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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//