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Teneurin-4 (Ten-4) (Protein Odd Oz/ten-m homolog 4) (Tenascin-M4) (Ten-m4) (Teneurin transmembrane protein 4)

 TEN4_DANRE              Reviewed;        2824 AA.
Q9W7R3;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 107.
RecName: Full=Teneurin-4;
Short=Ten-4;
AltName: Full=Protein Odd Oz/ten-m homolog 4;
AltName: Full=Tenascin-M4;
Short=Ten-m4;
AltName: Full=Teneurin transmembrane protein 4;
Name=tenm4; Synonyms=odz4, tnm4;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=10495292; DOI=10.1016/S0925-4773(99)00155-0;
Mieda M., Kikuchi Y., Hirate Y., Aoki M., Okamoto H.;
"Compartmentalized expression of zebrafish ten-m3 and ten-m4,
homologues of the Drosophila tenm /odd Oz gene, in the central nervous
system.";
Mech. Dev. 87:223-227(1999).
[2]
DISRUPTION PHENOTYPE.
PubMed=26188006; DOI=10.1093/hmg/ddv281;
Hor H., Francescatto L., Bartesaghi L., Ortega-Cubero S., Kousi M.,
Lorenzo-Betancor O., Jimenez-Jimenez F.J., Gironell A., Clarimon J.,
Drechsel O., Agundez J.A., Kenzelmann Broz D., Chiquet-Ehrismann R.,
Lleo A., Coria F., Garcia-Martin E., Alonso-Navarro H., Marti M.J.,
Kulisevsky J., Hor C.N., Ossowski S., Chrast R., Katsanis N.,
Pastor P., Estivill X.;
"Missense mutations in TENM4, a regulator of axon guidance and central
myelination, cause essential tremor.";
Hum. Mol. Genet. 24:5677-5686(2015).
-!- FUNCTION: Involved in neural development, regulating the
establishment of proper connectivity within the nervous system.
May play a role in the establishment of the anterior-posterior
axis during gastrulation. Regulates the differentiation of
oligodendrocytes and myelination of axons. May function as a
cellular signal transducer (By similarity).
{ECO:0000250|UniProtKB:Q3UHK6}.
-!- SUBUNIT: Homodimer; disulfide-linked (Probable). May also form
heterodimer with either TENM1 or TENM2 or TENM3 (By similarity).
{ECO:0000250, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q6N022}; Single-pass membrane protein
{ECO:0000255}. Cell projection {ECO:0000250|UniProtKB:Q3UHK6}.
Nucleus {ECO:0000250|UniProtKB:Q3UHK6}. Cytoplasm
{ECO:0000250|UniProtKB:Q3UHK6}.
-!- TISSUE SPECIFICITY: Mainly expressed in the brain.
{ECO:0000269|PubMed:10495292}.
-!- DEVELOPMENTAL STAGE: During gastrulation, expressed throughout the
embryo very faintly. Expressed along the anterior margin of the
neural plate. Later, this marginal expression extends caudally,
and eventually restricted only to the caudal neural plate. At 14 h
post-fertilization, it is expressed in the brain. Expressed in the
rhombomere 5 (r5) and more strongly in r6. Expressed in the
rostral diencephalon with weak expression in the optic vesicles,
and a region covering the mesencephalon and the midbrain/hindbrain
boundary (MHB) in a gradient manner with stronger expression at
its posterior end. At 17 hpf, expressed weakly in the dorsal edge
of the most caudal part of the neural tube. Faint expression is
detected in several neurons located at ventral and dorsal parts of
the caudal spinal cord. {ECO:0000269|PubMed:10495292}.
-!- 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.
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of the gene in embryos
resulted in a modest reduction of myelin in the brain and an
increase in the number of small-diameter neuronal axons with
aberrant branching along the notochord.
{ECO:0000269|PubMed:26188006}.
-!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB026980; BAA81893.1; -; mRNA.
UniGene; Dr.81257; -.
ProteinModelPortal; Q9W7R3; -.
SMR; Q9W7R3; -.
STRING; 7955.ENSDARP00000016395; -.
PaxDb; Q9W7R3; -.
PRIDE; Q9W7R3; -.
ZFIN; ZDB-GENE-990714-20; tenm4.
eggNOG; KOG4659; Eukaryota.
eggNOG; ENOG410XQQD; LUCA.
HOGENOM; HOG000231701; -.
HOVERGEN; HBG080306; -.
InParanoid; Q9W7R3; -.
PhylomeDB; Q9W7R3; -.
PRO; PR:Q9W7R3; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
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:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:ZFIN.
GO; GO:0032289; P:central nervous system myelin formation; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
GO; GO:0097264; P:self proteolysis; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 2.120.10.30; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
InterPro; IPR022385; Rhs_assc_core.
InterPro; IPR031325; RHS_repeat.
InterPro; IPR009471; Ten_N.
InterPro; IPR027688; TENM1/TENM4.
InterPro; IPR028916; Tox-GHH_dom.
InterPro; IPR006530; YD.
PANTHER; PTHR11219:SF9; PTHR11219:SF9; 1.
Pfam; PF05593; RHS_repeat; 1.
Pfam; PF06484; Ten_N; 1.
Pfam; PF15636; Tox-GHH; 1.
SMART; SM00181; EGF; 8.
SUPFAM; SSF49464; SSF49464; 1.
SUPFAM; SSF50952; SSF50952; 1.
TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
TIGRFAMs; TIGR01643; YD_repeat_2x; 3.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 6.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS51361; TENEURIN_N; 1.
2: Evidence at transcript level;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Glycoprotein; Membrane; Nucleus; Reference proteome;
Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 2824 Teneurin-4.
/FTId=PRO_0000259510.
TRANSMEM 417 437 Helical. {ECO:0000255}.
DOMAIN 1 412 Teneurin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00694}.
DOMAIN 633 664 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 665 695 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 697 729 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 730 761 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 763 796 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 797 828 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 829 858 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 859 893 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1278 1321 NHL 1.
REPEAT 1326 1363 NHL 2.
REPEAT 1389 1433 NHL 3.
REPEAT 1448 1499 NHL 4.
REPEAT 1522 1552 NHL 5.
REPEAT 1578 1621 NHL 6.
REPEAT 1631 1650 YD 1.
REPEAT 1667 1687 YD 2.
REPEAT 1730 1749 YD 3.
REPEAT 1750 1772 YD 4.
REPEAT 1942 1961 YD 5.
REPEAT 1983 2001 YD 6.
REPEAT 2002 2022 YD 7.
REPEAT 2029 2046 YD 8.
REPEAT 2047 2068 YD 9.
REPEAT 2069 2086 YD 10.
REPEAT 2089 2109 YD 11.
REPEAT 2112 2132 YD 12.
REPEAT 2140 2159 YD 13.
REPEAT 2165 2182 YD 14.
REPEAT 2183 2209 YD 15.
REPEAT 2211 2224 YD 16.
REPEAT 2225 2248 YD 17.
REPEAT 2251 2271 YD 18.
REPEAT 2272 2292 YD 19.
REPEAT 2294 2314 YD 20.
REPEAT 2326 2346 YD 21.
REPEAT 2348 2368 YD 22.
REPEAT 2394 2435 YD 23.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1002 1002 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1173 1173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1321 1321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1647 1647 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1664 1664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1760 1760 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1796 1796 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1854 1854 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1939 1939 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2040 2040 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2243 2243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2383 2383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2701 2701 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 637 647 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 641 652 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 654 663 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 672 683 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 685 694 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 701 712 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 706 717 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 719 728 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 733 744 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 738 749 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 751 760 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 771 784 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 786 795 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 800 810 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 804 815 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 817 826 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 831 841 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 835 846 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 848 857 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 862 872 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 866 881 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 883 892 {ECO:0000255|PROSITE-ProRule:PRU00076}.
SEQUENCE 2824 AA; 313506 MW; 27007746DD34E356 CRC64;
MEVKERRPYR SLTSRRDTER RYTSSSADSE DGKINPKSYS SSETLKAFDQ DSRLAYGSRV
KDLVHHEADE FSRQGPDFSL RDMAFGDPVP PHMGAYRTEM GLPHRDYSVS VASDADTETD
GIMSPEHAVR LWGRSNTKSG RSSCLFSRAN SNLTLTDTEH ENTENGPPLH CSSASSSPVD
SPYPPPSHAA NQSQGRLLGN SGAQAGRDSE SEDEFGPNSF LVKTGSGNVC TPAAATANEG
SFQNHSRLRT PPLPLFHSHS PSQHHTASIG SLSRSNYTQR SNPSPAPTDS SAPNEGPTSA
QDSSSAQDNW LLNSNVPLET RNIAKQTFLE TLQDNFIEMD ILATARRDGA YTDGHFLFKP
GGTSPLYCTT SPGYPLTSST VYSPPPRPLP RNTFSRPAFS LKKPYKHCNW KCAALSAILI
SVTLVFLLAY FIAMHLFGLN WHLQPVQRQI YQLTEDNTSG LHLPTDLGLP PLGNTGLEFP
DRGSRDDGKL DGFFPEDSFI DMGEIDVGRK VAQLIPPGIF WRSQVFIDHP MYLKFNVSLS
KDALVGIYGR RGLPPSHTQF DFVELLDGRR LLSQGLPGLD GPPFPAQQRS LVPITSHDTG
CIQYMDSGIW HLAVYNDGKE TEQVSFLTTA IDSIDDCPSN CFGNGDCVSG NCHCFPGFRG
PDCSRASCPV LCSGNGQYLK GRCMCHSGWK GSECDVPTNQ CIDITCSGHG TCIVGTCICN
PSYKGENCEE VDCLDPTCSG RGVCVRGECH CFVGWGGPGC ESPRASCMEQ CSGHGSFLAD
TNTCNCDHNW TGHDCSTELC AADCGGHGIC VAGSCRCDEG WMGTGCEQRA CHPRCSEHGT
CKDGKCECSP GWNGEHCTIE GCPGLCNGNG RCTLGNNGWY CVCQLGWRGA GCDTSMETAC
SDGKDNDGDG LTDCMDPDCC LQASCHTTSL CVGSPDPLDI IQETQISSSL STLQSFYQRI
HFLVGRDSTH VIPDVNPFDG IHACVIRGQV VTSDGTPLVG VNISFINKPA YGYTITRQDG
SFDLVSNGGV AIGLRFERAP FITQEHTLWL PWGRFFVMDT IVMRHEVNDI PSCDLSSFTR
PMPIVLPAPL TAFAGTCPER GIVVPEIQTL QEEVRIPGTD MRLGYLSSRT SGYKSLLRIT
LTHSTIPFSL MKVHLMVAVE GRLFRKWFSA APNLSYDFVW DKTDVYSQKV YGLSEAFVSV
GFEYESCPDL ILWEKRTAVL QGYETTASNL GGWSVDKHHA LNIQSGILHK GNGENIFISQ
QPPVIGSIMG NGRRRSISCP SCNGLADGNK LLAPVALACG SDGSLYVGDF NYVRRIFTTG
NVTSVLELSN SPAHKYYLAT SPVSGWLYLS DTSSRKVFKV KSLYAVKDVA KNLELVAGTG
DQCLPYDETR CGDGGKAVEA TLTNPRGITV DKYGVIFFVD GTMIRRIDQN GIISTLLGFN
DLTSARPLSC DSVMDISQVR LEWPTDLAVS PMDNSLYVLD NNVVLQISEN HQVRIVAGRP
MHCQVPGLDH FLVSKIAIHA TLESANALAV SHNGLLYIAE SDEKKINRVR QVSTNGEISL
LAGAPSGCDC KNDANCDCYS GDDGYAKDAK LNAPSSLAVS PDGELFIADL GNIRIRYVRR
NKAFLNPLNM YEISSPIDDE LYLFDVNASH VFTQSLTTGD YLYNFTYSGE GDLSSITDKN
KNRVSIRRDS TGLPLWLMGP DGQTFWFTMG TNNALKSVAA QGQEIAVMTY HGSSGLLATK
SNEDGWSTFY EYDNYGRLTN VTYPTGRVSS YRTDSDSTVR VQTEGSNKED ITVTTNLSAS
GTFYTLMQDQ VKNSYYIGLD GSLRLVLANG MEVSLHTEPH LLSGTVNPTI SKRNVTLPID
NGLNLVEWRQ RKEQARGQVT VYGRRLRVHN RNLLSMDFDR VTRTEKVYDD HRKFTLRIHY
DHAGRPTLWA PSSRLNGVNV TYSPGGHIAG IQRGTMSVRM EYDQNGRITS KIFADGKSWS
YTYLEKSMVL LLYSQRQYIF EFDKNDRLSS VTMPNVARQT LETTRSIGYY RNTYRPPEGN
ATVLQDYSED GLLLQTIHQG TGRRVIYKYG KLSRLLEILY DTTRIAFSYD ESAGMLKTVG
LQSEGFACTI RYRQIGPLID RQIFRFSEEG MVNARFDYNY DNSFRVTSMQ AVINETPLPI
DLYRYDDVSG KTEQFGKFGV IYYDINQIIT TAVMTHTKHF DAYGRVKEVQ YEIFRSLMYW
MMVQFDNMGR VVAKELKVGP YANTTRYAYE YDADGQLQVV SINDKPLWRY SYDLNGNLHL
LSPGNSARLT PLRYDIRDRI TRLGDVQYRL DEDGFLRQRG NDFFEYNSAG LLVKTYNKVN
GWTIKYRYDG LGRRVSSRST QGHHLQFFYA DLSSPTRVTH MYNHSSSEIT SLYYDLQGHL
FAMELSSGDE FYVACDNIGT PLAVFSGAGL MIKQILHTAF GEVYLDSNPS FQLVIGYQGG
LYEPLTKLVH MGRRDYDVLA GRWTTPDHDI RKRLNSDNIV PFNLYMFKNN NPLSNSQETK
CYMTDVNSWL VTFGFQLYNV IPGYRKPVTD AMEPSYELVH TQIKTQEWDS TKSVLGVQCE
VQRQLKSFVR LERFGQIYSA SDSGCPPTPL HTLFATGTSL FGKGVKVAIR EGRVEADIIS
LANEDGRRIA AVLDKASYLQ DLHFTIAGLD THYFVKSGLV EGDLSLLGMT VGQRTLETGV
NVTVSQVNMV LGGRSRRITD IQMQYGTLSL NVRYGSSVDE EKVRVLELAR QRAVATAWAH
ERHRLRQGEE GSRAWTDGER QQLLSSGRVQ GYEGFYIVSV DQFPELTDNI NNVHFWRQTE
MGRR


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