaptic target attraction Source: FlyBase
  • synaptic target recognition Source: UniProtKB
  • synaptic vesicle membrane organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Teneurin-m
Short name:
Tenm
Alternative name(s):
Odd Oz protein
Tenascin-like protein
Gene namesi
Name:Ten-m
Synonyms:odz
ORF Names:CG5723
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004449. Ten-m.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 229229CytoplasmicSequence analysisAdd
BLAST
Transmembranei230 – 25021HelicalSequence analysisAdd
BLAST
Topological domaini251 – 27312481ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: FlyBase
  • neuromuscular junction Source: FlyBase
  • neuronal cell body Source: UniProtKB
  • neuron projection Source: UniProtKB-SubCell
  • plasma membrane Source: FlyBase
  • postsynaptic membrane Source: UniProtKB
  • proteinaceous extracellular matrix Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Shows peripheral motor neuron axon guidance defects.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27312731Teneurin-mPRO_0000421021Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi540 ↔ 549PROSITE-ProRule annotation
Disulfide bondi545 ↔ 560PROSITE-ProRule annotation
Disulfide bondi562 ↔ 571PROSITE-ProRule annotation
Disulfide bondi578 ↔ 589PROSITE-ProRule annotation
Disulfide bondi583 ↔ 594PROSITE-ProRule annotation
Disulfide bondi596 ↔ 605PROSITE-ProRule annotation
Disulfide bondi651 ↔ 664PROSITE-ProRule annotation
Disulfide bondi666 ↔ 675PROSITE-ProRule annotation
Disulfide bondi742 ↔ 752PROSITE-ProRule annotation
Disulfide bondi746 ↔ 762PROSITE-ProRule annotation
Disulfide bondi764 ↔ 773PROSITE-ProRule annotation
Glycosylationi857 – 8571N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation occurs at tyrosine residues.1 Publication
Proteolytically cleaved.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO61307.

Expressioni

Tissue specificityi

Expressed in muscles and motor neurons (at protein level).1 Publication

Developmental stagei

Expressed in the central nervous system and heart. Expressed in the developing antennal lobe. Expressed in subset of matching olfactory receptor neurons (ORN) and projection neurons (PN) in select glomeruli between 12 to 48 hours after puparium formation (apf) (at protein level). Expressed in odd-numbered blastoderm parasegments, the central nervous system, muscle attachment points and tracheal precursor cells. Expressed in the ventral nerve cord, the cardiac mesoderm and epidermis at late embryonic stages. Expressed in all imaginal disks.4 Publications

Gene expression databases

BgeeiO61307.
ExpressionAtlasiO61307. differential.
GenevisibleiO61307. DM.

Interactioni

Subunit structurei

Homodimer. Heterodimer with Ten-a. Interacts with Ten-a; the interaction occurs at the neuromuscular junction. Interacts with alpha-Spec and cher.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cherQ9VEN14EBI-118556,EBI-133626

GO - Molecular functioni

  • filamin binding Source: FlyBase
  • identical protein binding Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi65699. 4 interactions.
IntActiO61307. 705 interactions.
MINTiMINT-804522.
STRINGi7227.FBpp0303192.

Structurei

3D structure databases

ProteinModelPortaliO61307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini536 – 57237EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini574 – 60633EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini643 – 67634EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini738 – 77437EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati1160 – 120142NHL 1Add
BLAST
Repeati1202 – 124645NHL 2Add
BLAST
Repeati1391 – 143444NHL 3Add
BLAST
Repeati1459 – 150244NHL 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi317 – 36852Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the tenascin family. Teneurin subfamily.Curated
Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 4 NHL repeats.Curated

Keywords - Domaini

EGF-like domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG4659. Eukaryota.
ENOG410XQQD. LUCA.
GeneTreeiENSGT00760000119131.
InParanoidiO61307.
OrthoDBiEOG74TWXP.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008969. CarboxyPept-like_regulatory.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR031325. RHS_repeat.
IPR028916. Tox-GHH_dom.
IPR006530. YD.
[Graphical view]
PfamiPF05593. RHS_repeat. 1 hit.
PF15636. Tox-GHH. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
TIGRFAMsiTIGR01643. YD_repeat_2x. 1 hit.
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: O61307-1) [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
MNPYEYESTL DCRDVGGGPT PAHAHPHAQG RTLPMSGHGR PTTDLGPVHG
60 70 80 90 100
SQTLQHQNQQ NLQAAQAAAQ SSHYDYEYQH LAHRPPDTAN NTAQRTHGRQ
110 120 130 140 150
GFLLEGVTPT APPDVPPRNP TMSRMQNGRL TVNNPNDADF EPSCLVRTPS
160 170 180 190 200
GNVYIPSGNL NINKGSPIDF KSGSACSTPT KDTLKGYERS TQGCMGPVLP
210 220 230 240 250
QRSVMNGLPA HHYSAPMNFR KDLVARCSSP WFGIGSISVL FAFVVMLILL
260 270 280 290 300
TTTGVIKWNQ SPPCSVLVGN EASEVTAAKS TNTDLSKLHN SSVRAKNGQG
310 320 330 340 350
IGLAQGQSGL GAAGVGSGGG SSAATVTTAT SNSGTAQGLQ STSASAEATS
360 370 380 390 400
SAATSSSQSS LTPSLSSSLA NANNGGARTF PARSFPPDGT TFGQITLGQK
410 420 430 440 450
LTKEIQPYSY WNMQFYQSEP AYVKFDYTIP RGASIGVYGR RNALPTHTQY
460 470 480 490 500
HFKEVLSGFS ASTRTARAAH LSITREVTRY MEPGHWFVSL YNDDGDVQEL
510 520 530 540 550
TFYAAVAEDM TQNCPNGCSG NGQCLLGHCQ CNPGFGGDDC SESVCPVLCS
560 570 580 590 600
QHGEYTNGEC ICNPGWKGKE CSLRHDECEV ADCSGHGHCV SGKCQCMRGY
610 620 630 640 650
KGKFCEEVDC PHPNCSGHGF CADGTCICKK GWKGPDCATM DQDALQCLPD
660 670 680 690 700
CSGHGTFDLD TQTCTCEAKW SGDDCSKELC DLDCGQHGRC EGDACACDPE
710 720 730 740 750
WGGEYCNTRL CDVRCNEHGQ CKNGTCLCVT GWNGKHCTIE GCPNSCAGHG
760 770 780 790 800
QCRVSGEGQW ECRCYEGWDG PDCGIALELN CGDSKDNDKD GLVDCEDPEC
810 820 830 840 850
CASHVCKTSQ LCVSAPKPID VLLRKQPPAI TASFFERMKF LIDESSLQNY
860 870 880 890 900
AKLETFNESR SAVIRGRVVT SLGMGLVGVR VSTTTLLEGF TLTRDDGWFD
910 920 930 940 950
LMVNGGGAVT LQFGRAPFRP QSRIVQVPWN EVVIIDLVVM SMSEEKGLAV
960 970 980 990 1000
TTTHTCFAHD YDLMKPVVLA SWKHGFQGAC PDRSAILAES QVIQESLQIP
1010 1020 1030 1040 1050
GTGLNLVYHS SRAAGYLSTI KLQLTPDVIP TSLHLIHLRI TIEGILFERI
1060 1070 1080 1090 1100
FEADPGIKFT YAWNRLNIYR QRVYGVTTAV VKVGYQYTDC TDIVWDIQTT
1110 1120 1130 1140 1150
KLSGHDMSIS EVGGWNLDIH HRYNFHEGIL QKGDGSNIYL RNKPRIILTT
1160 1170 1180 1190 1200
MGDGHQRPLE CPDCDGQATK QRLLAPVALA AAPDGSLFVG DFNYIRRIMT
1210 1220 1230 1240 1250
DGSIRTVVKL NATRVSYRYH MALSPLDGTL YVSDPESHQI IRVRDTNDYS
1260 1270 1280 1290 1300
QPELNWEAVV GSGERCLPGD EAHCGDGALA KDAKLAYPKG IAISSDNILY
1310 1320 1330 1340 1350
FADGTNIRMV DRDGIVSTLI GNHMHKSHWK PIPCEGTLKL EEMHLRWPTE
1360 1370 1380 1390 1400
LAVSPMDNTL HIIDDHMILR MTPDGRVRVI SGRPLHCATA STAYDTDLAT
1410 1420 1430 1440 1450
HATLVMPQSI AFGPLGELYV AESDSQRINR VRVIGTDGRI APFAGAESKC
1460 1470 1480 1490 1500
NCLERGCDCF EAEHYLATSA KFNTIAALAV TPDSHVHIAD QANYRIRSVM
1510 1520 1530 1540 1550
SSIPEASPSR EYEIYAPDMQ EIYIFNRFGQ HVSTRNILTG ETTYVFTYNV
1560 1570 1580 1590 1600
NTSNGKLSTV TDAAGNKVFL LRDYTSQVNS IENTKGQKCR LRMTRMKMLH
1610 1620 1630 1640 1650
ELSTPDNYNV TYEYHGPTGL LRTKLDSTGR SYVYNYDEFG RLTSAVTPTG
1660 1670 1680 1690 1700
RVIELSFDLS VKGAQVKVSE NAQKEMSLLI QGATVIVRNG AAESRTTVDM
1710 1720 1730 1740 1750
DGSTTSITPW GHNLQMEVAP YTILAEQSPL LGESYPVPAK QRTEIAGDLA
1760 1770 1780 1790 1800
NRFEWRYFVR RQQPLQAGKQ SKGPPRPVTE VGRKLRVNGD NVLTLEYDRE
1810 1820 1830 1840 1850
TQSVVVMVDD KQELLNVTYD RTSRPISFRP QSGDYADVDL EYDRFGRLVS
1860 1870 1880 1890 1900
WKWGVLQEAY SFDRNGRLNE IKYGDGSTMV YAFKDMFGSL PLKVTTPRRS
1910 1920 1930 1940 1950
DYLLQYDDAG ALQSLTTPRG HIHAFSLQTS LGFFKYQYYS PINRHPFEIL
1960 1970 1980 1990 2000
YNDEGQILAK IHPHQSGKVA FVHDTAGRLE TILAGLSSTH YTYQDTTSLV
2010 2020 2030 2040 2050
KSVEVQEPGF ELRREFKYHA GILKDEKLRF GSKNSLASAR YKYAYDGNAR
2060 2070 2080 2090 2100
LSGIEMAIDD KELPTTRYKY SQNLGQLEVV QDLKITRNAF NRTVIQDSAK
2110 2120 2130 2140 2150
QFFAIVDYDQ HGRVKSVLMN VKNIDVFRLE LDYDLRNRIK SQKTTFGRST
2160 2170 2180 2190 2200
AFDKINYNAD GHVVEVLGTN NWKYLFDENG NTVGVVDQGE KFNLGYDIGD
2210 2220 2230 2240 2250
RVIKVGDVEF NNYDARGFVV KRGEQKYRYN NRGQLIHSFE RERFQSWYYY
2260 2270 2280 2290 2300
DDRSRLVAWH DNKGNTTQYY YANPRTPHLV THVHFPKISR TMKLFYDDRD
2310 2320 2330 2340 2350
MLIALEHEDQ RYYVATDQNG SPLAFFDQNG SIVKEMKRTP FGRIIKDTKP
2360 2370 2380 2390 2400
EFFVPIDFHG GLIDPHTKLV YTEQRQYDPH VGQWMTPLWE TLATEMSHPT
2410 2420 2430 2440 2450
DVFIYRYHNN DPINPNKPQN YMIDLDSWLQ LFGYDLNNMQ SSRYTKLAQY
2460 2470 2480 2490 2500
TPQASIKSNT LAPDFGVISG LECIVEKTSE KFSDFDFVPK PLLKMEPKMR
2510 2520 2530 2540 2550
NLLPRVSYRR GVFGEGVLLS RIGGRALVSV VDGSNSVVQD VVSSVFNNSY
2560 2570 2580 2590 2600
FLDLHFSIHD QDVFYFVKDN VLKLRDDNEE LRRLGGMFNI STHEISDHGG
2610 2620 2630 2640 2650
SAAKELRLHG PDAVVIIKYG VDPEQERHRI LKHAHKRAVE RAWELEKQLV
2660 2670 2680 2690 2700
AAGFQGRGDW TEEEKEELVQ HGDVDGWNGI DIHSIHKYPQ LADDPGNVAF
2710 2720 2730
QRDAKRKRRK TGSSHRSASN RRQLKFGELS A
Length:2,731
Mass (Da):304,056
Last modified:February 6, 2013 - v2
Checksum:i6718B77B8F62D482
GO
Isoform D (identifier: O61307-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-375: G → GGRAMSTRLS...PDVMPVLILE
     858-858: E → ESIFWNYFNA

Note: No experimental confirmation available.
Show »
Length:3,297
Mass (Da):366,082
Checksum:iBD302737C911F209
GO

Sequence cautioni

The sequence CAA51678.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → G in AAB88281 (PubMed:9373139).Curated
Sequence conflicti22 – 221A → G in AAC05080 (PubMed:9373139).Curated
Sequence conflicti37 – 371G → S in AAB88281 (PubMed:9373139).Curated
Sequence conflicti37 – 371G → S in AAC05080 (PubMed:9373139).Curated
Sequence conflicti65 – 651A → V in AAB88281 (PubMed:9373139).Curated
Sequence conflicti89 – 891A → V in AAB88281 (PubMed:9373139).Curated
Sequence conflicti1837 – 18371D → Y in CAA51678 (PubMed:8070401).Curated
Sequence conflicti2099 – 20991A → G in AAB88281 (PubMed:9373139).Curated
Sequence conflicti2099 – 20991A → G in AAC05080 (PubMed:9373139).Curated
Sequence conflicti2315 – 23151A → T in AAB88281 (PubMed:9373139).Curated
Sequence conflicti2495 – 24951M → T in CAA51678 (PubMed:8070401).Curated
Sequence conflicti2710 – 27101K → R in AAB88281 (PubMed:9373139).Curated
Sequence conflicti2710 – 27101K → R in AAC05080 (PubMed:9373139).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei375 – 3751G → GGRAMSTRLSVRGAGERGRR HRRSLNEEQGEDDVATDGTF SDLITNESLNQQAAEKYLAT TLAKSPTDVHGSGNKTLPRM DGVYGTQRSEDTPDTSYDYV YEDEVEPETTPSLIRRTKTG QQFGKSLNSNLRSAAKTLVN KRRKYDHGTVEAEHIKHEEE EEEDEQKLERHEAIGMATEL TTESETSTLPAVIDDDNQSD NSSSGPTPETTVRSDTDDIV EINTPPSQTAQRTFAAVSHQ PAIEHDFQIKGTDAGGLQTE KPATDDINNERDLADNYEVD SKEPTSPGTPPQGKVSQQTG KASLQSLQSESDLMMNDASH YEDIDIVKLDGLTISHEEEI YKTADKENMAPKNQPSQHID RSQNEVLKGHQQGDEKQPQL EPLKPYVSERVDLPGKRIFL NLTIATDEGSDSVYTLHVEV PTGGGPHFIKEVLTHEKPTA QADSCVPEPPPRMPDCPCSC LPPPAPIYLDDTVDIDSAPP AKTVTTSTISAPINPFHSEE EDDEDGVRDEEQTPSSSTAT NLPSTEIDNHIAAFTEPAVG AGGVPFACPDVMPVLILE in isoform D. CuratedVSP_054459
Alternative sequencei858 – 8581E → ESIFWNYFNA in isoform D. CuratedVSP_054460

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73154 mRNA. Translation: CAA51678.1. Different initiation.
AF008227, AF008224, AF008226 Genomic DNA. Translation: AAC05080.1.
AF008228 mRNA. Translation: AAB88281.1.
AE014296 Genomic DNA. Translation: AAF51824.2.
AE014296 Genomic DNA. Translation: ABW08579.2.
RefSeqiNP_001097661.2. NM_001104191.3. [O61307-2]
NP_524215.2. NM_079491.3. [O61307-1]
UniGeneiDm.2499.

Genome annotation databases

EnsemblMetazoaiFBtr0078509; FBpp0078161; FBgn0004449. [O61307-1]
GeneIDi40464.
KEGGidme:Dmel_CG5723.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73154 mRNA. Translation: CAA51678.1. Different initiation.
AF008227, AF008224, AF008226 Genomic DNA. Translation: AAC05080.1.
AF008228 mRNA. Translation: AAB88281.1.
AE014296 Genomic DNA. Translation: AAF51824.2.
AE014296 Genomic DNA. Translation: ABW08579.2.
RefSeqiNP_001097661.2. NM_001104191.3. [O61307-2]
NP_524215.2. NM_079491.3. [O61307-1]
UniGeneiDm.2499.

3D structure databases

ProteinModelPortaliO61307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65699. 4 interactions.
IntActiO61307. 705 interactions.
MINTiMINT-804522.
STRINGi7227.FBpp0303192.

Proteomic databases

PaxDbiO61307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078509; FBpp0078161; FBgn0004449. [O61307-1]
GeneIDi40464.
KEGGidme:Dmel_CG5723.

Organism-specific databases

CTDi40464.
FlyBaseiFBgn0004449. Ten-m.

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG4659. Eukaryota.
ENOG410XQQD. LUCA.
GeneTreeiENSGT00760000119131.
InParanoidiO61307.
OrthoDBiEOG74TWXP.

Miscellaneous databases

ChiTaRSiTen-m. fly.
GenomeRNAii40464.
NextBioi818903.
PROiO61307.

Gene expression databases

BgeeiO61307.
ExpressionAtlasiO61307. differential.
GenevisibleiO61307. DM.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008969. CarboxyPept-like_regulatory.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR031325. RHS_repeat.
IPR028916. Tox-GHH_dom.
IPR006530. YD.
[Graphical view]
PfamiPF05593. RHS_repeat. 1 hit.
PF15636. Tox-GHH. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
TIGRFAMsiTIGR01643. YD_repeat_2x. 1 hit.
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tenm, a Drosophila gene related to tenascin, is a new pair-rule gene."
    Baumgartner S., Martin D., Hagios C., Chiquet-Ehrismann R.
    EMBO J. 13:3728-3740(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), DEVELOPMENTAL STAGE.
    Strain: Canton-S.
  2. "The genetics and molecular structure of the Drosophila pair-rule gene odd Oz (odz)."
    Levine A., Gartenberg D., Yakov R., Lieberman Y., Budai-Hadrian O., Bashan-Ahrend A., Wides R.
    Gene 200:59-74(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B), DEVELOPMENTAL STAGE.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION.
  6. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-857, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.
  7. "Drosophila Ten-m and filamin affect motor neuron growth cone guidance."
    Zheng L., Michelson Y., Freger V., Avraham Z., Venken K.J., Bellen H.J., Justice M.J., Wides R.
    PLoS ONE 6:E22956-E22956(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHER, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  8. "Teneurins instruct synaptic partner matching in an olfactory map."
    Hong W., Mosca T.J., Luo L.
    Nature 484:201-207(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPSE FORMATION, HOMODIMERIZATION, HETERODIMERIZATION, INTERACTION WITH TEN-A, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  9. "Trans-synaptic Teneurin signalling in neuromuscular synapse organization and target choice."
    Mosca T.J., Hong W., Dani V.S., Favaloro V., Luo L.
    Nature 484:237-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROMUSCULAR SYNAPSE FORMATION, INTERACTION WITH ALPHA-SPEC AND TEN-A, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTENM_DROME
AccessioniPrimary (citable) accession number: O61307
Secondary accession number(s): A8JNW8
, O18366, Q24551, Q9TX59, Q9VNU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: February 6, 2013
Last modified: May 11, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The name odz (odd Oz) reflects the odd pair rule nature of the gene and Oz reflects the prominent expression of the gene in the brain, heart and neurons, corresponding to the three gifts that the Wizard of Oz bestowed.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.