TENR_CHICK
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 03-AUG-2022, entry version 135.
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; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 579-586
RP AND 827-840, DEVELOPMENTAL STAGE, SUBUNIT, AND TISSUE 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: similarity
RT with EGF-, fibronectin type III-, and fibrinogen-like 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 of
RT 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 axonin-1,
RT F11, and tenascin-R, which promote attachment and neurite formation of
RT 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, is
RT 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., Chiquet-Ehrismann R.,
RA 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 after
RT 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 in
CC cell attachment and neurite formation. Interaction with CNTN1 enhances
CC the neurite outgrowth. {ECO:0000269|PubMed:7615642}.
CC -!- SUBUNIT: Forms homodimers and homotrimers. Interacts with CNTN1, NFASC
CC and CSPG5. {ECO:0000269|PubMed:11069908, ECO:0000269|PubMed:1375037,
CC ECO:0000269|PubMed:7615642, ECO:0000269|PubMed:9049254,
CC 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, reaches
CC 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 formation
CC of oligomers. The fibronectin type-III 2-3 mediate the binding to
CC contactin 1. The fibronectin type-III 9 mediates the cell attachment.
CC The fibronectin type-III 2-5 mediate NFASC binding. The fibrinogen C-
CC terminal domain mediates interaction with CSPG5.
CC {ECO:0000269|PubMed:11069908}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; X64649; CAA45920.1; -; mRNA.
DR PIR; JH0675; JH0675.
DR RefSeq; NP_990607.2; NM_205276.3.
DR AlphaFoldDB; 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 VEuPathDB; HostDB:geneid_396213; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q00546; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q00546; -.
DR PRO; PR:Q00546; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
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 Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
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; 1.
DR Pfam; PF18720; EGF_Tenascin; 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;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1353
FT /note="Tenascin-R"
FT /id="PRO_0000007750"
FT DOMAIN 187..198
FT /note="EGF-like 1"
FT DOMAIN 234..260
FT /note="EGF-like 2"
FT DOMAIN 265..291
FT /note="EGF-like 3"
FT DOMAIN 292..323
FT /note="EGF-like 4"
FT DOMAIN 327..419
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 420..504
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 505..594
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 595..686
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 687..776
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 777..863
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 864..952
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 953..1037
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1038..1126
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1124..1339
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 132..156
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 313..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 90..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1375037"
FT /id="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
