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Q3UHK6 (TEN4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Teneurin-4

Short name=Ten-4
Alternative name(s):
Downstream of CHOP4
Protein Odd Oz/ten-m homolog 4
Tenascin-M4
Short name=Ten-m4
Teneurin transmembrane protein 4
Gene names
Name:Tenm4
Synonyms:Doc4, Kiaa1302, Odz4, Tnm4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2771 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Plays a role in the establishment of the anterior-posterior axis during gastrulation. Regulates the differentiation and cellular process formation of oligodendrocytes and myelination of small-diameter axons in the central nervous system (CNS). Promotes activation of focal adhesion kinase. May function as a cellular signal transducer. Ref.7 Ref.9

Subunit structure

Homodimer; disulfide-linked. May also form heterodimer with either TENM1 or TENM2 or TENM3. Ref.5

Subcellular location

Membrane; Single-pass membrane protein Probable. Nucleus. Cytoplasm. Cell projection Ref.9.

Tissue specificity

Expressed in brain and spinal cord (at protein level). Expressed in neurons and oligodendrocytes of the spinal cord. Expressed weakly in kidney, lung and spleen. Expressed in the cortex, CA1, CA2 and CA3 of the hippocampus. Expressed in the white matter, Purkinje cells and molecular layer of the cerebellum. Ref.6 Ref.7 Ref.9

Developmental stage

Expressed in spinal cord at 18 dpc (at protein level). Expressed in the epiblast and extraembryonic regions as early as 6.5 dpc. Expressed in the neural plate and extraembryonic tissues at 7.5 dpc. Expressed in the forebrain, mid/hindbrain junction, somites and tail bud at 8.5 dpc. Expressed in the tail bud and limbs at 11.5 dpc. Expressed in the diencephalon and midbrain at 12.5 dpc. Ref.6 Ref.7 Ref.9

Induction

Up-regulated during oligodendrocyte differentiation. Ref.9

Domain

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.

Disruption phenotype

Mice show tremors and hypomyelination in the central nervous system (CNS), particularly in the spinal cord, but not in the sciatic nerve of the peripheral nervous system (PNS). Differentiation of oligodendrocytes is prevented in the spinal cord. Ref.9

Sequence similarities

Belongs to the tenascin family. Teneurin subfamily.

Contains 8 EGF-like domains.

Contains 5 NHL repeats.

Contains 1 teneurin N-terminal domain.

Contains 23 YD repeats.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentCell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac cell fate specification

Inferred from mutant phenotype PubMed 17350578. Source: MGI

cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 17350578. Source: MGI

central nervous system myelin formation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

gastrulation with mouth forming second

Inferred from mutant phenotype Ref.7. Source: MGI

neuron development

Inferred from electronic annotation. Source: InterPro

positive regulation of gastrulation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of myelination

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of oligodendrocyte differentiation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

neuron projection

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionprotein homodimerization activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional mRNAs also exist. Tissue-specific expression of isoforms was observed throughout embryogenesis and in the brain and ovary adult tissues.
Isoform 1 (identifier: Q3UHK6-1)

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.
Isoform 2 (identifier: Q3UHK6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     164-164: T → TGAPLHCSSASSTPIEQSPSPPPSPPANESQRRLLGNGVAQPTPDSDSEEEFVPNSFLVKSGSASLGVAAN
     791-799: Missing.
     1269-1275: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q3UHK6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPDHSALSAARAQFVDVEEREPEAM
     164-164: T → TGAPLHCSSASSTPIEQSPSPPPSPPANESQRRLLGNGVAQPTPDSDSEEEFVPNSFLVKSGSASLGVAAN
     251-283: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q3UHK6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPDHSALSAARAQFVDVEEREPEAM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27712771Teneurin-4
PRO_0000259509

Regions

Topological domain1 – 345345Cytoplasmic Potential
Transmembrane346 – 36621Helical; Potential
Topological domain367 – 27712405Extracellular Potential
Domain1 – 341341Teneurin N-terminal
Domain564 – 59532EGF-like 1
Domain596 – 62631EGF-like 2
Domain628 – 66033EGF-like 3
Domain661 – 69232EGF-like 4
Domain694 – 72734EGF-like 5
Domain728 – 75932EGF-like 6
Domain760 – 78930EGF-like 7
Domain790 – 83344EGF-like 8
Repeat1218 – 126144NHL 1
Repeat1266 – 131045NHL 2
Repeat1336 – 138045NHL 3
Repeat1395 – 144652NHL 4
Repeat1525 – 156844NHL 5
Repeat1578 – 159720YD 1
Repeat1614 – 163421YD 2
Repeat1677 – 169620YD 3
Repeat1697 – 171923YD 4
Repeat1889 – 190820YD 5
Repeat1930 – 194819YD 6
Repeat1949 – 196921YD 7
Repeat1976 – 199318YD 8
Repeat1994 – 201522YD 9
Repeat2016 – 203318YD 10
Repeat2036 – 205621YD 11
Repeat2059 – 207921YD 12
Repeat2087 – 210620YD 13
Repeat2112 – 212918YD 14
Repeat2130 – 215627YD 15
Repeat2158 – 217114YD 16
Repeat2172 – 219524YD 17
Repeat2198 – 221821YD 18
Repeat2219 – 223921YD 19
Repeat2241 – 226121YD 20
Repeat2273 – 229321YD 21
Repeat2295 – 231521YD 22
Repeat2341 – 238242YD 23
Compositional bias179 – 1846Poly-Pro

Amino acid modifications

Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Glycosylation12611N-linked (GlcNAc...) Potential
Glycosylation16111N-linked (GlcNAc...) Potential
Glycosylation17071N-linked (GlcNAc...) Ref.8
Glycosylation17431N-linked (GlcNAc...) Potential
Glycosylation18011N-linked (GlcNAc...) Potential
Glycosylation18861N-linked (GlcNAc...) Potential
Glycosylation19871N-linked (GlcNAc...) Potential
Glycosylation21901N-linked (GlcNAc...) Ref.8
Glycosylation23301N-linked (GlcNAc...) Potential
Glycosylation26481N-linked (GlcNAc...) Potential
Disulfide bond568 ↔ 578 By similarity
Disulfide bond572 ↔ 583 By similarity
Disulfide bond585 ↔ 594 By similarity
Disulfide bond603 ↔ 614 By similarity
Disulfide bond616 ↔ 625 By similarity
Disulfide bond632 ↔ 643 By similarity
Disulfide bond637 ↔ 648 By similarity
Disulfide bond650 ↔ 659 By similarity
Disulfide bond664 ↔ 675 By similarity
Disulfide bond669 ↔ 680 By similarity
Disulfide bond682 ↔ 691 By similarity
Disulfide bond702 ↔ 715 By similarity
Disulfide bond717 ↔ 726 By similarity
Disulfide bond731 ↔ 741 By similarity
Disulfide bond735 ↔ 746 By similarity
Disulfide bond748 ↔ 757 By similarity
Disulfide bond762 ↔ 772 By similarity
Disulfide bond766 ↔ 777 By similarity
Disulfide bond779 ↔ 788 By similarity
Disulfide bond802 ↔ 812 By similarity
Disulfide bond806 ↔ 821 By similarity
Disulfide bond823 ↔ 832 By similarity

Natural variations

Alternative sequence11M → MEPDHSALSAARAQFVDVEE REPEAM in isoform 3 and isoform 4.
VSP_021404
Alternative sequence1641T → TGAPLHCSSASSTPIEQSPS PPPSPPANESQRRLLGNGVA QPTPDSDSEEEFVPNSFLVK SGSASLGVAAN in isoform 2 and isoform 3.
VSP_021405
Alternative sequence251 – 28333Missing in isoform 3.
VSP_021406
Alternative sequence791 – 7999Missing in isoform 2.
VSP_021407
Alternative sequence1269 – 12757Missing in isoform 2.
VSP_021408

Experimental info

Sequence conflict136 – 1372TR → EK in BAE36695. Ref.3
Sequence conflict152 – 16413LTLTD…ENTET → EKSGSASLGVAAN in BAE36695. Ref.3
Sequence conflict2401L → V in AAC31807. Ref.1
Sequence conflict2441N → K in AAC31807. Ref.1
Sequence conflict2471L → V in AAC31807. Ref.1
Sequence conflict2611L → W in AAC31807. Ref.1
Sequence conflict2711L → F in AAC31807. Ref.1
Sequence conflict2761H → R in AAC31807. Ref.1
Sequence conflict2861L → F in AAC31807. Ref.1
Sequence conflict422 – 4298KPSSLFPE → RVAALSVL in BAE36695. Ref.3
Sequence conflict4931F → L in AAC31807. Ref.1
Sequence conflict7801S → T in AAC31807. Ref.1
Sequence conflict8951S → P in BAA77399. Ref.2
Sequence conflict10131C → R in AAC31807. Ref.1
Sequence conflict10391E → G in BAE28005. Ref.3
Sequence conflict10771L → V in AAC31807. Ref.1
Sequence conflict11331L → F in BAA77399. Ref.2
Sequence conflict14571H → Q in AAC31807. Ref.1
Sequence conflict17431N → H in AAC31807. Ref.1
Sequence conflict17461A → G in AAC31807. Ref.1
Sequence conflict18311R → P in AAC31807. Ref.1
Sequence conflict18751L → F in AAC31807. Ref.1
Sequence conflict19521N → D in BAE28005. Ref.3
Sequence conflict21441T → S in AAC31807. Ref.1
Sequence conflict21601I → T in AAC31807. Ref.1
Sequence conflict22561K → R in BAE28005. Ref.3
Sequence conflict22621F → S in AAC31807. Ref.1
Sequence conflict23301N → S in AAC31807. Ref.1
Sequence conflict26571V → M in AAC31807. Ref.1
Sequence conflict26571V → M in BAA77399. Ref.2
Sequence conflict26571V → M in BAC65772. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 15EF31E25A171FD0

FASTA2,771308,425
        10         20         30         40         50         60 
MDVKERKPYR SLTRRRDAER RYTSSSADSE EGKGPQKSYS SSETLKAYDQ DARLAYGSRV 

        70         80         90        100        110        120 
KDMVPQEAEE FCRTGTNFTL RELGLGEMTP PHGTLYRTDI GLPHCGYSMG ASSDADLEAD 

       130        140        150        160        170        180 
TVLSPEHPVR LWGRSTRSGR SSCLSSRANS NLTLTDTEHE NTETDHPSSL QNHPRLRTPP 

       190        200        210        220        230        240 
PPLPHAHTPN QHHAASINSL NRGNFTPRSN PSPAPTDHSL SGEPPAGSAQ EPTHAQDNWL 

       250        260        270        280        290        300 
LNSNIPLETR NLGKQPFLGT LQDNLIEMDI LSASRHDGAY SDGHFLFKPG GTSPLFCTTS 

       310        320        330        340        350        360 
PGYPLTSSTV YSPPPRPLPR STFSRPAFNL KKPSKYCNWK CAALSAILIS ATLVILLAYF 

       370        380        390        400        410        420 
VAMHLFGLNW HLQPMEGQMQ MYEITEDTAS SWPVPTDVSL YPSGGTGLET PDRKGKGAAE 

       430        440        450        460        470        480 
GKPSSLFPED SFIDSGEIDV GRRASQKIPP GTFWRSQVFI DHPVHLKFNV SLGKAALVGI 

       490        500        510        520        530        540 
YGRKGLPPSH TQFDFVELLD GRRLLTQEAR SLEGPQRQSR GPVPPSSHET GFIQYLDSGI 

       550        560        570        580        590        600 
WHLAFYNDGK ESEVVSFLTT AIESVDNCPS NCYGNGDCIS GTCHCFLGFL GPDCGRASCP 

       610        620        630        640        650        660 
VLCSGNGQYM KGRCLCHSGW KGAECDVPTN QCIDVACSSH GTCIMGTCIC NPGYKGESCE 

       670        680        690        700        710        720 
EVDCMDPTCS SRGVCVRGEC HCSVGWGGTN CETPRATCLD QCSGHGTFLP DTGLCNCDPS 

       730        740        750        760        770        780 
WTGHDCSIEI CAADCGGHGV CVGGTCRCED GWMGAACDQR ACHPRCAEHG TCRDGKCECS 

       790        800        810        820        830        840 
PGWNGEHCTI AHYLDRVVKE GCPGLCNGNG RCTLDLNGWH CVCQLGWRGT GCDTSMETGC 

       850        860        870        880        890        900 
GDGKDNDGDG LVDCMDPDCC LQPLCHVNPL CLGSPDPLDI IQETQAPVSQ QNLNSFYDRI 

       910        920        930        940        950        960 
KFLVGRDSTH SIPGENPFDG GHACVIRGQV MTSDGTPLVG VNISFINNPL FGYTISRQDG 

       970        980        990       1000       1010       1020 
SFDLVTNGGI SIILRFERAP FITQEHTLWL PWDRFFVMET IVMRHEENEI PSCDLSNFAR 

      1030       1040       1050       1060       1070       1080 
PNPVVSPSPL TSFASSCAEK GPIVPEIQAL QEEIVIAGCK MRLSYLSSRT PGYKSVLRIS 

      1090       1100       1110       1120       1130       1140 
LTHPTIPFNL MKVHLMVAVE GRLFRKWFAA APDLSYYFIW DKTDVYNQKV FGLSEAFVSV 

      1150       1160       1170       1180       1190       1200 
GYEYESCPDL ILWEKRTAVL QGYEIDASKL GGWSLDKHHA LNIQSGILHK GNGENQFVSQ 

      1210       1220       1230       1240       1250       1260 
QPPVIGSIMG NGRRRSISCP SCNGLADGNK LLAPVALTCG SDGSLYVGDF NYIRRIFPSG 

      1270       1280       1290       1300       1310       1320 
NVTNILEMRN KDFRHSHSPA HKYYLATDPM SGAVFLSDTN SRRVFKVKST TVVKDLVKNS 

      1330       1340       1350       1360       1370       1380 
EVVAGTGDQC LPFDDTRCGD GGKATEATLT NPRGITVDKF GLIYFVDGTM IRRVDQNGII 

      1390       1400       1410       1420       1430       1440 
STLLGSNDLT SARPLSCDSV MEISQVRLEW PTDLAINPMD NSLYVLDNNV VLQISENHQV 

      1450       1460       1470       1480       1490       1500 
RIVAGRPMHC QVPGIDHFLL SKVAIHATLE SATALAVSHN GVLYIAETDE KKINRIRQVT 

      1510       1520       1530       1540       1550       1560 
TSGEISLVAG APSGCDCKND ANCDCFSGDD GYAKDAKLNT PSSLAVCADG ELYVADLGNI 

      1570       1580       1590       1600       1610       1620 
RIRFIRKNKP FLNTQNMYEL SSPIDQELYL FDTSGKHLYT QSLPTGDYLY NFTYTGDGDI 

      1630       1640       1650       1660       1670       1680 
THITDNNGNM VNVRRDSTGM PLWLVVPDGQ VYWVTMGTNS ALRSVTTQGH ELAMMTYHGN 

      1690       1700       1710       1720       1730       1740 
SGLLATKSNE NGWTTFYEYD SFGRLTNVTF PTGQVSSFRS DTDSSVHVQV ETSSKDDVTI 

      1750       1760       1770       1780       1790       1800 
TTNLSASGAF YTLLQDQVRN SYYIGADGSL RLLLANGMEV ALQTEPHLLA GTVNPTVGKR 

      1810       1820       1830       1840       1850       1860 
NVTLPIDNGL NLVEWRQRKE QARGQVTVFG RRLRVHNRNL LSLDFDRVTR TEKIYDDHRK 

      1870       1880       1890       1900       1910       1920 
FTLRILYDQA GRPSLWSPSS RLNGVNVTYS PGGHIAGIQR GIMSERMEYD QAGRITSRIF 

      1930       1940       1950       1960       1970       1980 
ADGKMWSYTY LEKSMVLHLH SQRQYIFEFD KNDRLSSVTM PNVARQTLET IRSVGYYRNI 

      1990       2000       2010       2020       2030       2040 
YQPPEGNASV IQDFTEDGHL LHTFYLGTGR RVIYKYGKLS KLAETLYDTT KVSFTYDETA 

      2050       2060       2070       2080       2090       2100 
GMLKTVNLQN EGFTCTIRYR QIGPLIDRQI FRFTEEGMVN ARFDYNYDNS FRVTSMQAVI 

      2110       2120       2130       2140       2150       2160 
NETPLPIDLY RYDDVSGKTE QFGKFGVIYY DINQIITTAV MTHTKHFDAY GRMKEVQYEI 

      2170       2180       2190       2200       2210       2220 
FRSLMYWMTV QYDNMGRVVK KELKVGPYAN TTRYSYEYDA DGQLQTVSIN DKPLWRYSYD 

      2230       2240       2250       2260       2270       2280 
LNGNLHLLSP GNSARLTPLR YDLRDRITRL GDVQYKMDED GFLRQRGGDV FEYNSAGLLI 

      2290       2300       2310       2320       2330       2340 
KAYNRASGWS VRYRYDGLGR RVSSKSSHSH HLQFFYADLT NPTKVTHLYN HSSSEITSLY 

      2350       2360       2370       2380       2390       2400 
YDLQGHLFAM ELSSGDEFYI ACDNIGTPLA VFSGTGLMIK QILYTAYGEI YMDTNPNFQI 

      2410       2420       2430       2440       2450       2460 
IIGYHGGLYD PLTKLVHMGR RDYDVLAGRW TSPDHELWKR LSSNSIVPFH LYMFKNNNPI 

      2470       2480       2490       2500       2510       2520 
SNSQDIKCFM TDVNSWLLTF GFQLHNVIPG YPKPDTDAME PSYELVHTQM KTQEWDNSKS 

      2530       2540       2550       2560       2570       2580 
ILGVQCEVQK QLKAFVTLER FDQLYGSTIT SCQQAPETKK FASSGSIFGK GVKFALKDGR 

      2590       2600       2610       2620       2630       2640 
VTTDIISVAN EDGRRIAAIL NNAHYLENLH FTIDGVDTHY FVKPGPSEGD LAILGLSGGR 

      2650       2660       2670       2680       2690       2700 
RTLENGVNVT VSQINTVLSG RTRRYTDIQL QYRALCLNTR YGTTVDEEKV RVLELARQRA 

      2710       2720       2730       2740       2750       2760 
VRQAWAREQQ RLREGEEGLR AWTDGEKQQV LNTGRVQGYD GFFVTSVEQY PELSDSANNI 

      2770 
HFMRQSEMGR R 

« Hide

Isoform 2 [UniParc].

Checksum: 820622CCE037744E
Show »

FASTA2,825313,428
Isoform 3 [UniParc].

Checksum: 1578D6B6F3E079B1
Show »

FASTA2,833314,673
Isoform 4 [UniParc].

Checksum: 70437010F777878E
Show »

FASTA2,796311,192

References

« Hide 'large scale' references
[1]"Identification of novel stress-induced genes downstream of chop."
Wang X.-Z., Kuroda M., Sok J., Batchvarova N., Kimmel R., Chung P., Zinszner H., Ron D.
EMBO J. 17:3619-3630(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: NIH Swiss.
[2]"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] (ISOFORM 1).
Strain: BALB/c.
Tissue: Brain.
[3]"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. expand/collapse author list , 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] (ISOFORMS 3 AND 4).
Strain: C57BL/6J.
Tissue: Muellerian duct.
[4]"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."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1574-2771.
Tissue: Brain.
[5]"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.
[6]"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, DEVELOPMENTAL STAGE.
[7]"Mutation of l7Rn3 shows that Odz4 is required for mouse gastrulation."
Lossie A.C., Nakamura H., Thomas S.E., Justice M.J.
Genetics 169:285-299(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN GASTRULATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1707 AND ASN-2190.
[9]"Teneurin-4 is a novel regulator of oligodendrocyte differentiation and myelination of small-diameter axons in the CNS."
Suzuki N., Fukushi M., Kosaki K., Doyle A.D., de Vega S., Yoshizaki K., Akazawa C., Arikawa-Hirasawa E., Yamada Y.
J. Neurosci. 32:11586-11599(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OLIGODENDROCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF059485 mRNA. Translation: AAC31807.1.
AB025413 mRNA. Translation: BAA77399.1.
AK147579 mRNA. Translation: BAE28005.1.
AK147329 mRNA. Translation: BAE27851.1.
AK162046 mRNA. Translation: BAE36695.1.
AK122490 mRNA. Translation: BAC65772.1.
CCDSCCDS40024.1. [Q3UHK6-4]
PIRT14271.
RefSeqNP_035988.2. NM_011858.3. [Q3UHK6-4]
XP_006507872.1. XM_006507809.1. [Q3UHK6-3]
XP_006507873.1. XM_006507810.1. [Q3UHK6-2]
XP_006507874.1. XM_006507811.1. [Q3UHK6-4]
UniGeneMm.254610.
Mm.391678.

3D structure databases

ProteinModelPortalQ3UHK6.
SMRQ3UHK6. Positions 541-871, 1537-1566.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3UHK6. 1 interaction.

PTM databases

PhosphoSiteQ3UHK6.

Proteomic databases

PaxDbQ3UHK6.
PRIDEQ3UHK6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107162; ENSMUSP00000102780; ENSMUSG00000048078. [Q3UHK6-2]
ENSMUST00000107165; ENSMUSP00000102783; ENSMUSG00000048078. [Q3UHK6-3]
ENSMUST00000107166; ENSMUSP00000102784; ENSMUSG00000048078. [Q3UHK6-4]
GeneID23966.
KEGGmmu:23966.
UCSCuc009iio.1. mouse. [Q3UHK6-4]
uc009iip.1. mouse. [Q3UHK6-3]
uc009iiq.1. mouse. [Q3UHK6-2]

Organism-specific databases

CTD26011.
MGIMGI:2447063. Tenm4.
RougeSearch...

Phylogenomic databases

eggNOGNOG323120.
GeneTreeENSGT00660000095277.
HOGENOMHOG000231701.
HOVERGENHBG080306.
InParanoidQ3UHK6.
OMANQFVSQQ.
OrthoDBEOG7H791C.
PhylomeDBQ3UHK6.
TreeFamTF316833.

Gene expression databases

ArrayExpressQ3UHK6.
BgeeQ3UHK6.
CleanExMM_ODZ4.
GenevestigatorQ3UHK6.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR008969. CarboxyPept-like_regulatory.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR013111. EGF_extracell.
IPR022385. Rhs_assc_core.
IPR027691. Ten-4.
IPR009471. Ten_N.
IPR028916. Tox-GHH_dom.
IPR006530. YD.
[Graphical view]
PANTHERPTHR11219:SF9. PTHR11219:SF9. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF12661. hEGF. 1 hit.
PF05593. RHS_repeat. 1 hit.
PF06484. Ten_N. 2 hits.
PF15636. Tox-GHH. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 7 hits.
[Graphical view]
SUPFAMSSF49464. SSF49464. 1 hit.
TIGRFAMsTIGR03696. Rhs_assc_core. 1 hit.
TIGR01643. YD_repeat_2x. 1 hit.
PROSITEPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 5 hits.
PS51361. TENEURIN_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303833.
PROQ3UHK6.
SOURCESearch...

Entry information

Entry nameTEN4_MOUSE
AccessionPrimary (citable) accession number: Q3UHK6
Secondary accession number(s): O70465 expand/collapse secondary AC list , Q3TSI0, Q3UH52, Q80TF5, Q9WTS7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot