TENA_CHICK
ID TENA_CHICK Reviewed; 1808 AA.
AC P10039; O73584; O73585; P13132;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tenascin;
DE Short=TN;
DE AltName: Full=Cytotactin;
DE AltName: Full=GMEM;
DE AltName: Full=GP 150-225;
DE AltName: Full=Glioma-associated-extracellular matrix antigen;
DE AltName: Full=Hexabrachion;
DE AltName: Full=JI;
DE AltName: Full=Myotendinous antigen;
DE AltName: Full=Neuronectin;
DE AltName: Full=Tenascin-C;
DE Short=TN-C;
DE Flags: Precursor;
GN Name=TNC;
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; 2 AND 3).
RC TISSUE=Embryo;
RX PubMed=2478295; DOI=10.1016/0092-8674(89)90294-8;
RA Spring J., Beck K., Chiquet-Ehrismann R.;
RT "Two contrary functions of tenascin: dissection of the active sites by
RT recombinant tenascin fragments.";
RL Cell 59:325-334(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-722 (ISOFORMS 1/2/3), AND PROTEIN SEQUENCE
RP OF 79-96.
RC TISSUE=Fibroblast;
RX PubMed=2460335; DOI=10.1002/j.1460-2075.1988.tb03160.x;
RA Pearson C.A., Pearson D., Shibahara S., Hofsteenge J.,
RA Chiquet-Ehrismann R.;
RT "Tenascin: cDNA cloning and induction by TGF-beta.";
RL EMBO J. 7:2977-2982(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 464-1018 AND 1412-1661 (ISOFORMS 1/2/3), AND
RP PROTEIN SEQUENCE OF 852-868.
RC TISSUE=Embryo;
RX PubMed=2451243; DOI=10.1073/pnas.85.7.2186;
RA Jones F.S., Burgoon M.P., Hoffman S., Crossin K.L., Cunningham B.A.,
RA Edelman G.M.;
RT "A cDNA clone for cytotactin contains sequences similar to epidermal growth
RT factor-like repeats and segments of fibronectin and fibrinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2186-2190(1988).
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: Extracellular matrix protein implicated in guidance of
CC migrating neurons as well as axons during development, synaptic
CC plasticity as well as neuronal regeneration. Ligand for integrins
CC alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.
CC -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in
CC the triple coiled-coil region and may be stabilized by disulfide rings
CC at both ends. Two of such half-hexabrachions may be disulfide linked
CC within the central globule. Interacts with CSPG4.
CC {ECO:0000269|PubMed:11069908, ECO:0000269|PubMed:9049254}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms are produced in a tissue- and time-specific manner
CC during development.;
CC Name=1; Synonyms=230 kDa;
CC IsoId=P10039-1; Sequence=Displayed;
CC Name=2; Synonyms=200 kDa;
CC IsoId=P10039-2; Sequence=VSP_001410;
CC Name=3; Synonyms=190 kDa;
CC IsoId=P10039-3; Sequence=VSP_001411;
CC -!- INDUCTION: By TGF-beta.
CC -!- DOMAIN: The fibrinogen C-terminal domain mediates interaction with
CC CSPG5. {ECO:0000269|PubMed:11069908}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; M23121; AAA49086.1; -; mRNA.
DR EMBL; X08031; CAB40811.1; -; mRNA.
DR EMBL; X08030; CAA30824.1; ALT_TERM; mRNA.
DR EMBL; J03641; AAA48748.1; ALT_SEQ; mRNA.
DR EMBL; M20816; AAA48749.1; ALT_SEQ; mRNA.
DR PIR; A31930; A31930.
DR PDB; 1QR4; X-ray; 2.55 A; A/B=950-1042, A/B=1316-1408.
DR PDBsum; 1QR4; -.
DR AlphaFoldDB; P10039; -.
DR SMR; P10039; -.
DR IntAct; P10039; 1.
DR STRING; 9031.ENSGALP00000011509; -.
DR PaxDb; P10039; -.
DR PRIDE; P10039; -.
DR VEuPathDB; HostDB:geneid_396440; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; P10039; -.
DR OrthoDB; 18592at2759; -.
DR EvolutionaryTrace; P10039; -.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR CDD; cd00063; FN3; 11.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
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; IPR033078; TNC.
DR PANTHER; PTHR46708:SF1; PTHR46708:SF1; 3.
DR Pfam; PF07974; EGF_2; 3.
DR Pfam; PF18720; EGF_Tenascin; 9.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 11.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 11.
DR SUPFAM; SSF49265; SSF49265; 8.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion;
KW Cleavage on pair of basic residues; Coiled coil; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT PROPEP 23..33
FT /id="PRO_0000007743"
FT CHAIN 34..1808
FT /note="Tenascin"
FT /id="PRO_0000007744"
FT DOMAIN 176..188
FT /note="EGF-like 1; incomplete"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 188..219
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 219..250
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 250..281
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 281..312
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 312..343
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 343..374
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 374..405
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 405..436
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 436..467
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 467..498
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 498..529
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 529..560
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 560..591
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 595..685
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 686..775
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 776..866
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 867..957
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 958..1046
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1047..1138
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1139..1228
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1229..1318
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1319..1408
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1409..1495
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1496..1584
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1582..1797
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 118..142
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 192..202
FT /evidence="ECO:0000250"
FT DISULFID 196..207
FT /evidence="ECO:0000250"
FT DISULFID 209..218
FT /evidence="ECO:0000250"
FT DISULFID 223..233
FT /evidence="ECO:0000250"
FT DISULFID 227..238
FT /evidence="ECO:0000250"
FT DISULFID 240..249
FT /evidence="ECO:0000250"
FT DISULFID 254..264
FT /evidence="ECO:0000250"
FT DISULFID 258..269
FT /evidence="ECO:0000250"
FT DISULFID 271..280
FT /evidence="ECO:0000250"
FT DISULFID 285..295
FT /evidence="ECO:0000250"
FT DISULFID 289..300
FT /evidence="ECO:0000250"
FT DISULFID 302..311
FT /evidence="ECO:0000250"
FT DISULFID 316..326
FT /evidence="ECO:0000250"
FT DISULFID 320..331
FT /evidence="ECO:0000250"
FT DISULFID 333..342
FT /evidence="ECO:0000250"
FT DISULFID 347..357
FT /evidence="ECO:0000250"
FT DISULFID 351..362
FT /evidence="ECO:0000250"
FT DISULFID 364..373
FT /evidence="ECO:0000250"
FT DISULFID 378..388
FT /evidence="ECO:0000250"
FT DISULFID 382..393
FT /evidence="ECO:0000250"
FT DISULFID 395..404
FT /evidence="ECO:0000250"
FT DISULFID 409..419
FT /evidence="ECO:0000250"
FT DISULFID 413..424
FT /evidence="ECO:0000250"
FT DISULFID 426..435
FT /evidence="ECO:0000250"
FT DISULFID 440..450
FT /evidence="ECO:0000250"
FT DISULFID 444..455
FT /evidence="ECO:0000250"
FT DISULFID 457..466
FT /evidence="ECO:0000250"
FT DISULFID 471..481
FT /evidence="ECO:0000250"
FT DISULFID 475..486
FT /evidence="ECO:0000250"
FT DISULFID 488..497
FT /evidence="ECO:0000250"
FT DISULFID 502..512
FT /evidence="ECO:0000250"
FT DISULFID 506..517
FT /evidence="ECO:0000250"
FT DISULFID 519..528
FT /evidence="ECO:0000250"
FT DISULFID 533..543
FT /evidence="ECO:0000250"
FT DISULFID 537..548
FT /evidence="ECO:0000250"
FT DISULFID 550..559
FT /evidence="ECO:0000250"
FT DISULFID 564..574
FT /evidence="ECO:0000250"
FT DISULFID 568..579
FT /evidence="ECO:0000250"
FT DISULFID 581..590
FT /evidence="ECO:0000250"
FT VAR_SEQ 1043..1315
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2478295"
FT /id="VSP_001411"
FT VAR_SEQ 1043..1224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2478295"
FT /id="VSP_001410"
FT CONFLICT 182
FT /note="W -> R (in Ref. 2; CAA30824)"
FT /evidence="ECO:0000305"
FT CONFLICT 563..571
FT /note="SCPNDCNNV -> PAPMTATTW (in Ref. 3; AAA48748)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="E -> G (in Ref. 3; AAA48748)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="T -> TEY (in Ref. 3; AAA48748)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="N -> F (in Ref. 3; AAA48748)"
FT /evidence="ECO:0000305"
FT STRAND 1233..1237
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1240..1248
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1255..1262
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1268..1272
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1280..1286
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1292..1303
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1309..1314
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1323..1327
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1333..1337
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1345..1353
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1360..1365
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1370..1373
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1381..1390
FT /evidence="ECO:0007829|PDB:1QR4"
FT STRAND 1398..1403
FT /evidence="ECO:0007829|PDB:1QR4"
SQ SEQUENCE 1808 AA; 198859 MW; B924A06CF9EFD6DE CRC64;
MGLPSQVLAC AILGLLYQHA SGGLIKRIIR QKRETGLNVT LPEDNQPVVF NHVYNIKLPV
GSLCSVDLDT ASGDADLKAE IEPVKNYEEH TVNEGNQIVF THRINIPRRA CGCAAAPDIK
DLLSRLEELE GLVSSLREQC ASGAGCCPNS QTAEGRLDTA PYCSGHGNYS TEICGCVCEP
GWKGPNCSEP ACPRNCLNRG LCVRGKCICE EGFTGEDCSQ AACPSDCNDQ GKCVDGVCVC
FEGYTGPDCG EELCPHGCGI HGRCVGGRCV CHEGFTGEDC NEPLCPNNCH NRGRCVDNEC
VCDEGYTGED CGELICPNDC FDRGRCINGT CFCEEGYTGE DCGELTCPNN CNGNGRCENG
LCVCHEGFVG DDCSQKRCPK DCNNRGHCVD GRCVCHEGYL GEDCGELRCP NDCHNRGRCI
NGQCVCDEGF IGEDCGELRC PNDCHNRGRC VNGQCECHEG FIGEDCGELR CPNDCNSHGR
CVNGQCVCDE GYTGEDCGEL RCPNDCHNRG RCVEGRCVCD NGFMGEDCGE LSCPNDCHQH
GRCVDGRCVC HEGFTGEDCR ERSCPNDCNN VGRCVEGRCV CEEGYMGIDC SDVSPPTELT
VTNVTDKTVN LEWKHENLVN EYLVTYVPTS SGGLDLQFTV PGNQTSATIH ELEPGVEYFI
RVFAILKNKK SIPVSARVAT YLPAPEGLKF KSVRETSVQV EWDPLSISFD GWELVFRNMQ
KKDDNGDITS SLKRPETSYM QPGLAPGQQY NVSLHIVKNN TRGPGLSRVI TTKLDAPSQI
EAKDVTDTTA LITWSKPLAE IEGIELTYGP KDVPGDRTTI DLSEDENQYS IGNLRPHTEY
EVTLISRRGD MESDPAKEVF VTDLDAPRNL KRVSQTDNSI TLEWKNSHAN IDNYRIKFAP
ISGGDHTELT VPKGNQATTR ATLTGLRPGT EYGIGVTAVR QDRESAPATI NAGTDLDNPK
DLEVSDPTET TLSLRWRRPV AKFDRYRLTY VSPSGKKNEM EIPVDSTSFI LRGLDAGTEY
TISLVAEKGR HKSKPTTIKG STEEEPELGN LSVSETGWDG FQLTWTAADG AYENFVIQVQ
QSDNPEETWN ITVPGGQHSV NVTGLKANTP YNVTLYGVIR GYRTKPLYVE TTTGAHPEVG
ELTVSDITPE SFNLSWTTTN GDFDAFTIEI IDSNRLLEPM EFNISGNSRT AHISGLSPST
DFIVYLYGIS HGFRTQAISA AATTEAEPEV DNLLVSDATP DGFRLSWTAD DGVFDSFVLK
IRDTKRKSDP LELIVPGHER THDITGLKEG TEYEIELYGV SSGRRSQPIN SVATTVVGSP
KGISFSDITE NSATVSWTPP RSRVDSYRVS YVPITGGTPN VVTVDGSKTR TKLVKLVPGV
DYNVNIISVK GFEESEPISG ILKTALDSPS GLVVMNITDS EALATWQPAI AAVDNYIVSY
SSEDEPEVTQ MVSGNTVEYD LNGLRPATEY TLRVHAVKDA QKSETLSTQF TTGLDAPKDL
SATEVQSETA VITWRPPRAP VTDYLLTYES IDGRVKEVIL DPETTSYTLT ELSPSTQYTV
KLQALSRSMR SKMIQTVFTT TGLLYPYPKD CSQALLNGEV TSGLYTIYLN GDRTQPLQVF
CDMAEDGGGW IVFLRRQNGK EDFYRNWKNY VAGFGDPKDE FWIGLENLHK ISSQGQYELR
VDLRDRGETA YAVYDKFSVG DAKTRYRLRV DGYSGTAGDS MTYHNGRSFS TFDKDNDSAI
TNCALSYKGA FWYKNCHRVN LMGRYGDNNH SQGVNWFHWK GHEYSIQFAE MKLRPSSFRN
LEGRRKRA
