TENR_RAT
ID TENR_RAT Reviewed; 1356 AA.
AC Q05546;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Tenascin-R;
DE Short=TN-R;
DE AltName: Full=Janusin;
DE AltName: Full=Neural recognition molecule J1-160/180;
DE AltName: Full=Restrictin;
DE Flags: Precursor;
GN Name=Tnr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=7679676; DOI=10.1083/jcb.120.5.1237;
RA Fuss B., Wintergerst E.-S., Bartsch U., Schachner M.;
RT "Molecular characterization and in situ mRNA localization of the neural
RT recognition molecule J1-160/180: a modular structure similar to tenascin.";
RL J. Cell Biol. 120:1237-1249(1993).
RN [2]
RP INTERACTION WITH CNTN1.
RX PubMed=9081628; DOI=10.1111/j.1460-9568.1996.tb01262.x;
RA Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M.;
RT "Distinct effects of recombinant tenascin-R domains in neuronal cell
RT functions and identification of the domain interacting with the neuronal
RT recognition molecule F3/11.";
RL Eur. J. Neurosci. 8:766-782(1996).
RN [3]
RP INTERACTION WITH BCAN.
RX PubMed=9294172; DOI=10.1073/pnas.94.19.10116;
RA Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D.,
RA Schachner M., Ruoslahti E., Yamaguchi Y.;
RT "The C-type lectin domains of lecticans, a family of aggregating
RT chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein
RT interactions independent of carbohydrate moiety.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10116-10121(1997).
RN [4]
RP INTERACTION WITH SCN2B, AND FUNCTION.
RX PubMed=9861042; DOI=10.1073/pnas.95.26.15753;
RA Srinivasan J., Schachner M., Catterall W.A.;
RT "Interaction of voltage-gated sodium channels with the extracellular matrix
RT molecules tenascin-C and tenascin-R.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15753-15757(1998).
RN [5]
RP INTERACTION WITH PTPRZ1 AND CSPG3.
RX PubMed=9507007; DOI=10.1074/jbc.273.12.6998;
RA Milev P., Chiba A., Haring M., Rauvala H., Schachner M., Ranscht B.,
RA Margolis R.K., Margolis R.U.;
RT "High affinity binding and overlapping localization of neurocan and
RT phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R,
RT amphoterin, and the heparin-binding growth-associated molecule.";
RL J. Biol. Chem. 273:6998-7005(1998).
RN [6]
RP GLYCOSYLATION, AND FUNCTION.
RX PubMed=10723065;
RX DOI=10.1002/(sici)1097-4547(20000401)60:1<21::aid-jnr3>3.0.co;2-h;
RA Probstmeier R., Stichel C.C., Muller H.W., Asou H., Pesheva P.;
RT "Chondroitin sulfates expressed on oligodendrocyte-derived tenascin-R are
RT involved in neural cell recognition. Functional implications during CNS
RT development and regeneration.";
RL J. Neurosci. Res. 60:21-36(2000).
RN [7]
RP GLYCOSYLATION.
RX PubMed=12393878; DOI=10.1074/jbc.m209876200;
RA Woodworth A., Fiete D., Baenziger J.U.;
RT "Spatial and temporal regulation of tenascin-R glycosylation in the
RT cerebellum.";
RL J. Biol. Chem. 277:50941-50947(2002).
RN [8]
RP GLYCOSYLATION, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=14681222; DOI=10.1074/jbc.m312466200;
RA Woodworth A., Pesheva P., Fiete D., Baenziger J.U.;
RT "Neuronal-specific synthesis and glycosylation of tenascin-R.";
RL J. Biol. Chem. 279:10413-10421(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION BY INJURY.
RX PubMed=28270793; DOI=10.3389/fneur.2017.00049;
RA Lindholm T., Risling M., Carlstedt T., Hammarberg H., Wallquist W.,
RA Cullheim S., Skoeld M.K.;
RT "Expression of Semaphorins, Neuropilins, VEGF, and Tenascins in Rat and
RT Human Primary Sensory Neurons after a Dorsal Root Injury.";
RL Front. Neurol. 8:49-49(2017).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 489-771, AND INTERACTION WITH
RP ACAN.
RX PubMed=15296743; DOI=10.1016/j.str.2004.05.021;
RA Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A.,
RA Logan D.T.;
RT "Structural basis for interactions between tenascins and lectican C-type
RT lectin domains: evidence for a crosslinking role for tenascins.";
RL Structure 12:1495-1506(2004).
CC -!- FUNCTION: Neural extracellular matrix (ECM) protein involved in
CC interactions with different cells and matrix components. Theses
CC interactions can influence cellular behavior by either evoking a stable
CC adhesion and differentiation, or repulsion and inhibition of neurite
CC growth. Binding to cell surface gangliosides inhibits RGD-dependent
CC integrin-mediated cell adhesion and results in an inhibition of
CC PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to
CC membrane surface sulfatides results in a oligodendrocyte adhesion and
CC differentiation. Interaction with CNTN1 induces a repulsion of neurons
CC and an inhibition of neurite outgrowth. Interacts with SCN2B may play a
CC crucial role in clustering and regulation of activity of sodium
CC channels at nodes of Ranvier. TNR-linked chondroitin sulfate
CC glycosaminoglycans are involved in the interaction with FN1 and
CC mediates inhibition of cell adhesion and neurite outgrowth. The highly
CC regulated addition of sulfated carbohydrate structure may modulate the
CC adhesive properties of TNR over the course of development and during
CC synapse maintenance (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10723065, ECO:0000269|PubMed:14681222,
CC ECO:0000269|PubMed:9861042}.
CC -!- SUBUNIT: Forms oligomers. Interacts with TNC and FN1 (By similarity).
CC Interacts with BCAN and ACAN in a calcium -dependent manner. Interacts
CC with CNTN1, SCN2B, PTPRZ1, and CSPG3. {ECO:0000250,
CC ECO:0000269|PubMed:15296743, ECO:0000269|PubMed:9081628,
CC ECO:0000269|PubMed:9294172, ECO:0000269|PubMed:9507007,
CC ECO:0000269|PubMed:9861042}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TN-R 180, 180 kDa form;
CC IsoId=Q05546-1; Sequence=Displayed;
CC Name=2; Synonyms=TN-R 160, 160 kDa form;
CC IsoId=Q05546-2; Sequence=VSP_012995;
CC -!- TISSUE SPECIFICITY: Brain-specific (PubMed:7679676). Expressed in
CC oligodendrocytes and small subsets of neurons (mainly interneurons and
CC motoneurons) of the cerebellum, hippocampus and olfactory bulb
CC (PubMed:7679676). Expressed in dorsal root ganglia (PubMed:28270793).
CC {ECO:0000269|PubMed:28270793, ECO:0000269|PubMed:7679676}.
CC -!- DEVELOPMENTAL STAGE: Expression in oligodendrocytes is highest between
CC the second and third postnatal week and low in the adult. In contrast
CC the expression in neurons increases from birth to third postnatal week
CC and is continuous from late development to adulthood. Isoform 1 is the
CC dominant form early in development. Isoform 2 is more prominent later
CC in development and in adulthood. {ECO:0000269|PubMed:14681222,
CC ECO:0000269|PubMed:7679676}.
CC -!- INDUCTION: Transiently increased in dorsal root ganglia 1 day post-
CC dorsal rhizotomy, returning to comparable levels 3 days post-injury
CC (PubMed:28270793). Increased in dorsal root ganglia in response to both
CC sciatic nerve crush and transection injury (PubMed:28270793).
CC {ECO:0000269|PubMed:28270793}.
CC -!- DOMAIN: The EGF-like domains mediate interaction with CNTN1. The
CC fibronectin type-III domains 3-5 mediate interaction with BCAN. The
CC fibronectin type-III domains 1-2 and 7-9 mediate interaction with
CC SCN2B.
CC -!- PTM: Contains N-linked oligosaccharides, O-linked sialylated structures
CC (By similarity). Contains O-linked chondroitin sulfate
CC glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated
CC carbohydrate structure type GalNAc-4-SO4 or HNK-1 (SO4-3-
CC GlcUABeta1,3GalBeta1,4GlcNAc). The levels of HNK-1 rise and fall in
CC parallel to those of TNR during postnatal development of the
CC cerebellum. In contrast, levels of GalNAc-4-SO4 are regulated
CC independently from those of TNR, rising late in cerebellar development
CC and continuing into adulthood. Early in postnatal development, GalNAc-
CC 4-SO4 is found predominantly on isoform 1, whereas in the adult it is
CC predominantly on isoform 2. {ECO:0000250, ECO:0000269|PubMed:10723065,
CC ECO:0000269|PubMed:12393878, ECO:0000269|PubMed:14681222}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; Z18630; CAA79229.1; -; mRNA.
DR PIR; A45445; A45445.
DR RefSeq; NP_037177.1; NM_013045.1. [Q05546-1]
DR PDB; 1TDQ; X-ray; 2.60 A; A=502-771.
DR PDBsum; 1TDQ; -.
DR AlphaFoldDB; Q05546; -.
DR SMR; Q05546; -.
DR BioGRID; 247598; 2.
DR IntAct; Q05546; 2.
DR MINT; Q05546; -.
DR STRING; 10116.ENSRNOP00000068101; -.
DR GlyGen; Q05546; 13 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q05546; -.
DR PhosphoSitePlus; Q05546; -.
DR PRIDE; Q05546; -.
DR GeneID; 25567; -.
DR KEGG; rno:25567; -.
DR CTD; 7143; -.
DR RGD; 3886; Tnr.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q05546; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q05546; -.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR EvolutionaryTrace; Q05546; -.
DR PRO; PR:Q05546; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0072534; C:perineuronal net; ISO:RGD.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0090733; C:tenascin complex; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:RGD.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; ISO:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; TAS:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISO:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0022029; P:telencephalon cell migration; ISO:RGD.
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; 3.
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 3D-structure; Alternative splicing; Cell adhesion; Coiled coil;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Sialic acid; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1356
FT /note="Tenascin-R"
FT /id="PRO_0000007749"
FT DOMAIN 188..199
FT /note="EGF-like 1"
FT DOMAIN 204..230
FT /note="EGF-like 2"
FT DOMAIN 235..261
FT /note="EGF-like 3"
FT DOMAIN 281..292
FT /note="EGF-like 4"
FT DOMAIN 293..324
FT /note="EGF-like 5"
FT DOMAIN 328..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..596
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 597..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..864
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 865..953
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 954..1040
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1041..1129
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1127..1342
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 127..157
FT /evidence="ECO:0000255"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
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 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 297..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 314..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 772..861
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7679676"
FT /id="VSP_012995"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 531..543
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 568..577
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 597..604
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 621..629
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 644..652
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 689..696
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 713..720
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 727..734
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 736..740
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 749..757
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:1TDQ"
SQ SEQUENCE 1356 AA; 149371 MW; 9BFE2BF7AD4CA781 CRC64;
MGIEGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERV QRQTVEEEGG ASSYNTSSKE
QPMVFNHVYN INVPLESLCS SGLEASAEQD VSAEDDTLAE YTGQTSDHES QVTFTHKINL
PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNTNCC QESAATGQLD YVPHCSGHGN
FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS
SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA
CSGRGHCQEG LCICEEGYQG PDCSAVTPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ
PSLGGLQLQQ RVPGDWSGVT ITELEPGLTY NISVYAVISN ILSLPITAKV ATHLSTPQGL
QFKTITETTV EVQWEPFSFS FDGWEISFTP KNNEGGVIAQ LPSDVTSFNQ TGLKPGEEYI
VNVVALKEQA RGPPTSASVS TVIDGPTQIL VRDVSDTVAF VEWTPPRAKV DFILLKYGLV
GGEGGKTTFR LQPPLSQYSV QALRPGSRYE VSISAVRGTN ESDASSTQFT TEIDAPKNLR
VGSRTATSLD LEWDNSEAEA QEYKVVYSTL AGEQYHEVLV PKGIGPTTKT TLTDLVPGTE
YGVGISAVMN SKQSIPATMN ARTELDSPRD LMVTASSETS ISLIWTKASG PIDHYRITFT
PSSGISSEVT VPRDRTSYTL TDLEPGAEYI ISITAERGRQ QSLESTVDAF TGFRPISHLH
FSHVTSSSVN ITWSDPSPPA DRLILNYSPR DEEEEMMEVL LDATKRHAVL MGLQPATEYI
VNLVAVHGTV TSEPIVGSIT TGIDPPKNIT ISNVTKDSLT VSWSPPVAPF DYYEYPIDHP
SGRLDSSVVP NTVTEFTITR LYPASQYEIS LNSVRGREES ERICTLVHTA MDSPMDLIAT
NITPTEALLQ WKAPMGEVEN YVIVLTHFAM AGETILVDGV SEEFQLVDLL PRTHYTVTMY
ATSGPLVSGT IATNFSTLLD PPANLTASEV TRQSALISWQ PPRAAIENYV LTYKSTDGSR
KELIVDAEDT WIRLEGLSEN TDYTVLLQAA QEATRSSLTS TIFTTGGRVF SHPQDCAQHL
MNGDTLSGVY TIFLNGELSH KLQVYCDMTT DGGGWIVFQR RQNGQTDFFR KWADYRVGFG
NLEDEFWLGL DNYHRITAQG RYELRVDMRD GQEAVFAYYD KFAVEDSRSL YKLRIGGYNG
TAGDSLSYHQ GRPFSTEDRD NDVAVTNCAM SYKGAWWYKN CHRTNLNGKY GESRHSQGIN
WYHWKGHEFS IPFVEMKMRP YIHRLTAGRK RRALKF
