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Teneurin-2 (Ten-2) (Protein Odd Oz/ten-m homolog 2) (Tenascin-M2) (Ten-m2) (Teneurin transmembrane protein 2) [Cleaved into: Ten-2, soluble form; Ten-2 intracellular domain (Ten-2 ICD)]

 TEN2_MOUSE              Reviewed;        2764 AA.
Q9WTS5; Q5NBW7; Q5NBW8; Q80TJ0; Q9JLC0; Q9QYZ1;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 126.
RecName: Full=Teneurin-2;
Short=Ten-2;
AltName: Full=Protein Odd Oz/ten-m homolog 2;
AltName: Full=Tenascin-M2;
Short=Ten-m2;
AltName: Full=Teneurin transmembrane protein 2;
Contains:
RecName: Full=Ten-2, soluble form;
Contains:
RecName: Full=Ten-2 intracellular domain;
Short=Ten-2 ICD;
Name=Tenm2; Synonyms=Kiaa1127, Odz2, Tnm2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10225957; DOI=10.1083/jcb.145.3.563;
Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
"Mouse ten-m/Odz is a new family of dimeric type II transmembrane
proteins expressed in many tissues.";
J. Cell Biol. 145:563-577(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 572-799.
PubMed=10588872; DOI=10.1006/dbio.1999.9503;
Rubin B.P., Tucker R.P., Martin D., Chiquet-Ehrismann R.;
"Teneurins: a novel family of neuronal cell surface proteins in
vertebrates, homologous to the Drosophila pair-rule gene product Ten-
m.";
Dev. Biol. 216:195-209(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1835-2764.
PubMed=10625539; DOI=10.1006/dbio.1999.9532;
Ben-Zur T., Feige E., Motro B., Wides R.;
"The mammalian Odz gene family: homologs of a Drosophila pair-rule
gene with expression implying distinct yet overlapping developmental
roles.";
Dev. Biol. 217:107-120(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2512-2764.
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[6]
HOMODIMERIZATION, AND HETERODIMERIZATION.
PubMed=12000766; DOI=10.1074/jbc.M203722200;
Feng K., Zhou X.H., Oohashi T., Morgelin M., Lustig A., Hirakawa S.,
Ninomiya Y., Engel J., Rauch U., Fassler R.;
"All four members of the Ten-m/Odz family of transmembrane proteins
form dimers.";
J. Biol. Chem. 277:26128-26135(2002).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12915301; DOI=10.1016/S1567-133X(03)00087-5;
Zhou X.H., Brandau O., Feng K., Oohashi T., Ninomiya Y., Rauch U.,
Fassler R.;
"The murine Ten-m/Odz genes show distinct but overlapping expression
patterns during development and in adult brain.";
Gene Expr. Patterns 3:397-405(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Involved in neural development, regulating the
establishment of proper connectivity within the nervous system.
Acts as a ligand of the ADGRL1 receptor. 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).
{ECO:0000250}.
-!- FUNCTION: Ten-2 intracellular domain: Induces gene transcription
inhibition. {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either
TENM1 or TENM3. May also form heterodimer with TENM4.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum
{ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction,
synapse {ECO:0000250}. Cell projection, dendritic spine
{ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell
projection, growth cone {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250}; Single-pass membrane
protein {ECO:0000250}. Cell junction, synapse, synaptosome
{ECO:0000250}. Note=Colocalizes with ADGRL1 across intercellular
junctions. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Ten-2 intracellular domain: Nucleus, PML
body {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the cortex, CA1, CA2, CA3,
dentate gyrus and granular layer of the hippocampus. Expressed in
the Purkinje cells and molecular layer of the cerebellum.
{ECO:0000269|PubMed:12915301}.
-!- DEVELOPMENTAL STAGE: Expressed in the midbrain and spinal cord at
12.5 dpc. {ECO:0000269|PubMed:12915301}.
-!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
cysteines might enable the formation of intermolecular disulfide
bonds.
-!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
domains for intracellular SH3-containing proteins.
-!- PTM: Ten-2, soluble form: Derives from the membrane form by
proteolytic processing. {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
{ECO:0000305}.
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EMBL; AB025411; BAA77397.1; -; mRNA.
EMBL; AL713956; CAI35933.1; -; Genomic_DNA.
EMBL; AL645912; CAI35933.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35933.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35933.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35933.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35933.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35934.1; -; Genomic_DNA.
EMBL; AL645912; CAI35934.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35934.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35934.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35934.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35934.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI36037.1; -; Genomic_DNA.
EMBL; AL645912; CAI36037.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI36037.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI36037.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI36037.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI36037.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI36038.1; -; Genomic_DNA.
EMBL; AL645912; CAI36038.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI36038.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI36038.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI36038.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI36038.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35941.1; -; Genomic_DNA.
EMBL; AL645912; CAI35941.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35941.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35941.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35941.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35941.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35942.1; -; Genomic_DNA.
EMBL; AL645912; CAI35942.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35942.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35942.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35942.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35942.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35944.1; -; Genomic_DNA.
EMBL; AL645912; CAI35944.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35944.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35944.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35944.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35944.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35945.1; -; Genomic_DNA.
EMBL; BX539311; CAI35945.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35945.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35945.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35945.1; JOINED; Genomic_DNA.
EMBL; AL645912; CAI35945.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35946.1; -; Genomic_DNA.
EMBL; AL645912; CAI35946.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35946.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35946.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35946.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35946.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35947.1; -; Genomic_DNA.
EMBL; AL645912; CAI35947.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35947.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35947.1; JOINED; Genomic_DNA.
EMBL; AL713915; CAI35947.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35947.1; JOINED; Genomic_DNA.
EMBL; AL645912; CAI35083.1; -; Genomic_DNA.
EMBL; AL713915; CAI35083.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35083.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35083.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35083.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35083.1; JOINED; Genomic_DNA.
EMBL; AL645912; CAI35084.1; -; Genomic_DNA.
EMBL; AL713915; CAI35084.1; JOINED; Genomic_DNA.
EMBL; AL713919; CAI35084.1; JOINED; Genomic_DNA.
EMBL; AL713956; CAI35084.1; JOINED; Genomic_DNA.
EMBL; BX000433; CAI35084.1; JOINED; Genomic_DNA.
EMBL; BX539311; CAI35084.1; JOINED; Genomic_DNA.
EMBL; AJ245710; CAB57282.1; -; mRNA.
EMBL; AF195419; AAF28317.1; -; mRNA.
EMBL; AK122455; BAC65737.1; -; mRNA.
CCDS; CCDS24546.1; -.
UniGene; Mm.439889; -.
UniGene; Mm.445432; -.
ProteinModelPortal; Q9WTS5; -.
SMR; Q9WTS5; -.
IntAct; Q9WTS5; 1.
STRING; 10090.ENSMUSP00000099865; -.
iPTMnet; Q9WTS5; -.
PhosphoSitePlus; Q9WTS5; -.
EPD; Q9WTS5; -.
MaxQB; Q9WTS5; -.
PaxDb; Q9WTS5; -.
PRIDE; Q9WTS5; -.
MGI; MGI:1345184; Tenm2.
eggNOG; KOG1225; Eukaryota.
eggNOG; KOG4659; Eukaryota.
eggNOG; ENOG410XQQD; LUCA.
HOGENOM; HOG000231701; -.
HOVERGEN; HBG080306; -.
InParanoid; Q9WTS5; -.
PhylomeDB; Q9WTS5; -.
TreeFam; TF316833; -.
PRO; PR:Q9WTS5; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ODZ2; -.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0097264; P:self proteolysis; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR022385; Rhs_assc_core.
InterPro; IPR027689; Ten-2/3.
InterPro; IPR009471; Ten_N.
InterPro; IPR028916; Tox-GHH_dom.
InterPro; IPR006530; YD.
PANTHER; PTHR11219:SF64; PTHR11219:SF64; 2.
Pfam; PF06484; Ten_N; 1.
Pfam; PF15636; Tox-GHH; 1.
SMART; SM00181; EGF; 8.
SUPFAM; SSF49464; SSF49464; 1.
TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
TIGRFAMs; TIGR01643; YD_repeat_2x; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS51361; TENEURIN_N; 1.
1: Evidence at protein level;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
EGF-like domain; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Repressor; Synapse; Synaptosome;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix.
CHAIN 1 2764 Teneurin-2.
/FTId=PRO_0000259502.
CHAIN 1 ? Ten-2 intracellular domain.
{ECO:0000250}.
/FTId=PRO_0000421013.
CHAIN 529 2764 Ten-2, soluble form. {ECO:0000250}.
/FTId=PRO_0000421014.
TOPO_DOM 1 379 Cytoplasmic. {ECO:0000255}.
TRANSMEM 380 400 Helical. {ECO:0000255}.
TOPO_DOM 401 2764 Extracellular. {ECO:0000255}.
DOMAIN 1 375 Teneurin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00694}.
DOMAIN 575 603 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 598 634 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 636 668 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 669 701 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 702 735 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 737 765 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 768 796 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 798 831 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1262 1306 NHL 1.
REPEAT 1332 1376 NHL 2.
REPEAT 1391 1442 NHL 3.
REPEAT 1464 1491 NHL 4.
REPEAT 1520 1563 NHL 5.
REPEAT 1573 1592 YD 1.
REPEAT 1609 1629 YD 2.
REPEAT 1672 1691 YD 3.
REPEAT 1692 1714 YD 4.
REPEAT 1885 1904 YD 5.
REPEAT 1926 1944 YD 6.
REPEAT 1945 1965 YD 7.
REPEAT 1972 1989 YD 8.
REPEAT 1990 2011 YD 9.
REPEAT 2012 2029 YD 10.
REPEAT 2032 2052 YD 11.
REPEAT 2055 2075 YD 12.
REPEAT 2083 2103 YD 13.
REPEAT 2109 2126 YD 14.
REPEAT 2127 2153 YD 15.
REPEAT 2155 2168 YD 16.
REPEAT 2169 2192 YD 17.
REPEAT 2195 2215 YD 18.
REPEAT 2216 2236 YD 19.
REPEAT 2238 2258 YD 20.
REPEAT 2270 2290 YD 21.
REPEAT 2292 2312 YD 22.
REPEAT 2338 2379 YD 23.
COMPBIAS 175 178 Poly-Ser.
COMPBIAS 331 334 Poly-Ser.
SITE 528 529 Cleavage. {ECO:0000250}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHK6}.
MOD_RES 155 155 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R1K2}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R1K2}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 915 915 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 938 938 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1257 1257 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1606 1606 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1702 1702 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1739 1739 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1763 1763 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1797 1797 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1882 1882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1983 1983 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2187 2187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2327 2327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2638 2638 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 576 586 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 580 591 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 593 602 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 611 622 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 624 633 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 640 651 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 645 656 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 658 667 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 672 683 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 677 688 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 690 699 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 710 723 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 725 734 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 738 748 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 742 753 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 755 764 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 769 779 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 773 784 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 786 795 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 800 810 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 804 819 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 821 830 {ECO:0000255|PROSITE-ProRule:PRU00076}.
CONFLICT 736 736 V -> VE (in Ref. 2; CAI35934/CAI36038/
CAI35942/CAI35945/CAI35947/CAI35084 and
3; CAB57282). {ECO:0000305}.
CONFLICT 2369 2369 Y -> F (in Ref. 2; CAI35083/CAI35084/
CAI35933/CAI35934/CAI35941/CAI35942/
CAI35944/CAI35945/CAI35946/CAI35947/
CAI36037/CAI36038 and 4; AAF28317).
{ECO:0000305}.
CONFLICT 2690 2690 G -> R (in Ref. 2; CAI35083/CAI35084/
CAI35933/CAI35934/CAI35941/CAI35942/
CAI35944/CAI35945/CAI35946/CAI35947/
CAI36037/CAI36038 and 5; BAC65737).
{ECO:0000305}.
SEQUENCE 2764 AA; 306468 MW; 73BA3D916D0F0344 CRC64;
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
VTDLVHRESD EFSRQGTNFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL
PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGVRT
GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCAA
GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDS
GLCSCDPNWM GPDCSVVCSV DCGTHGVCIG GACRCEEGWT GAACDQRVCH PRCIEHGTCK
DGKCECREGW NGEHCTIDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD
NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK SFYDRIKLLA
GKDSTHIIPG DNPFNSSLVS LIRGQVVTMD GTPLVGVNVS FVKYPKYGYT ITRQDGTFDL
IANGGSALTL HFERAPFMSQ ERTVWLPWNS FYAMDTLVMK TEENSIPSCD LSGFVRPDPI
IISSPLSTFF SASPASNPIV PETQVLHEEI ELPGTNVKLR YLSSRTAGYK SLLKITMTQS
TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS DAVVSVGFEY
ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILHKGTGE NQFLTQQPAI
ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR RIFPSRNVTS
ILELRNKEFK HSNSPGHKYY LAVDPVTGSL YVSDTNSRRI YRVKSLSGAK DLAGNSEVVA
GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV DQNGIISTLL
GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI TENHQVSIIA
GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR LRQVTTNGEI
CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA VAPDGTIYIA DLGNIRIRAV
SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS ADNDVTELID
NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKAV STQNLELGLM TYDGNTGLLA
TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITIDIENSNR DDDVTVITNL
SSVEASYTVV QDQVRNSYQL CNNGTLRVMY ANGMAVSFHS EPHVLAGTIT PTIGRCNISL
PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI YDDHRKFTLR
IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR IVSRMFADGK
VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI GYIRNIYNPP
ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF GYDETTGVLK
MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI ASIKPVISET
PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI KEVQYEMFRS
LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP TWRYSYDLNG
NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY NSKGLLTRAY
NKASGWSVQY RYDGVGRRAS YKTNLGHHLQ YFYSDLHNPT RITHVYNHSN SEITSLYYDL
QGHLFAMESS SGEEYYVASD NTGTPLAVYS INGLMIKQLQ YTAYGEIYYD SNPDFQMVIG
FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPFNLYMF KNNNPLSNEL
DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG QLITGVQQTT
ERHNQAFLAL EGQVITKKLH ASIREKAGHW FATTTPIIGK GIMFAIKEGR VTTGVSSIAS
EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR KVLESGVNVT
VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAG QRALGTAWAK
EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS SNIQFLRQNE
MGKR


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