ID   TECTA_MOUSE             Reviewed;        2155 AA.
AC   O08523; E9QNR3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Alpha-tectorin;
DE   Flags: Precursor;
GN   Name=Tecta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 25-34,
RP   SUBUNIT, SUBCELLULAR LOCATION, POST-TRANSLATIONAL MODIFICATIONS, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=CD-1; TISSUE=Cochlea;
RX   PubMed=9079715; DOI=10.1074/jbc.272.13.8791;
RA   Legan P.K., Rau A., Keene J.N., Richardson G.P.;
RT   "The mouse tectorins. Modular matrix proteins of the inner ear homologous
RT   to components of the sperm-egg adhesion system.";
RL   J. Biol. Chem. 272:8791-8801(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=9590290; DOI=10.1038/ng0598-60;
RA   Verhoeven K., Van Laer L., Kirschhofer K., Legan P.K., Hughes D.C.,
RA   Schatteman I., Verstreken M., Van Hauwe P., Coucke P., Chen A.,
RA   Smith R.J.H., Somers T., Offeciers F.E., Van de Heyning P.,
RA   Richardson G.P., Wachtler F., Kimberling W.J., Willems P.J., Govaerts P.J.,
RA   Van Camp G.;
RT   "Mutations in the human alpha-tectorin gene cause autosomal dominant non-
RT   syndromic hearing impairment.";
RL   Nat. Genet. 19:60-62(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   INTERACTION WITH CEACAM16.
RX   PubMed=25080593; DOI=10.1523/jneurosci.1256-14.2014;
RA   Cheatham M.A., Goodyear R.J., Homma K., Legan P.K., Korchagina J.,
RA   Naskar S., Siegel J.H., Dallos P., Zheng J., Richardson G.P.;
RT   "Loss of the tectorial membrane protein CEACAM16 enhances spontaneous,
RT   stimulus-frequency, and transiently evoked otoacoustic emissions.";
RL   J. Neurosci. 34:10325-10338(2014).
CC   -!- FUNCTION: One of the major non-collagenous components of the tectorial
CC       membrane (By similarity). The tectorial membrane is an extracellular
CC       matrix of the inner ear that covers the neuroepithelium of the cochlea
CC       and contacts the stereocilia bundles of specialized sensory hair cells.
CC       Sound induces movement of these hair cells relative to the tectorial
CC       membrane, deflects the stereocilia and leads to fluctuations in hair-
CC       cell membrane potential, transducing sound into electrical signals.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: May form homomeric filament after self-association or
CC       heteromeric filament after association with beta-tectorin (Probable).
CC       Interacts with CEACAM16 (PubMed:25080593).
CC       {ECO:0000269|PubMed:25080593, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9079715};
CC       Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9079715}; Extracellular
CC       side {ECO:0000305|PubMed:9079715}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000269|PubMed:9079715}. Note=Found in the
CC       non-collagenous matrix of the tectorial membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O08523-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O08523-2; Sequence=VSP_010557;
CC   -!- TISSUE SPECIFICITY: Cochlea-specific. {ECO:0000269|PubMed:9079715}.
CC   -!- DOMAIN: Zona pellucida domain may enable to form filaments.
CC   -!- PTM: 3 products of tectorin seem to exist: HMM, MMM and LMM. They may
CC       be generated by active processing or the result of proteolysis
CC       occurring between intrachain disulfide bonds.
CC   -!- PTM: The presence of a hydrophobic C-terminus preceded by a potential
CC       cleavage site strongly suggests that tectorins are synthesized as
CC       glycosylphosphatidylinositol-linked, membrane-bound precursors.
CC       Tectorins are targeted to the apical surface of the inner ear epithelia
CC       by the lipid and proteolytically released into the extracellular
CC       compartment.
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DR   EMBL; X99805; CAA68138.1; -; mRNA.
DR   EMBL; AC156631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS23087.1; -. [O08523-1]
DR   CCDS; CCDS85660.1; -. [O08523-2]
DR   PIR; T30197; T30197.
DR   RefSeq; NP_001311477.1; NM_001324548.1. [O08523-2]
DR   RefSeq; NP_033373.2; NM_009347.3. [O08523-1]
DR   RefSeq; XP_017168765.1; XM_017313276.1.
DR   AlphaFoldDB; O08523; -.
DR   SMR; O08523; -.
DR   STRING; 10090.ENSMUSP00000040262; -.
DR   GlyCosmos; O08523; 31 sites, No reported glycans.
DR   GlyGen; O08523; 31 sites.
DR   PhosphoSitePlus; O08523; -.
DR   MaxQB; O08523; -.
DR   PaxDb; 10090-ENSMUSP00000040262; -.
DR   Antibodypedia; 18890; 33 antibodies from 15 providers.
DR   DNASU; 21683; -.
DR   Ensembl; ENSMUST00000042190.14; ENSMUSP00000040262.8; ENSMUSG00000037705.14. [O08523-1]
DR   Ensembl; ENSMUST00000160940.2; ENSMUSP00000125370.2; ENSMUSG00000037705.14. [O08523-2]
DR   GeneID; 21683; -.
DR   KEGG; mmu:21683; -.
DR   UCSC; uc009pau.1; mouse. [O08523-1]
DR   UCSC; uc012grn.1; mouse. [O08523-2]
DR   AGR; MGI:109575; -.
DR   CTD; 7007; -.
DR   MGI; MGI:109575; Tecta.
DR   VEuPathDB; HostDB:ENSMUSG00000037705; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   eggNOG; KOG4291; Eukaryota.
DR   GeneTree; ENSGT00950000183155; -.
DR   HOGENOM; CLU_001423_0_0_1; -.
DR   InParanoid; O08523; -.
DR   OMA; RVQTGCV; -.
DR   OrthoDB; 2872912at2759; -.
DR   PhylomeDB; O08523; -.
DR   TreeFam; TF300299; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 21683; 2 hits in 76 CRISPR screens.
DR   PRO; PR:O08523; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O08523; Protein.
DR   Bgee; ENSMUSG00000037705; Expressed in epithelium of cochlear duct and 28 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IGI:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0007605; P:sensory perception of sound; TAS:MGI.
DR   CDD; cd19941; TIL; 3.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR   Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR025615; TILa_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   PANTHER; PTHR46160:SF3; ALPHA-TECTORIN; 1.
DR   PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR   Pfam; PF08742; C8; 4.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF01826; TIL; 3.
DR   Pfam; PF12714; TILa; 2.
DR   Pfam; PF00094; VWD; 4.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00215; VWC_out; 3.
DR   SMART; SM00216; VWD; 4.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 3.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS51233; VWFD; 4.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
DR   Genevisible; O08523; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; GPI-anchor; Hearing;
KW   Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:9079715"
FT   CHAIN           25..2091
FT                   /note="Alpha-tectorin"
FT                   /id="PRO_0000041737"
FT   PROPEP          2092..2155
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000041738"
FT   DOMAIN          98..252
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          260..314
FT                   /note="VWFC"
FT   DOMAIN          320..500
FT                   /note="VWFD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          597..650
FT                   /note="TIL 1"
FT   DOMAIN          711..886
FT                   /note="VWFD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          984..1036
FT                   /note="TIL 2"
FT   DOMAIN          1098..1278
FT                   /note="VWFD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1372..1425
FT                   /note="TIL 3"
FT   DOMAIN          1485..1666
FT                   /note="VWFD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1805..2059
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   LIPID           2091
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
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        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        670
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        687
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        813
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        843
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        855
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        898
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        920
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        931
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        949
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1048
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1064
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1756
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1794
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1851
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1864
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1880
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1920
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1939
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        344..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        713..849
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1100..1241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1122..1277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1487..1622
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1509..1665
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1717..1775
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        1741..1784
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        1786..1818
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        1806..1898
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        1837..1857
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        1980..2040
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        2001..2056
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   DISULFID        2045..2052
FT                   /evidence="ECO:0000250|UniProtKB:P07911"
FT   VAR_SEQ         1659..1663
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9079715,
FT                   ECO:0000303|PubMed:9590290"
FT                   /id="VSP_010557"
FT   CONFLICT        803
FT                   /note="S -> T (in Ref. 1; CAA68138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1024
FT                   /note="A -> R (in Ref. 1; CAA68138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1032
FT                   /note="P -> T (in Ref. 1; CAA68138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1229
FT                   /note="V -> I (in Ref. 1; CAA68138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2148
FT                   /note="I -> V (in Ref. 1; CAA68138)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2155 AA;  239433 MW;  1F93E76E0FFB2C23 CRC64;
     MNYSSLLRIW VSFIFALVRH QAQPRELMYP FWQNDTRTPK VDDGSSSEIK LAIPVFFFGV
     PYRTVYVNNN GVVSFNVLVS QFTPESFPLT DGRAFIAPFW ADVHNGIRGE IYYRETMDPA
     ILRRATKDIR KYFKDMTTFS ATWVFIVTWE EVTFYGGSST TPVNTFQAVL VSDGSYTFTL
     FNYYEINWTT GTASGGDPLT GLGGVMAQAG FNGGNLTNFF SLPGSRTPEI VNIQETTNVN
     VPGRWAFKVD GKEIDPANGC TSRGQFLRRG EVFWDDLNCT IKCRCLDFNN EIYCQEASCS
     PYEVCEPKGR FFYCSPVETS TCVVFGEPHY HTFDGFLFHF QGSCAYLLAR QCLQTSSLPF
     FSVEAKNEHR GGSAVSWVKE LSVEVNGYKI LIPKGSYGKV KVNDLVTSLP VTLELGAVKI
     YQSGMSTAVE TDFGLLVTFD GQHYASISIP GSYINSTCGL CGNYNKNPLD DFLRPDGRPA
     MSVLDLGESW RVYHADWKCG SGCVDNCTQC DAATEALYFG SDYCGFLNKT DGPLWECGTV
     VDATAFVHSC VYDLCSVRDN GTLLCQAIQA YALVCQALGI PIGDWRIQTG CVSTVRCPSF
     SHYSVCTSSC PDTCSDLTAS QNCATPCTEG CECNEGFVLS TSQCVPLHKC GCDFDGHYYT
     MGEFFWATAN CTVQCLCEEG GDVYCFNKTC RSGEVCAVED GYQGCFPKRE TVCLLSQNQV
     LHTFDGAAYA FPSELSYTLL KTCPERPEYL EIDINKKKPD AGPAWLRGVR ILVADQEVKI
     GGVGALEVKL NGQDVELPFF HPSGRLEIHR NKNSTTVESK GVVSVQYSDV GLLYIRLSTM
     YFNCTGGLCG FFNANASDEF CLPNGKCTDN LAVFLESWTT FEEICNGECG DLLKACNNDS
     ELLKFYRSRS RCGIINDPSN SSFLECHGVV NVTAYYRTCL FRLCQSGGNE SELCDSVARY
     ASACKNADVE VGPWRTYDFC PLECPENSHF EECMTCTETC ETLALGPICV DSCSEGCQCD
     EGYALQGSQC VPRSECGCNF EGHQLATNET FWVDQDCQIF CYCNGTDNSV HCETIPCRDD
     EYCMEESGLY YCQPRTDASC IVSGYGHYLT FDGYPFDFQT SCPLILCTTG SRPISDSFPK
     FIVTAKNEDR DPSLALWVKQ VDVNVFGYSI VIHRAYKHTV LVNNERLYLP LKLGQGKINI
     FSFGFHVVVE TDFGLKVVYD WKTFLSITVP RSMQNGTYGL CGRYNGNPDD DLEMPMGLPA
     LSINEFGQSW VKRDTFCQVG CGDRCPSCAK VEGFSKVQQL CSLIPNQNAG FAKCHSKVNP
     TFFYKNCLFD SCIDGGAVQT ACSWLQNYAS TCQTQGIAVT GWRNYTSCSV TCPPNSHYES
     CVSVCQPRCA AIRLKSDCNH YCVEGCQCDA GYVLNGKSCI LPHNCGCYSD GKYYEPKQLF
     WNGDCTRRCR CFRRNLIQCD PRQCKSDEEC ALRSGVRGCF STKTSYCLAA GGGVFRTFDG
     AFLRFPANCA FVLSTICQKL PDISFQLIIN FDKWSSPNLT IISPVYFYIN EEQILINDRN
     TVKVNGTQVN VPFITGLATK IYSSEGFLVI DTSPDIQIYY NGFNVIKISI SERLQNKVCG
     LCGNFNGDMT DDYVTLRGKP VVSSVVLAQS WKTNGMQKRP LAPSCNELQF SQYAATCDNV
     HIQAMQGDGY CLKLTDMKGF FQPCYGLLDP LPFYESCYLD GCYNHKKFQL CGSLAAYGEA
     CRSFGILSTE WIEKENCSGV VEDPCVGADC PNRTCELDNG GELCGCIEPP PYGNNSHDII
     DAEVTCKAAQ MEVSISKCKL FQLGFEREGV RINDRQCSGI EGEDFISFQI NNTKGNCGNI
     VQSNGTHIMY KNTIWIESAN NTGNIITRDR TINVEFSCAY ELDIKISLDS VVKPMLSVIN
     LTVPTQEGSF TTKMALYKNA SYKHPYRQGE VVLTTRDVLY VGVFVVGADS THLILTLNKC
     YATPSRDSND KLRYFIIEGG CQNIKDNTIG IEENGVSLTC RFHVTVFKFI GDYDEVHLHC
     AVSLCDSEKY SCKINCPQNS RIATDYSKEH KEQIISVGPI RRKRLDWCED NGGCEQICTS
     RVDGPLCSCV TGSLQEDGRS CRASNSSVEL QVWTLLLIMT QISLWHLIYK SGATS
//