GenomeNet

Database: UniProt
Entry: A0A139WIN8_TRICA
LinkDB: A0A139WIN8_TRICA
Original site: A0A139WIN8_TRICA 
ID   A0A139WIN8_TRICA        Unreviewed;      2473 AA.
AC   A0A139WIN8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein-like Protein {ECO:0000313|EMBL:KYB27637.1};
GN   Name=AUGUSTUS-3.0.2_33077 {ECO:0000313|EMBL:KYB27637.1};
GN   ORFNames=TcasGA2_TC033077 {ECO:0000313|EMBL:KYB27637.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB27637.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB27637.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB27637.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB27637.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB27637.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KQ971342; KYB27637.1; -; Genomic_DNA.
DR   STRING; 7070.A0A139WIN8; -.
DR   EnsemblMetazoa; TC033077_008; TC033077_008; TC033077.
DR   InParanoid; A0A139WIN8; -.
DR   OMA; ECANNTE; -.
DR   Proteomes; UP000007266; Linkage group 5.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd00055; EGF_Lam; 3.
DR   CDD; cd00112; LDLa; 19.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 20.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 3.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR000082; SEA_dom.
DR   PANTHER; PTHR24270:SF8; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   Pfam; PF00052; Laminin_B; 3.
DR   Pfam; PF00053; Laminin_EGF; 7.
DR   Pfam; PF00057; Ldl_recept_a; 19.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00180; EGF_Lam; 8.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00281; LamB; 3.
DR   SMART; SM00192; LDLa; 20.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 19.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS51115; LAMININ_IVA; 3.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 20.
DR   PROSITE; PS50024; SEA; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..2473
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007299989"
FT   DOMAIN          290..403
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          1131..1221
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1356..1431
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1513..1687
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1741..1780
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1743..1799
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1873..2054
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          2088..2135
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2140..2188
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2214..2397
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   REGION          99..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..199
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        409..421
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        416..434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        428..443
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        496..511
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        515..527
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        522..540
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        534..549
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        570..585
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        611..626
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        630..642
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        637..655
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        649..664
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        666..678
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        673..691
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        685..700
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        714..726
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        721..739
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        733..748
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        755..767
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        762..780
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        774..789
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        800..812
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        818..833
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        836..848
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        843..861
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        855..870
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        874..886
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        881..899
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        893..908
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        920..932
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        927..945
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        939..954
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        967..985
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        979..994
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1001..1013
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1008..1026
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1020..1035
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1037..1049
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1044..1062
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1056..1071
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1113..1128
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1236..1248
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1243..1261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1255..1270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1275..1287
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1282..1300
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1294..1309
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1338..1353
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1770..1779
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2107..2116
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2119..2133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2140..2152
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2159..2168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   2473 AA;  273349 MW;  4CA74BB70D6C328E CRC64;
     MGAFGKDTPR LAWLCLIATF CFLILDHSVY QVSAESKVDS DLVFENLEQT DLANHENHHR
     IARDLSDSEE HLLESSPPVE EHWLSSTVNR IRRSINSLLS SQSNRSHSRS KRKLLRVPRQ
     DTPEGQQEAK EDYDEEEEDP QDFNDLEDAE NDNGDNEYDD NTGDNEYDEE NGEEIGNGED
     YNEEDQTEDN TEDEVPEEEY SPSLNNNETT ESTANTITES PQVNYFSTEN GDGVNRMGFD
     LFKPDTAYNR SIPETRNETQ FGYDDEDNLI TSGEGSTDGT SVPHIPVPHH PVYYRISFTV
     SEPYVDAFSD RNSFRYRDFS EDLIREIDRL YQSIPGTQSA TVIKIEKREA DAFTSKVTID
     LGSDGYINDE IIKDVLYSQI TNNHRLGKTT VLPEDFQFRV FEASTNVMCD VNEIPCHSGE
     CVPSEARCNG NFECADHSDE AGCEIFAETS STTTLDDLDL GSGLPDEGRS PESKCRADDI
     VRCADGSPSI CADQVCDGVK DCADGGDEKN CSSDCAKGEI SCDITRCIPE SKRCDGMKDC
     QDDTDERDCI VCRDDEIKCD NKCIPLNKRC DGTADCSNRA DELNCPAEAQ CRHDEFLCHG
     SSQCIPLQQR CDGNRNCPNN EDETDCSVRC GADQFTCQNG ACIPISAKCD SKYDCQDLSD
     ERNCPCKPTD FQCNNGVCIL PHLRCNGVHN CQDKSDEIGC PSSPRPGTPD YKYCTSDQFK
     CKEGTCISLS KRCDGKFDCG QGEDELSCGY PLSKCPEGTF ECAAGFCIMG YKRCNGIKDC
     PSGNDEDGCP TTITPVTPAC ATDEVLCNDG SCVSGKKCDR SFDCPDGSDE SGCSFCTPDQ
     FPCQGGGCIA EHLRCDGTIH CSDGSDERNC VFTCPEDQFR CGNGVCLDNR RVCDTHPDCP
     DGSDEQNCTG PLPGPDDKRC LPSQFDCGDS SCINSEFRCD GYQDCKNGRD EMECSSTYCH
     EEDEFRCSDG TCIPNSAFCD GVRHCRDGSD ELDCPPPPSI CTVNEFQCDN GECIPNYLRC
     DGVSECPDRS DERECQCRTD QFQCSNGTCI AGNLRCNRRN DCSDGSDEFN CPTQPPPFVT
     EQPLPPRPPQ ITCSPGTQPC HSGDRCILHS QFCDGRVDCN DMSDETNCPG PSEGLNLRTY
     PSSQEIKENR EVVFQCRDEG PFRARVRWTR PNGEPLPPGS RDHNGRLEIP NIKVEHSGTY
     TCEAVGYPPN TPGAHVSVHL QVDRWIPPPI RPPTACALHE ATCSNGDCIP KHQVCDEKYD
     CTDGSDENRC NPNGCEPNEF RCANKKCVLK TWRCDSDDDC GDGSDEENCA TNPPGSLCAY
     HQFACHSNNQ CIPRSYHCDL ERDCIDGSDE IGCSIPVVSK PPPPMVNLEV GSTFEITCTA
     VGVPTPEIVW RLNWGHIPPK CRTTSDNGFG TLSCPNIQVE DQGAYSCEVI NIKGTVFAIP
     DTILVINQNT VCPAGYFNEE ARSQAECIKC FCFGQSTKCR SADLFIYHFQ PPFDTLKLLG
     VRIDSNTGVI DIRDEPIYRN AQPQLTGLGR NGVHAQLPPY GQISSSDLVP YFAMPENYHG
     NQLKSYGGYL RFTVRHYNRG YTIAGPTVIL TGNGYTLLSR HNISPPSNRD EQIEVRFFEG
     EWVKRSDRQL ETPATREEIM MALAEVDNIL IKLQYNEGPL NTTITNIEMD SAGAPNSGLG
     PASYVEECEC PVGYSGSSCE RCADGFVRHK TGPWLGQCYR VQPQPCPPGT YGDPSRGRPC
     EICPCPLTSP SNQFARTCSL GSDGEVTCDC PPGYVGRRCE QCAPGYSGNP LIPGDSCRAS
     SYCNSEGTSL EEQGRCRCKD YVDGPTCDTC KANTFHLSGE NQFGCIACFC MGVTRQCSSS
     TWFRDQISTT FTSSRDHFTL IDTERREEPI TDAIRLDQNQ REISYSSFSN PNVHYWSLPR
     RYLGNKIASY GGYLKYTLRY VPLPGGQISR NSAADVELVS ANEITLLYYA REQSQPTGSP
     QTFVVPLLEQ YWQRSDGQKA DREHLLMALA DLNAIYIKAT YNTNTRESAL ISVSLDTANE
     YNTGSSERAL AVEQCRCPEG YTGLSCEDCA VGYTRAEEGI YLGICEPCNC NGNSRECHPE
     TGVCQNCDNF TTGDNCELCL PGYEGDPANG IPCVGGSSQC NCDQQGAISP ECYNGICRCK
     TNVEGNRCNR CRPGTFGLSG GNIHGCQTCF CSGVATECVE GNLFYEQIPI FIDADRHGFT
     LTDQYQTQRI DSGFQIHTSM NEIGYTFRPS TSERWFWSLP REFTGNQVKS YGGRLEFTQR
     FTQRPQAGYV PDKSVIIIGN GITIYWTNPQ SQIPDVPNKV SVVLNPSSNW QRLDGNQGPR
     PATREDIMTV LANIDVILIN AQPSSDTESA YISDVTLDTA IEQNTFNPQS RAIEVEICRC
     PTGYQGTSCE SCAPGFYRDT NDFSTGPLGS CSRCPCNNHE QSCYLAPNNR VVCNCLPGYM
     GERCVTGGKY LFL
//
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