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Protein

Teneurin-2

Gene

Tenm2

Organism
Rattus norvegicus (Rat)
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. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Mediates axon guidance and homophilic and heterophilic cell-cell adhesion. May function as a cellular signal transducer (By similarity). Acts as a ligand of the ADGRL1 receptor.By similarity1 Publication
Ten-2 intracellular domain: Induces gene transcription inhibition.By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • cell adhesion molecule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Teneurin-2
Short name:
Ten-2
Alternative name(s):
Neurestin
Protein Odd Oz/ten-m homolog 2
Tenascin-M2
Short name:
Ten-m2
Teneurin transmembrane protein 2
Cleaved into the following 2 chains:
Gene namesi
Name:Tenm2
Synonyms:Odz2, Tnm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi727907. Tenm2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 379379CytoplasmicSequence analysisAdd
BLAST
Transmembranei380 – 40021HelicalSequence analysisAdd
BLAST
Topological domaini401 – 27742374ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell junction Source: UniProtKB
  • dendrite Source: UniProtKB
  • dendritic spine Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • filopodium Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • growth cone Source: UniProtKB
  • integral component of plasma membrane Source: InterPro
  • neuron projection Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • PML body Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus, Postsynaptic cell membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27742774Teneurin-2PRO_0000259503Add
BLAST
Chaini1 – ?Ten-2 intracellular domainBy similarityPRO_0000421015
Chaini529 – 27742246Ten-2, soluble formBy similarityPRO_0000421016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei124 – 1241PhosphoserineBy similarity
Modified residuei155 – 1551PhosphothreonineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi576 ↔ 586PROSITE-ProRule annotation
Disulfide bondi580 ↔ 591PROSITE-ProRule annotation
Disulfide bondi593 ↔ 602PROSITE-ProRule annotation
Disulfide bondi611 ↔ 622PROSITE-ProRule annotation
Disulfide bondi624 ↔ 633PROSITE-ProRule annotation
Disulfide bondi640 ↔ 651PROSITE-ProRule annotation
Disulfide bondi645 ↔ 656PROSITE-ProRule annotation
Disulfide bondi658 ↔ 667PROSITE-ProRule annotation
Disulfide bondi672 ↔ 683PROSITE-ProRule annotation
Disulfide bondi677 ↔ 688PROSITE-ProRule annotation
Disulfide bondi690 ↔ 699PROSITE-ProRule annotation
Disulfide bondi710 ↔ 723PROSITE-ProRule annotation
Disulfide bondi725 ↔ 734PROSITE-ProRule annotation
Disulfide bondi739 ↔ 749PROSITE-ProRule annotation
Disulfide bondi743 ↔ 754PROSITE-ProRule annotation
Disulfide bondi756 ↔ 765PROSITE-ProRule annotation
Disulfide bondi770 ↔ 780PROSITE-ProRule annotation
Disulfide bondi774 ↔ 785PROSITE-ProRule annotation
Disulfide bondi787 ↔ 796PROSITE-ProRule annotation
Disulfide bondi810 ↔ 820PROSITE-ProRule annotation
Disulfide bondi814 ↔ 829PROSITE-ProRule annotation
Disulfide bondi831 ↔ 840PROSITE-ProRule annotation
Glycosylationi925 – 9251N-linked (GlcNAc...)Sequence analysis
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence analysis
Glycosylationi1616 – 16161N-linked (GlcNAc...)Sequence analysis
Glycosylationi1712 – 17121N-linked (GlcNAc...)Sequence analysis
Glycosylationi1749 – 17491N-linked (GlcNAc...)Sequence analysis
Glycosylationi1773 – 17731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1807 – 18071N-linked (GlcNAc...)Sequence analysis
Glycosylationi1892 – 18921N-linked (GlcNAc...)Sequence analysis
Glycosylationi1993 – 19931N-linked (GlcNAc...)Sequence analysis
Glycosylationi2197 – 21971N-linked (GlcNAc...)Sequence analysis
Glycosylationi2337 – 23371N-linked (GlcNAc...)Sequence analysis
Glycosylationi2648 – 26481N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Ten-2, soluble form: Derives from the membrane form by proteolytic processing.By similarity
Ten-2 intracellular domain: Derives from the plasma membrane form by proteolytic cleavage and translocates to the nucleus. Homophilic binding of the C-terminal extracellular domain stimulates its proteolytic cleavage and release in the cytoplasmic. Is subjected to rapid degradation by the proteasome pathway (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei528 – 5292CleavageBy similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9R1K2.

PTM databases

iPTMnetiQ9R1K2.
PhosphoSiteiQ9R1K2.
SwissPalmiQ9R1K2.
UniCarbKBiQ9R1K2.

Expressioni

Tissue specificityi

Expressed in the brain (at protein level).1 Publication

Developmental stagei

From E17-E18 embryos, a very strong signal appeared and continued throughout the remaining prenatal days. The signal was strongest in the cerebral cortex (including the cingulate cortex, neocortex, and orbital and insular area), thalamus (anterior and intermediate thalamus), and weak in posterior thalamus and midbrain.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked (Probable). Heterodimer with either TENM1 or TENM3. May also form heterodimer with TENM4 (By similarity). Interacts with ADGRL1 isoform 2.By similarityCurated

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011922.

Structurei

3D structure databases

ProteinModelPortaliQ9R1K2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 375375Teneurin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini575 – 60329EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini605 – 63430EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini636 – 66833EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini669 – 70133EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini702 – 73534EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini738 – 76629EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini769 – 79729EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini808 – 84134EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati1272 – 131645NHL 1Add
BLAST
Repeati1342 – 138645NHL 2Add
BLAST
Repeati1401 – 145252NHL 3Add
BLAST
Repeati1474 – 150128NHL 4Add
BLAST
Repeati1530 – 157344NHL 5Add
BLAST
Repeati1583 – 160220YD 1Add
BLAST
Repeati1619 – 163921YD 2Add
BLAST
Repeati1682 – 170120YD 3Add
BLAST
Repeati1702 – 172423YD 4Add
BLAST
Repeati1895 – 191420YD 5Add
BLAST
Repeati1936 – 195419YD 6Add
BLAST
Repeati1955 – 197521YD 7Add
BLAST
Repeati1982 – 199918YD 8Add
BLAST
Repeati2000 – 202122YD 9Add
BLAST
Repeati2022 – 203918YD 10Add
BLAST
Repeati2042 – 206221YD 11Add
BLAST
Repeati2065 – 208521YD 12Add
BLAST
Repeati2093 – 211321YD 13Add
BLAST
Repeati2119 – 213618YD 14Add
BLAST
Repeati2137 – 216327YD 15Add
BLAST
Repeati2165 – 217814YD 16Add
BLAST
Repeati2179 – 220224YD 17Add
BLAST
Repeati2205 – 222521YD 18Add
BLAST
Repeati2226 – 224621YD 19Add
BLAST
Repeati2248 – 226821YD 20Add
BLAST
Repeati2280 – 230021YD 21Add
BLAST
Repeati2302 – 232221YD 22Add
BLAST
Repeati2348 – 238942YD 23Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi175 – 1784Poly-Ser
Compositional biasi331 – 3344Poly-Ser

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

eggNOGiKOG1225. Eukaryota.
KOG4659. Eukaryota.
ENOG410XQQD. LUCA.
HOGENOMiHOG000231701.
HOVERGENiHBG080306.
InParanoidiQ9R1K2.
PhylomeDBiQ9R1K2.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008969. CarboxyPept-like_regulatory.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR022385. Rhs_assc_core.
IPR027690. Ten2.
IPR009471. Ten_N.
IPR028916. Tox-GHH_dom.
IPR006530. YD.
[Graphical view]
PANTHERiPTHR11219:SF8. PTHR11219:SF8. 2 hits.
PfamiPF12661. hEGF. 1 hit.
PF06484. Ten_N. 1 hit.
PF15636. Tox-GHH. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
TIGRFAMsiTIGR03696. Rhs_assc_core. 1 hit.
TIGR01643. YD_repeat_2x. 1 hit.
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 5 hits.
PS51361. TENEURIN_N. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R1K2-1) [UniParc]FASTAAdd to basket

Also known as: Gamma

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
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD
60 70 80 90 100
HDSRMHYGNR VTDLVHRESD EFSRQGANFT LAELGICEPS PHRSGYCSDM
110 120 130 140 150
GILHQGYSLS TGSDADSDTE GGMSPEHAIR LWGRGIKSRR SSGLSSRENS
160 170 180 190 200
ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL PSAQLPSSHN PPPVSCQMPL
210 220 230 240 250
LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP NHHSQSTLRP
260 270 280 290 300
PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
310 320 330 340 350
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR
360 370 380 390 400
LLPRNTFSRK AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL
410 420 430 440 450
GLNWQLQPAD GHTFNNGVRT GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE
460 470 480 490 500
AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK FNISLGKDAL FGVYIRRGLP
510 520 530 540 550
PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF VQYLDVGLWH
560 570 580 590 600
LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
610 620 630 640 650
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS
660 670 680 690 700
CIDGNCVCAA GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE
710 720 730 740 750
LARVQCPDQC SGHGTYLPDS GLCNCDPNWM GPDCSVEVCS VDCGTHGVCI
760 770 780 790 800
GGACRCEEGW TGAACDQRVC HPRCIEHGTC KDGKCECREG WNGEHCTIGR
810 820 830 840 850
QTAGTETDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD
860 870 880 890 900
NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK
910 920 930 940 950
SFYDRIKLLA GKDSTHIIPG DNPFNSSLVS LIRGQVVTTD GTPLVGVNVS
960 970 980 990 1000
FVKYPKYGYT ITRQDGTFDL IANGGSALTL HFERAPFMSR ERTVWPPWNS
1010 1020 1030 1040 1050
FYAMDTLVMK TEENSIPSCD LSGFVRPDPI IISSPLSTFF SASPAANPIV
1060 1070 1080 1090 1100
PETQVLHEEI ELPGTNVKLR YLSSRTAGYK SLLKITMTQS TVPLNLIRVH
1110 1120 1130 1140 1150
LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS DAVVSVGFEY
1160 1170 1180 1190 1200
ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILLKGTGE
1210 1220 1230 1240 1250
NQFLTQQPAI ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS
1260 1270 1280 1290 1300
LFVGDFNYIR RIFPSRNVTS ILELRNKEFK HSNSPGHKYY LAVDPVTGSL
1310 1320 1330 1340 1350
YVSDTNSRRI YRVKSLSGAK DLAGNSEVVA GTGEQCLPFD EARCGDGGKA
1360 1370 1380 1390 1400
VDATLMSPRG IAVDKNGLMY FVDATMIRKV DQNGIISTLL GSNDLTAVRP
1410 1420 1430 1440 1450
LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI TENHQVSIIA
1460 1470 1480 1490 1500
GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR
1510 1520 1530 1540 1550
LRQVTTNGEI CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA
1560 1570 1580 1590 1600
VAPDGTIYIA DLGNIRIRAV SKNKPVLNAF NQYEAASPGE QELYVFNADG
1610 1620 1630 1640 1650
IHQYTVSLVT GEYLYNFTYS ADNDVTELID NNGNSLKIRR DSSGMPRHLL
1660 1670 1680 1690 1700
MPDNQIITLT VGTNGGLKAV STQNLELGLM TYDGNTGLLA TKSDETGWTT
1710 1720 1730 1740 1750
FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITVDIENSNR DNDVTVITNL
1760 1770 1780 1790 1800
SSVEASYTVV QDQVRNSYQL CSNGTLRVMY ANGMGVSFHS EPHVLAGTLT
1810 1820 1830 1840 1850
PTIGRCNISL PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID
1860 1870 1880 1890 1900
YDRNIRTEKI YDDHRKFTLR IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR
1910 1920 1930 1940 1950
LAGLQRGAMS ERTDIDKQGR IVSRMFADGK VWSYSYLDKS MVLLLQSQRQ
1960 1970 1980 1990 2000
YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI GYIRNIYNPP ESNASVIFDY
2010 2020 2030 2040 2050
SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF GYDETTGVLK
2060 2070 2080 2090 2100
MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI
2110 2120 2130 2140 2150
ASIKPVISET PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL
2160 2170 2180 2190 2200
SKHFDTHGRI KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK
2210 2220 2230 2240 2250
YTYDYDGDGQ LQSVAVNDRP TWRYSYDLNG NLHLLNPGNS ARLMPLRYDL
2260 2270 2280 2290 2300
RDRITRLGDV QYKIDDDGYL CQRGSDIFEY NSKGLLTRAY NKASGWSVQY
2310 2320 2330 2340 2350
RYDGVSRRAS YKTNLGHHLQ YFYSDLHHPT RITHVYNHSN SEITSLYYDL
2360 2370 2380 2390 2400
QGHLFAMESS SGEEYYVASD NTGTPLAVFS INGLMIKQLQ YTAYGEIYYD
2410 2420 2430 2440 2450
SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK
2460 2470 2480 2490 2500
EPAPFNLYMF KNNNPLSNEL DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA
2510 2520 2530 2540 2550
KMYFVPPPYE LSESQASENG QLITGVQQTT ERHNQAFLAL EGQVISKKLH
2560 2570 2580 2590 2600
AGIREKAGHW FATTTPIIGK GIMFAIKEGR VTTGVSSIAS EDSRKVASVL
2610 2620 2630 2640 2650
NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR KVLESGVNVT
2660 2670 2680 2690 2700
VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAR
2710 2720 2730 2740 2750
QRALGTAWAK EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV
2760 2770
EQYPELADSS SNIQFLRQNE MGKR
Length:2,774
Mass (Da):307,474
Last modified:October 31, 2006 - v2
Checksum:i7916D882A6C9E9A1
GO
Isoform 2 (identifier: Q9R1K2-2) [UniParc]FASTAAdd to basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     799-807: Missing.

Note: No experimental confirmation available.
Show »
Length:2,765
Mass (Da):306,572
Checksum:i6748D70D5FFD8F0E
GO
Isoform 3 (identifier: Q9R1K2-3) [UniParc]FASTAAdd to basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     605-669: Missing.

Note: No experimental confirmation available.
Show »
Length:2,709
Mass (Da):300,838
Checksum:iA840B4A997AF1E78
GO
Isoform 4 (identifier: Q9R1K2-4) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     737-807: Missing.

Note: No experimental confirmation available.
Show »
Length:2,703
Mass (Da):299,933
Checksum:iA79358CF93743204
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei605 – 66965Missing in isoform 3. 1 PublicationVSP_021395Add
BLAST
Alternative sequencei737 – 80771Missing in isoform 4. 1 PublicationVSP_021397Add
BLAST
Alternative sequencei799 – 8079Missing in isoform 2. 1 PublicationVSP_021396

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086607 mRNA. Translation: AAD47383.1.
AF086608 mRNA. Translation: AAD47384.1.
AF086609 mRNA. Translation: AAD47385.1.
AF086610 mRNA. Translation: AAD47386.1.
RefSeqiNP_064473.1. NM_020088.1. [Q9R1K2-2]
UniGeneiRn.229571.

Genome annotation databases

GeneIDi117242.
KEGGirno:117242.
UCSCiRGD:727907. rat. [Q9R1K2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086607 mRNA. Translation: AAD47383.1.
AF086608 mRNA. Translation: AAD47384.1.
AF086609 mRNA. Translation: AAD47385.1.
AF086610 mRNA. Translation: AAD47386.1.
RefSeqiNP_064473.1. NM_020088.1. [Q9R1K2-2]
UniGeneiRn.229571.

3D structure databases

ProteinModelPortaliQ9R1K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011922.

PTM databases

iPTMnetiQ9R1K2.
PhosphoSiteiQ9R1K2.
SwissPalmiQ9R1K2.
UniCarbKBiQ9R1K2.

Proteomic databases

PaxDbiQ9R1K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117242.
KEGGirno:117242.
UCSCiRGD:727907. rat. [Q9R1K2-1]

Organism-specific databases

CTDi57451.
RGDi727907. Tenm2.

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG4659. Eukaryota.
ENOG410XQQD. LUCA.
HOGENOMiHOG000231701.
HOVERGENiHBG080306.
InParanoidiQ9R1K2.
PhylomeDBiQ9R1K2.

Miscellaneous databases

PROiQ9R1K2.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR008969. CarboxyPept-like_regulatory.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR022385. Rhs_assc_core.
IPR027690. Ten2.
IPR009471. Ten_N.
IPR028916. Tox-GHH_dom.
IPR006530. YD.
[Graphical view]
PANTHERiPTHR11219:SF8. PTHR11219:SF8. 2 hits.
PfamiPF12661. hEGF. 1 hit.
PF06484. Ten_N. 1 hit.
PF15636. Tox-GHH. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
TIGRFAMsiTIGR03696. Rhs_assc_core. 1 hit.
TIGR01643. YD_repeat_2x. 1 hit.
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 5 hits.
PS51361. TENEURIN_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Neurestin: putative transmembrane molecule implicated in neuronal development."
    Otaki J.M., Firestein S.
    Dev. Biol. 212:165-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 1), DEVELOPMENTAL STAGE.
    Strain: Sprague-Dawley.
    Tissue: Olfactory bulb.
  2. "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities."
    Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G., Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S., Tonevitsky A.G., Dell A., Volynski K.E., Ushkaryov Y.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS ADGRL1 LIGAND, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTEN2_RAT
AccessioniPrimary (citable) accession number: Q9R1K2
Secondary accession number(s): Q9R1J9, Q9R1K0, Q9R1K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 8, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.