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Protein

Tenascin

Gene

TNC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Tenascin
Short name:
TN
Alternative name(s):
Cytotactin
GMEM
GP 150-225
Glioma-associated-extracellular matrix antigen
Hexabrachion
JI
Myotendinous antigen
Neuronectin
Tenascin-C
Short name:
TN-C
Gene namesi
Name:TNC
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Propeptidei23 – 3311PRO_0000007743Add
BLAST
Chaini34 – 18081775TenascinPRO_0000007744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi64 – 64InterchainPROSITE-ProRule annotation
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi192 ↔ 202By similarity
Disulfide bondi196 ↔ 207By similarity
Disulfide bondi209 ↔ 218By similarity
Disulfide bondi223 ↔ 233By similarity
Disulfide bondi227 ↔ 238By similarity
Disulfide bondi240 ↔ 249By similarity
Disulfide bondi254 ↔ 264By similarity
Disulfide bondi258 ↔ 269By similarity
Disulfide bondi271 ↔ 280By similarity
Disulfide bondi285 ↔ 295By similarity
Disulfide bondi289 ↔ 300By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi316 ↔ 326By similarity
Disulfide bondi320 ↔ 331By similarity
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi347 ↔ 357By similarity
Disulfide bondi351 ↔ 362By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi378 ↔ 388By similarity
Disulfide bondi382 ↔ 393By similarity
Disulfide bondi395 ↔ 404By similarity
Disulfide bondi409 ↔ 419By similarity
Disulfide bondi413 ↔ 424By similarity
Disulfide bondi426 ↔ 435By similarity
Disulfide bondi440 ↔ 450By similarity
Disulfide bondi444 ↔ 455By similarity
Disulfide bondi457 ↔ 466By similarity
Disulfide bondi471 ↔ 481By similarity
Disulfide bondi475 ↔ 486By similarity
Disulfide bondi488 ↔ 497By similarity
Disulfide bondi502 ↔ 512By similarity
Disulfide bondi506 ↔ 517By similarity
Disulfide bondi519 ↔ 528By similarity
Disulfide bondi533 ↔ 543By similarity
Disulfide bondi537 ↔ 548By similarity
Disulfide bondi550 ↔ 559By similarity
Disulfide bondi564 ↔ 574By similarity
Disulfide bondi568 ↔ 579By similarity
Disulfide bondi581 ↔ 590By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence analysis
Glycosylationi643 – 6431N-linked (GlcNAc...)Sequence analysis
Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence analysis
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence analysis
Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence analysis
Glycosylationi1090 – 10901N-linked (GlcNAc...)Sequence analysis
Glycosylationi1101 – 11011N-linked (GlcNAc...)Sequence analysis
Glycosylationi1112 – 11121N-linked (GlcNAc...)Sequence analysis
Glycosylationi1153 – 11531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence analysis
Glycosylationi1416 – 14161N-linked (GlcNAc...)Sequence analysis
Glycosylationi1736 – 17361N-linked (GlcNAc...)Sequence analysis
Glycosylationi1769 – 17691N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP10039.

Expressioni

Inductioni

By TGF-beta.

Interactioni

Subunit structurei

Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule. Interacts with CSPG4.2 Publications

Protein-protein interaction databases

IntActiP10039. 1 interaction.
MINTiMINT-1534624.
STRINGi9031.ENSGALP00000011509.

Structurei

Secondary structure

1
1808
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi960 – 9667Combined sources
Beta strandi969 – 9779Combined sources
Beta strandi984 – 9918Combined sources
Beta strandi997 – 10026Combined sources
Beta strandi1007 – 10137Combined sources
Beta strandi1019 – 103012Combined sources
Beta strandi1036 – 10416Combined sources
Beta strandi1323 – 13275Combined sources
Beta strandi1333 – 13375Combined sources
Beta strandi1345 – 13539Combined sources
Beta strandi1360 – 13656Combined sources
Beta strandi1370 – 13734Combined sources
Beta strandi1381 – 139010Combined sources
Beta strandi1398 – 14036Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QR4X-ray2.55A/B950-1408[»]
ProteinModelPortaliP10039.
SMRiP10039. Positions 774-862, 1232-1404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10039.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 18813EGF-like 1; incompletePROSITE-ProRule annotationAdd
BLAST
Domaini188 – 21932EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini219 – 25032EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini250 – 28132EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini281 – 31232EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini312 – 34332EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini343 – 37432EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini374 – 40532EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 43632EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 46732EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini467 – 49832EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini498 – 52932EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini529 – 56032EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini560 – 59132EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini595 – 68591Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini686 – 77590Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini776 – 86691Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini867 – 95791Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini958 – 104689Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1047 – 113892Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini1139 – 122890Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1229 – 131890Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1319 – 140890Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1409 – 149587Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1496 – 158489Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini1582 – 1797216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili118 – 14225Sequence analysisAdd
BLAST

Domaini

The fibrinogen C-terminal domain mediates interaction with CSPG5.1 Publication

Sequence similaritiesi

Belongs to the tenascin family.Curated
Contains 14 EGF-like domains.PROSITE-ProRule annotation
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
Contains 11 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG4111MDJ. LUCA.
HOVERGENiHBG008949.
InParanoidiP10039.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR013111. EGF_extracell.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033078. TNC.
[Graphical view]
PANTHERiPTHR19143:SF38. PTHR19143:SF38. 2 hits.
PfamiPF07974. EGF_2. 5 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 11 hits.
PF12661. hEGF. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 13 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 11 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 8 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 14 hits.
PS01186. EGF_2. 14 hits.
PS50026. EGF_3. 5 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 11 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoforms are produced in a tissue- and time-specific manner during development.

Isoform 1 (identifier: P10039-1) [UniParc]FASTAAdd to basket

Also known as: 230 kDa

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
MGLPSQVLAC AILGLLYQHA SGGLIKRIIR QKRETGLNVT LPEDNQPVVF
60 70 80 90 100
NHVYNIKLPV GSLCSVDLDT ASGDADLKAE IEPVKNYEEH TVNEGNQIVF
110 120 130 140 150
THRINIPRRA CGCAAAPDIK DLLSRLEELE GLVSSLREQC ASGAGCCPNS
160 170 180 190 200
QTAEGRLDTA PYCSGHGNYS TEICGCVCEP GWKGPNCSEP ACPRNCLNRG
210 220 230 240 250
LCVRGKCICE EGFTGEDCSQ AACPSDCNDQ GKCVDGVCVC FEGYTGPDCG
260 270 280 290 300
EELCPHGCGI HGRCVGGRCV CHEGFTGEDC NEPLCPNNCH NRGRCVDNEC
310 320 330 340 350
VCDEGYTGED CGELICPNDC FDRGRCINGT CFCEEGYTGE DCGELTCPNN
360 370 380 390 400
CNGNGRCENG LCVCHEGFVG DDCSQKRCPK DCNNRGHCVD GRCVCHEGYL
410 420 430 440 450
GEDCGELRCP NDCHNRGRCI NGQCVCDEGF IGEDCGELRC PNDCHNRGRC
460 470 480 490 500
VNGQCECHEG FIGEDCGELR CPNDCNSHGR CVNGQCVCDE GYTGEDCGEL
510 520 530 540 550
RCPNDCHNRG RCVEGRCVCD NGFMGEDCGE LSCPNDCHQH GRCVDGRCVC
560 570 580 590 600
HEGFTGEDCR ERSCPNDCNN VGRCVEGRCV CEEGYMGIDC SDVSPPTELT
610 620 630 640 650
VTNVTDKTVN LEWKHENLVN EYLVTYVPTS SGGLDLQFTV PGNQTSATIH
660 670 680 690 700
ELEPGVEYFI RVFAILKNKK SIPVSARVAT YLPAPEGLKF KSVRETSVQV
710 720 730 740 750
EWDPLSISFD GWELVFRNMQ KKDDNGDITS SLKRPETSYM QPGLAPGQQY
760 770 780 790 800
NVSLHIVKNN TRGPGLSRVI TTKLDAPSQI EAKDVTDTTA LITWSKPLAE
810 820 830 840 850
IEGIELTYGP KDVPGDRTTI DLSEDENQYS IGNLRPHTEY EVTLISRRGD
860 870 880 890 900
MESDPAKEVF VTDLDAPRNL KRVSQTDNSI TLEWKNSHAN IDNYRIKFAP
910 920 930 940 950
ISGGDHTELT VPKGNQATTR ATLTGLRPGT EYGIGVTAVR QDRESAPATI
960 970 980 990 1000
NAGTDLDNPK DLEVSDPTET TLSLRWRRPV AKFDRYRLTY VSPSGKKNEM
1010 1020 1030 1040 1050
EIPVDSTSFI LRGLDAGTEY TISLVAEKGR HKSKPTTIKG STEEEPELGN
1060 1070 1080 1090 1100
LSVSETGWDG FQLTWTAADG AYENFVIQVQ QSDNPEETWN ITVPGGQHSV
1110 1120 1130 1140 1150
NVTGLKANTP YNVTLYGVIR GYRTKPLYVE TTTGAHPEVG ELTVSDITPE
1160 1170 1180 1190 1200
SFNLSWTTTN GDFDAFTIEI IDSNRLLEPM EFNISGNSRT AHISGLSPST
1210 1220 1230 1240 1250
DFIVYLYGIS HGFRTQAISA AATTEAEPEV DNLLVSDATP DGFRLSWTAD
1260 1270 1280 1290 1300
DGVFDSFVLK IRDTKRKSDP LELIVPGHER THDITGLKEG TEYEIELYGV
1310 1320 1330 1340 1350
SSGRRSQPIN SVATTVVGSP KGISFSDITE NSATVSWTPP RSRVDSYRVS
1360 1370 1380 1390 1400
YVPITGGTPN VVTVDGSKTR TKLVKLVPGV DYNVNIISVK GFEESEPISG
1410 1420 1430 1440 1450
ILKTALDSPS GLVVMNITDS EALATWQPAI AAVDNYIVSY SSEDEPEVTQ
1460 1470 1480 1490 1500
MVSGNTVEYD LNGLRPATEY TLRVHAVKDA QKSETLSTQF TTGLDAPKDL
1510 1520 1530 1540 1550
SATEVQSETA VITWRPPRAP VTDYLLTYES IDGRVKEVIL DPETTSYTLT
1560 1570 1580 1590 1600
ELSPSTQYTV KLQALSRSMR SKMIQTVFTT TGLLYPYPKD CSQALLNGEV
1610 1620 1630 1640 1650
TSGLYTIYLN GDRTQPLQVF CDMAEDGGGW IVFLRRQNGK EDFYRNWKNY
1660 1670 1680 1690 1700
VAGFGDPKDE FWIGLENLHK ISSQGQYELR VDLRDRGETA YAVYDKFSVG
1710 1720 1730 1740 1750
DAKTRYRLRV DGYSGTAGDS MTYHNGRSFS TFDKDNDSAI TNCALSYKGA
1760 1770 1780 1790 1800
FWYKNCHRVN LMGRYGDNNH SQGVNWFHWK GHEYSIQFAE MKLRPSSFRN

LEGRRKRA
Length:1,808
Mass (Da):198,859
Last modified:March 1, 1992 - v2
Checksum:iB924A06CF9EFD6DE
GO
Isoform 2 (identifier: P10039-2) [UniParc]FASTAAdd to basket

Also known as: 200 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1043-1224: Missing.

Show »
Length:1,626
Mass (Da):178,977
Checksum:i3C85565BA96A21B7
GO
Isoform 3 (identifier: P10039-3) [UniParc]FASTAAdd to basket

Also known as: 190 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1043-1315: Missing.

Show »
Length:1,535
Mass (Da):168,905
Checksum:iD7019911B76F1F4D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821W → R in CAA30824 (PubMed:2460335).Curated
Sequence conflicti563 – 5719SCPNDCNNV → PAPMTATTW in AAA48748 (PubMed:2451243).Curated
Sequence conflicti598 – 5981E → G in AAA48748 (PubMed:2451243).Curated
Sequence conflicti838 – 8381T → TEY in AAA48748 (PubMed:2451243).Curated
Sequence conflicti886 – 8861N → F in AAA48748 (PubMed:2451243).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1043 – 1315273Missing in isoform 3. 1 PublicationVSP_001411Add
BLAST
Alternative sequencei1043 – 1224182Missing in isoform 2. 1 PublicationVSP_001410Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23121 mRNA. Translation: AAA49086.1.
X08031 mRNA. Translation: CAB40811.1.
X08030 mRNA. Translation: CAA30824.1. Different termination.
J03641 mRNA. Translation: AAA48748.1. Sequence problems.
M20816 mRNA. Translation: AAA48749.1. Sequence problems.
PIRiA31930.
UniGeneiGga.3818.
Gga.51524.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23121 mRNA. Translation: AAA49086.1.
X08031 mRNA. Translation: CAB40811.1.
X08030 mRNA. Translation: CAA30824.1. Different termination.
J03641 mRNA. Translation: AAA48748.1. Sequence problems.
M20816 mRNA. Translation: AAA48749.1. Sequence problems.
PIRiA31930.
UniGeneiGga.3818.
Gga.51524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QR4X-ray2.55A/B950-1408[»]
ProteinModelPortaliP10039.
SMRiP10039. Positions 774-862, 1232-1404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10039. 1 interaction.
MINTiMINT-1534624.
STRINGi9031.ENSGALP00000011509.

Proteomic databases

PaxDbiP10039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG4111MDJ. LUCA.
HOVERGENiHBG008949.
InParanoidiP10039.

Miscellaneous databases

EvolutionaryTraceiP10039.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR013111. EGF_extracell.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033078. TNC.
[Graphical view]
PANTHERiPTHR19143:SF38. PTHR19143:SF38. 2 hits.
PfamiPF07974. EGF_2. 5 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 11 hits.
PF12661. hEGF. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 13 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 11 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 8 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 14 hits.
PS01186. EGF_2. 14 hits.
PS50026. EGF_3. 5 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments."
    Spring J., Beck K., Chiquet-Ehrismann R.
    Cell 59:325-334(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Embryo.
  2. "Tenascin: cDNA cloning and induction by TGF-beta."
    Pearson C.A., Pearson D., Shibahara S., Hofsteenge J., Chiquet-Ehrismann R.
    EMBO J. 7:2977-2982(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-722 (ISOFORMS 1/2/3), PROTEIN SEQUENCE OF 79-96.
    Tissue: Fibroblast.
  3. "A cDNA clone for cytotactin contains sequences similar to epidermal growth factor-like repeats and segments of fibronectin and fibrinogen."
    Jones F.S., Burgoon M.P., Hoffman S., Crossin K.L., Cunningham B.A., Edelman G.M.
    Proc. Natl. Acad. Sci. U.S.A. 85:2186-2190(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 464-1018 AND 1412-1661 (ISOFORMS 1/2/3), PROTEIN SEQUENCE OF 852-868.
    Tissue: Embryo.
  4. "Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formation."
    Schumacher S., Volkmer H., Buck F., Otto A., Tarnok A., Roth S., Rathjen F.G.
    J. Cell Biol. 136:895-906(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG5.
  5. "CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion."
    Schumacher S., Jung M., Noerenberg U., Dorner A., Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.
    J. Biol. Chem. 276:7337-7345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG5, DOMAIN.

Entry informationi

Entry nameiTENA_CHICK
AccessioniPrimary (citable) accession number: P10039
Secondary accession number(s): O73584, O73585, P13132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 1, 1992
Last modified: May 11, 2016
This is version 148 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.