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Database: UniProt
Entry: Q00546
LinkDB: Q00546
Original site: Q00546 
ID   TENR_CHICK              Reviewed;        1353 AA.
AC   Q00546;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-APR-2019, entry version 123.
DE   RecName: Full=Tenascin-R;
DE            Short=TN-R;
DE   AltName: Full=Restrictin;
DE   Flags: Precursor;
GN   Name=TNR;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
RP   579-586 AND 827-840, DEVELOPMENTAL STAGE, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=1375037; DOI=10.1016/0896-6273(92)90199-N;
RA   Noerenberg U., Wille H., Wolff J.M., Frank R., Rathjen F.G.;
RT   "The chicken neural extracellular matrix molecule restrictin:
RT   similarity with EGF-, fibronectin type III-, and fibrinogen-like
RT   motifs.";
RL   Neuron 8:849-863(1992).
RN   [2]
RP   INTERACTION WITH CNTN1, FUNCTION, AND CELL ATTACHMENT SITE.
RX   PubMed=7615642; DOI=10.1083/jcb.130.2.473;
RA   Noerenberg U., Hubert M., Bruemmendorf T., Tarnok A., Rathjen F.G.;
RT   "Characterization of functional domains of the tenascin-R (restrictin)
RT   polypeptide: cell attachment site, binding with F11, and enhancement
RT   of F11-mediated neurite outgrowth by tenascin-R.";
RL   J. Cell Biol. 130:473-484(1995).
RN   [3]
RP   INTERACTION WITH NFASC.
RX   PubMed=9722619; DOI=10.1083/jcb.142.4.1083;
RA   Volkmer H., Zacharias U., Noerenberg U., Rathjen F.G.;
RT   "Dissection of complex molecular interactions of neurofascin with
RT   axonin-1, F11, and tenascin-R, which promote attachment and neurite
RT   formation of tectal cells.";
RL   J. Cell Biol. 142:1083-1093(1998).
RN   [4]
RP   INTERACTION WITH CSPG5.
RX   PubMed=9049254; DOI=10.1083/jcb.136.4.895;
RA   Schumacher S., Volkmer H., Buck F., Otto A., Tarnok A., Roth S.,
RA   Rathjen F.G.;
RT   "Chicken acidic leucine-rich EGF-like domain containing brain protein
RT   (CALEB), a neural member of the EGF family of differentiation factors,
RT   is implicated in neurite formation.";
RL   J. Cell Biol. 136:895-906(1997).
RN   [5]
RP   INTERACTION WITH CSPG5, AND DOMAIN.
RX   PubMed=11069908; DOI=10.1074/jbc.M007234200;
RA   Schumacher S., Jung M., Noerenberg U., Dorner A.,
RA   Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.;
RT   "CALEB binds via its acidic stretch to the fibrinogen-like domain of
RT   tenascin-C or tenascin-R and its expression is dynamically regulated
RT   after optic nerve lesion.";
RL   J. Biol. Chem. 276:7337-7345(2001).
CC   -!- FUNCTION: Neural extracellular matrix (ECM) protein involved in
CC       interactions with different cells and matrix components. Involved
CC       in cell attachment and neurite formation. Interaction with CNTN1
CC       enhances the neurite outgrowth. {ECO:0000269|PubMed:7615642}.
CC   -!- SUBUNIT: Forms homodimers and homotrimers. Interacts with CNTN1,
CC       NFASC and CSPG5. {ECO:0000269|PubMed:11069908,
CC       ECO:0000269|PubMed:1375037, ECO:0000269|PubMed:7615642,
CC       ECO:0000269|PubMed:9049254, ECO:0000269|PubMed:9722619}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix. Note=May be attach to the cell surface of neural cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q00546-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q00546-2; Sequence=VSP_012996;
CC   -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:1375037}.
CC   -!- DEVELOPMENTAL STAGE: Expression weakly detectable at E6 embryo,
CC       reaches a maximum at E16 and declines in the adult.
CC       {ECO:0000269|PubMed:1375037}.
CC   -!- DOMAIN: The N-terminus cysteine-rich segment may mediate the
CC       formation of oligomers. The fibronectin type-III 2-3 mediate the
CC       binding to contactin 1. The fibronectin type-III 9 mediates the
CC       cell attachment. The fibronectin type-III 2-5 mediate NFASC
CC       binding. The fibrinogen C-terminal domain mediates interaction
CC       with CSPG5. {ECO:0000269|PubMed:11069908}.
CC   -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
DR   EMBL; X64649; CAA45920.1; -; mRNA.
DR   PIR; JH0675; JH0675.
DR   RefSeq; NP_990607.2; NM_205276.3.
DR   UniGene; Gga.711; -.
DR   ProteinModelPortal; Q00546; -.
DR   SMR; Q00546; -.
DR   STRING; 9031.ENSGALP00000042383; -.
DR   PaxDb; Q00546; -.
DR   PRIDE; Q00546; -.
DR   GeneID; 396213; -.
DR   KEGG; gga:396213; -.
DR   CTD; 7143; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2579; Eukaryota.
DR   eggNOG; ENOG410ZYS4; LUCA.
DR   HOGENOM; HOG000234355; -.
DR   HOVERGEN; HBG008949; -.
DR   InParanoid; Q00546; -.
DR   KO; K06252; -.
DR   OrthoDB; 18592at2759; -.
DR   PhylomeDB; Q00546; -.
DR   PRO; PR:Q00546; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0050767; P:regulation of neurogenesis; IEA:InterPro.
DR   CDD; cd00063; FN3; 9.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 2.60.40.10; -; 9.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR033079; TNR.
DR   PANTHER; PTHR19143:SF254; PTHR19143:SF254; 4.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 9.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF49265; SSF49265; 5.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Coiled coil; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34   1353       Tenascin-R.
FT                                /FTId=PRO_0000007750.
FT   DOMAIN      187    198       EGF-like 1.
FT   DOMAIN      234    260       EGF-like 2.
FT   DOMAIN      265    291       EGF-like 3.
FT   DOMAIN      292    323       EGF-like 4.
FT   DOMAIN      327    419       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      420    504       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      505    594       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      595    686       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      687    776       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      777    863       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      864    952       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      953   1037       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1038   1126       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1124   1339       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   COILED      132    156       {ECO:0000255}.
FT   COMPBIAS    154    313       Cys-rich.
FT   CARBOHYD    179    179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    197    197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    277    277       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    580    580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    734    734       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    790    790       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    872    872       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1031   1031       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1041   1041       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1256   1256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1342   1342       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    296    306       {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   DISULFID    313    322       {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   VAR_SEQ      90    134       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1375037}.
FT                                /FTId=VSP_012996.
SQ   SEQUENCE   1353 AA;  148280 MW;  CD8393C4203171D9 CRC64;
     MGTDSENPVL RNVLISFNLL LLGAVLKPFE CRLEVTTEPA ERPAVDEEGG LANCSPPVKE
     QPMVFHHIYN INVPVDSCCS SMLRSSAEEV SSEDDRLAEY TEQTSDSESQ VTFTHRINLP
     KQACKCSTSL PSLQELLSRI EMLEREVSML RDQCNSNCCQ ENAATGRLDY TLPCSGHGNF
     SLESCRCICS EGWAGSNCSE PRCPRGCSSR GVCLEGQCVC DNDYGGEDCS QLRCPAGCGS
     RGLCVDGECI CEEGFGGEDC SQPRCPRDCS GRGHCDNGTC VCAEGYAGED CGWLRCPNAC
     SGRGVCQDGL CICEDGYGGQ DCSAVAPPEN LRVTGISDGS IELAWDSLGA ATEYVVSYQP
     AGPGGSQLQQ RVPGDWSTIT ITELEPGVAY NVSIYAVISD VLSSPVTTKV TTNLATPQGL
     KFKTITETTV EVQWEPFSFP FDGWEISFIP KNNEGGVIAQ LPSTVTTFNQ TGLKPGEEYT
     VTVVALKDQA RSPPASDSIS TLIDGPTQIL VRDVSDTVAF VEWTPPRARV DAILLKYGLA
     DGEGGRTTFR LQPPLSQYSL QALRPGARYH LAVSALRGAN ESQPALAQFT TEIDAPKNLR
     VGSRTPASLE LTWDNSEAEA HSYRVVYSTL AGEHYHEVLV PRDTGPTTRA TLADLVPGTE
     YGIGISAVMD SQQSVPATMN ARTELDSPRD LLVTASTETS ISLSWTKAMG PIDHYRVTFT
     PASGMASEVT VSRNESQLTL SELEPGTEYT ISIIAERGRQ QSLEATVDAF TGVRPITQLH
     FSQLTSSSVN ITWSDPSPPA DRLVLTYSPR DEEAPQQLAL DGTRRHASLT GLRPSTEYLV
     SLVAVHGAVS SEPVTGSITT GMDAPKDLRV GNITQDSMVI YWSPPVAPFD HYRISYRAAE
     GRTDSTAIGN DATEYIMRLL QPATKYEIGV KSVRGREESE VASITTYTAM DAPLGVTATN
     ITPTEALLQW NPPLMDVESY VLVLTRHTGE TILVDGINQE YQLTNLQPST TYTVAMYATN
     GPLTSQTIST NFTTLLDPPT NLTASEVTRR SALLSWVPPV GDIENYILTY RSTDGSRKEL
     IVDAEDTWIR LEGLSETTQY TVRLQAAQNA MRSGFISTTF TTGGRVFANP QDCAQHLMNG
     DTLSGVYTIS INGDLSQRVQ VFCDMSTDGG GWIVFQRRQN GLTDFFRKWA DYRVGFGNLE
     DEFWLGLDNI HKITSQGRYE LRIDMRDGQE AAYAYYDKFS VGDSRSLYKL RIGDYNGTSG
     DSLTYHQGRP FSTKDRDNDV AVTNCAMSYK GAWWYKNCHR TNLNGKYGES RHSQGINWYH
     WKGHEFSIPF VEMKMRPYNH RNISGRKRRS LQL
//
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