ID   TENN_HUMAN              Reviewed;        1299 AA.
AC   Q9UQP3; A0A0A6YY94; B9EGP3; Q5R360;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Tenascin-N {ECO:0000312|HGNC:HGNC:22942};
DE            Short=TN-N;
DE   AltName: Full=Tenascin-W {ECO:0000303|PubMed:17909022};
DE            Short=TN-W;
DE   Flags: Precursor;
GN   Name=TNN {ECO:0000312|HGNC:HGNC:22942};
GN   Synonyms=TNW {ECO:0000303|PubMed:17909022};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000312|EMBL:CAB41260.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1299.
RA   Rhodes S.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1149.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17909022; DOI=10.1158/0008-5472.can-07-0666;
RA   Degen M., Brellier F., Kain R., Ruiz C., Terracciano L., Orend G.,
RA   Chiquet-Ehrismann R.;
RT   "Tenascin-W is a novel marker for activated tumor stroma in low-grade human
RT   breast cancer and influences cell behavior.";
RL   Cancer Res. 67:9169-9179(2007).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=19884327; DOI=10.1096/fj.09-140491;
RA   Martina E., Degen M., Rueegg C., Merlo A., Lino M.M., Chiquet-Ehrismann R.,
RA   Brellier F.;
RT   "Tenascin-W is a specific marker of glioma-associated blood vessels and
RT   stimulates angiogenesis in vitro.";
RL   FASEB J. 24:778-787(2010).
CC   -!- FUNCTION: Extracellular matrix protein that seems to be a ligand for
CC       ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity)
CC       (PubMed:17909022). Involved in neurite outgrowth and cell migration in
CC       hippocampal explants (By similarity). During endochondral bone
CC       formation, inhibits proliferation and differentiation of proteoblasts
CC       mediated by canonical WNT signaling (By similarity). In tumors,
CC       stimulates angiogenesis by elongation, migration and sprouting of
CC       endothelial cells (PubMed:19884327). Expressed in most mammary tumors,
CC       may facilitate tumorigenesis by supporting the migratory behavior of
CC       breast cancer cells (PubMed:17909022). {ECO:0000250|UniProtKB:Q80YX1,
CC       ECO:0000250|UniProtKB:Q80Z71, ECO:0000269|PubMed:17909022,
CC       ECO:0000269|PubMed:19884327}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q80Z71}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:19884327}.
CC   -!- TISSUE SPECIFICITY: Not detected in normal adult mammary tissues or
CC       brain but expressed in most breast tumors and brain tumors, such as
CC       glioblastomas, astrocytomas and oligodendrogliomas, tested
CC       (PubMed:17909022, PubMed:19884327). In brain tumors, detected around
CC       the endothelial cell layer of the clood vessels (PubMed:19884327).
CC       {ECO:0000269|PubMed:17909022, ECO:0000269|PubMed:19884327}.
CC   -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44209/TNN";
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DR   EMBL; Z99297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z99715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC136619; AAI36620.1; -; mRNA.
DR   EMBL; AL049689; CAB41260.1; -; mRNA.
DR   CCDS; CCDS30943.1; -.
DR   RefSeq; NP_071376.1; NM_022093.1.
DR   AlphaFoldDB; Q9UQP3; -.
DR   SMR; Q9UQP3; -.
DR   BioGRID; 121992; 5.
DR   ComplexPortal; CPX-1012; Tenascin-W complex.
DR   IntAct; Q9UQP3; 1.
DR   STRING; 9606.ENSP00000239462; -.
DR   GlyConnect; 1793; 11 N-Linked glycans (3 sites).
DR   GlyCosmos; Q9UQP3; 4 sites, 13 glycans.
DR   GlyGen; Q9UQP3; 4 sites, 12 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UQP3; -.
DR   PhosphoSitePlus; Q9UQP3; -.
DR   BioMuta; TNN; -.
DR   DMDM; 81175198; -.
DR   EPD; Q9UQP3; -.
DR   jPOST; Q9UQP3; -.
DR   MassIVE; Q9UQP3; -.
DR   PaxDb; 9606-ENSP00000239462; -.
DR   PeptideAtlas; Q9UQP3; -.
DR   ProteomicsDB; 85562; -.
DR   ABCD; Q9UQP3; 3 sequenced antibodies.
DR   Antibodypedia; 4397; 123 antibodies from 27 providers.
DR   DNASU; 63923; -.
DR   Ensembl; ENST00000239462.9; ENSP00000239462.4; ENSG00000120332.17.
DR   GeneID; 63923; -.
DR   KEGG; hsa:63923; -.
DR   MANE-Select; ENST00000239462.9; ENSP00000239462.4; NM_022093.2; NP_071376.1.
DR   UCSC; uc001gkl.1; human.
DR   AGR; HGNC:22942; -.
DR   CTD; 63923; -.
DR   DisGeNET; 63923; -.
DR   GeneCards; TNN; -.
DR   HGNC; HGNC:22942; TNN.
DR   HPA; ENSG00000120332; Tissue enhanced (adipose tissue, breast).
DR   MIM; 617472; gene.
DR   neXtProt; NX_Q9UQP3; -.
DR   OpenTargets; ENSG00000120332; -.
DR   PharmGKB; PA134973710; -.
DR   VEuPathDB; HostDB:ENSG00000120332; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000160553; -.
DR   InParanoid; Q9UQP3; -.
DR   OMA; EAPIDRY; -.
DR   OrthoDB; 4173903at2759; -.
DR   PhylomeDB; Q9UQP3; -.
DR   TreeFam; TF329915; -.
DR   PathwayCommons; Q9UQP3; -.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   SignaLink; Q9UQP3; -.
DR   BioGRID-ORCS; 63923; 10 hits in 1148 CRISPR screens.
DR   ChiTaRS; TNN; human.
DR   GenomeRNAi; 63923; -.
DR   Pharos; Q9UQP3; Tbio.
DR   PRO; PR:Q9UQP3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UQP3; Protein.
DR   Bgee; ENSG00000120332; Expressed in periodontal ligament and 80 other cell types or tissues.
DR   ExpressionAtlas; Q9UQP3; baseline and differential.
DR   GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:1990026; C:hippocampal mossy fiber expansion; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0090733; C:tenascin complex; IPI:ComplexPortal.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0070593; P:dendrite self-avoidance; ISA:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:2001223; P:negative regulation of neuron migration; ISA:UniProtKB.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
DR   GO; GO:1990138; P:neuron projection extension; IBA:GO_Central.
DR   GO; GO:0002076; P:osteoblast development; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:ComplexPortal.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:ComplexPortal.
DR   GO; GO:1903010; P:regulation of bone development; ISO:ComplexPortal.
DR   GO; GO:0030155; P:regulation of cell adhesion; IDA:ComplexPortal.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:ComplexPortal.
DR   GO; GO:1905899; P:regulation of smooth muscle tissue development; ISO:ComplexPortal.
DR   CDD; cd00035; ChtBD1; 1.
DR   CDD; cd00063; FN3; 9.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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; IPR020837; Fibrinogen_CS.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR46708; TENASCIN; 1.
DR   PANTHER; PTHR46708:SF5; TENASCIN N; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF18720; EGF_Tenascin; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 9.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
DR   Genevisible; Q9UQP3; HS.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1299
FT                   /note="Tenascin-N"
FT                   /id="PRO_0000007745"
FT   DOMAIN          167..198
FT                   /note="EGF-like 1"
FT   DOMAIN          199..229
FT                   /note="EGF-like 2"
FT   DOMAIN          230..260
FT                   /note="EGF-like 3"
FT   DOMAIN          264..352
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          353..444
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          445..532
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          533..623
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          624..709
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          710..800
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          801..886
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          887..976
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          977..1063
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1061..1278
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          605..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        1149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   DISULFID        171..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        175..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        202..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        206..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        233..243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        237..248
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        250..259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   VARIANT         79
FT                   /note="R -> G (in dbSNP:rs2072032)"
FT                   /id="VAR_049007"
FT   VARIANT         289
FT                   /note="D -> N (in dbSNP:rs16847812)"
FT                   /id="VAR_033832"
FT   VARIANT         440
FT                   /note="R -> S (in dbSNP:rs6664276)"
FT                   /id="VAR_049008"
FT   VARIANT         499
FT                   /note="T -> M (in dbSNP:rs17374761)"
FT                   /id="VAR_033833"
FT   VARIANT         807
FT                   /note="W -> R (in dbSNP:rs6696455)"
FT                   /id="VAR_033834"
FT   VARIANT         859
FT                   /note="M -> V (in dbSNP:rs6694078)"
FT                   /id="VAR_059275"
FT   VARIANT         930
FT                   /note="P -> L (in dbSNP:rs2285215)"
FT                   /id="VAR_024269"
FT   VARIANT         941
FT                   /note="T -> M (in dbSNP:rs10798333)"
FT                   /id="VAR_033835"
FT   VARIANT         1135
FT                   /note="D -> E (in dbSNP:rs10158841)"
FT                   /id="VAR_049009"
FT   VARIANT         1156
FT                   /note="A -> V (in dbSNP:rs2072036)"
FT                   /id="VAR_049010"
SQ   SEQUENCE   1299 AA;  144034 MW;  CC4BBD5CE47ADBED CRC64;
     MSLQEMFRFP MGLLLGSVLL VASAPATLEP PGCSNKEQQV TVSHTYKIDV PKSALVQVDA
     DPQPLSDDGA SLLALGEARE EQNIIFRHNI RLQTPQKDCE LAGSVQDLLA RVKKLEEEMV
     EMKEQCSAQR CCQGVTDLSR HCSGHGTFSL ETCSCHCEEG REGPACERLA CPGACSGHGR
     CVDGRCLCHE PYVGADCGYP ACPENCSGHG ECVRGVCQCH EDFMSEDCSE KRCPGDCSGH
     GFCDTGECYC EEGFTGLDCA QVVTPQGLQL LKNTEDSLLV SWEPSSQVDH YLLSYYPLGK
     ELSGKQIQVP KEQHSYEILG LLPGTKYIVT LRNVKNEVSS SPQHLLATTD LAVLGTAWVT
     DETENSLDVE WENPSTEVDY YKLRYGPMTG QEVAEVTVPK SSDPKSRYDI TGLHPGTEYK
     ITVVPMRGEL EGKPILLNGR TEIDSPTNVV TDRVTEDTAT VSWDPVQAVI DKYVVRYTSA
     DGDTKEMAVH KDESSTVLTG LKPGEAYKVY VWAERGNQGS KKADTNALTE IDSPANLVTD
     RVTENTATIS WDPVQATIDK YVVRYTSADD QETREVLVGK EQSSTVLTGL RPGVEYTVHV
     WAQKGDRESK KADTNAPTDI DSPKNLVTDR VTENMATVSW DPVQAAIDKY VVRYTSAGGE
     TREVPVGKEQ SSTVLTGLRP GMEYMVHVWA QKGDQESKKA DTKAQTDIDS PQNLVTDRVT
     ENMATVSWDP VRATIDRYVV RYTSAKDGET REVPVGKEQS STVLTGLRPG VEYTVHVWAQ
     KGAQESKKAD TKAQTDIDSP QNLVTDWVTE NTATVSWDPV QATIDRYVVH YTSANGETRE
     VPVGKEQSST VLTGLRPGME YTVHVWAQKG NQESKKADTK AQTEIDGPKN LVTDWVTENM
     ATVSWDPVQA TIDKYMVRYT SADGETREVP VGKEHSSTVL TGLRPGMEYM VHVWAQKGAQ
     ESKKADTKAQ TELDPPRNLR PSAVTQSGGI LTWTPPSAQI HGYILTYQFP DGTVKEMQLG
     REDQRFALQG LEQGATYPVS LVAFKGGRRS RNVSTTLSTV GARFPHPSDC SQVQQNSNAA
     SGLYTIYLHG DASRPLQVYC DMETDGGGWI VFQRRNTGQL DFFKRWRSYV EGFGDPMKEF
     WLGLDKLHNL TTGTPARYEV RVDLQTANES AYAIYDFFQV ASSKERYKLT VGKYRGTAGD
     ALTYHNGWKF TTFDRDNDIA LSNCALTHHG GWWYKNCHLA NPNGRYGETK HSEGVNWEPW
     KGHEFSIPYV ELKIRPHGYS REPVLGRKKR TLRGRLRTF
//