ID A0A0Q9WN66_DROMO Unreviewed; 4314 AA.
AC A0A0Q9WN66;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Uncharacterized protein, isoform J {ECO:0000313|EMBL:KRF94157.1};
GN Name=Dmoj\GI15893 {ECO:0000313|EMBL:KRF94157.1};
GN ORFNames=Dmoj_GI15893 {ECO:0000313|EMBL:KRF94157.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:KRF94157.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:KRF94157.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH933810; KRF94157.1; -; Genomic_DNA.
DR RefSeq; XP_015017089.1; XM_015161603.1.
DR EnsemblMetazoa; FBtr0431619; FBpp0388890; FBgn0138642.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 5.
DR CDD; cd00096; Ig; 2.
DR CDD; cd00110; LamG; 3.
DR CDD; cd00112; LDLa; 16.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 13.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 16.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR001791; Laminin_G.
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:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13927; Ig_3; 10.
DR Pfam; PF00052; Laminin_B; 3.
DR Pfam; PF00053; Laminin_EGF; 6.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF00057; Ldl_recept_a; 12.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 7.
DR SMART; SM00409; IG; 13.
DR SMART; SM00408; IGc2; 13.
DR SMART; SM00281; LamB; 3.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 17.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 13.
DR SUPFAM; SSF57424; LDL receptor-like module; 16.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS50835; IG_LIKE; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 3.
DR PROSITE; PS01209; LDLRA_1; 8.
DR PROSITE; PS50068; LDLRA_2; 17.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..267
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1050..1131
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1271..1354
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1418..1590
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1780..1959
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1994..2043
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2064..2111
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2135..2312
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 2383..2482
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2487..2574
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2586..2678
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2693..2777
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2782..2863
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2869..2957
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2979..3061
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3073..3157
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3160..3255
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3428..3515
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3520..3597
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3608..3785
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3783..3819
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3821..3856
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3863..4039
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 4075..4111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 4117..4299
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 109..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2044..2058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 308..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 345..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 405..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 412..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 464..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 489..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 508..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 595..607
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 602..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 614..629
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 715..730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 745..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 752..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 812..827
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 847..865
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 859..874
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 875..887
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 882..900
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 894..909
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 914..926
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 921..939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 933..948
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 989..1001
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 996..1014
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1151..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1158..1176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1170..1185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1191..1203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1198..1216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1210..1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1234..1246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1241..1259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1253..1268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2013..2022
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2082..2091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3327..3342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3790..3807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3809..3818
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3825..3835
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3846..3855
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 4101..4110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 4272..4299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 4314 AA; 479879 MW; 977BA7498DFE9B65 CRC64;
MGSTGSQTAA TLRQRHALSL LWRLFAVVLV LNACHVPLLN AKQISNLEDN DKMFFDVEDQ
TPFTGSDNLQ SYAPLIDDSP VEGNWFHQGV KRVRRELTRL FGNSDVHHRQ KRAKNPAVQK
AKRQNRMMTR KRASDDYESE IGSGTYGVET VIYRTRFTVN EPYSNDFSDK QSEQFLNLTE
EISLGLRDLF RRSYENDDDE VDLRSTLLQV GPTNDKYKSY VIVNLEIPTN VVDFESKLRE
QLQNYNRIGN QSASLDDDFY FRLTLDPNAP ETPEPTDEED GSGEPECRGD ATFFCYRSKT
RVCDEMTCDS KKDCPHGEDE EDCAKVCTDE EFKCDDTCLP LQMRCDGQTQ CRDQTDEAGC
PPKDIEQPDI DQDQDQDQEN EHEQEPDRDR EQDRPRIPDS PPQECNANEY RCRNGKCIDN
SKVCNYVVDC ADGEDEGDDC PAACSGMEYQ CRDGTRCISV SQQCDGHADC SDADDEEQCD
GSGYDADQCL YNEFRCRNGE CIPMRQVCDN IYDCNDYTDE EDCDPNDIGN NIDDDVIDRD
GIIRQYGDHR HPPPAPGRDN ERNRHNDGLH KLDAEEYELY YPQDHYAKAT PQKPCDADHF
KCQNNVCIPI RLRCDGFHHC NDRSDEADCD RYRPPTTTRR PVTLAPTRYP WVTYGPAPLE
RLTTAAPPLF RVTPAATRPT TNPIPITTRG VASSSSCAIN QIACNGACLD WSLRCDGIRD
CDNGVDELDC PAGSKHFRNT TVRKCQPYQW QCSNSECINA DFLCDKHADC TDESDELPSR
CLGQATDRLT ANDCRRDQFF CDESCFDRSI LCDGNIDCID RSDERDCHLH TTRHPLYPPL
PCPQHTCPSG RCYTESERCD GRRHCEDSSD EANCCASDQF RCRDGNCVSQ DDVCNGIRQC
MDGSDEENCD ILQCQHNQFR CRNGQCVSLT ARCNGKTDCQ DSSDESNCAS YRPASPTTTT
TTTATTTTTT TVAPTTTTVL PVGPLRIICP PTAFRCENGP CIALTARCNG VIDCPFDASD
ELDCEPITNE IDTSDTSPAG RSQLNLKTYP DSQIIKERYI REGREVIFRC RDEGPARAKV
RWTRPGGRPL PVGFSDKGGR LEIPNIRVED SGTYVCEAVG YPSYIQGQQV TVHLTVERFN
IDEHERPPTA CTEYQATCMN SECIDKSEIC DGVPNCSDGS DEHRCSHGRR CQPNQFLCRN
TKCVERTWRC DGEDDCGDNS DEESCDPEPS GAPCRYDEFQ CSTGHCVPKS FHCDGINDCR
DGSDEFGCTD PKPLRKPPPM QSLLEGQSLN LTCTGTGVPV PTIIWRLNWG HVPDQCTFTS
SNGRGDLYCP NMQYKDSGAY SCEIMNTRGT IFVTPDTIVK VIPDRNQVCE AGFFNMLARS
TEECIKCFCF GVASSCDSAN LFTYAIQPPI LSHRVVTVDL TPYQQIVINE GSGHSLLTLH
HGVQFRASDV QYNSRETPYL ALPSEYMGNQ LKSYGGELRY EVNYLGSGRP ISGPDAIITG
NGFILTNRVR TQANILNKVK ISFLPGNWLK PDGRKATREE IMMILANVDN ILIRLGYIDS
VAREVELTNI AMDSAGTTDQ GLGSASLVEK CNCPPGYIGD SCESCAPGFV RQPGGPWLGR
CVPFVPELCP AGTFGDPRHG IPCSECPCPH TGTNNFANGC KLSPDNDVIC NCHEGYEGRR
CESCAAGYQG NPLIPGGACH KTPESQCNIE GTYNQNADGS CDCKALVTGD RCDTCAQNSF
HLNSFTYSGC IECFCSGLQA ECTSTSWYRE QVSSSFGHSH VPHGFQLVRD YTLASPQSVP
FDTLSNEISF RSGSEYSADT LYWSLPAPFL GNKLTAYGGR LNYTLSYSPL PGGQMSRNSA
PDVVIKSGED LTLIHFRKAA VSPSTSNSYA VPIIESAWQR IDGEATNREH LLMALSKIDA
IYIKATYTTS TMEGSLKQVV MDVATSNGYG TQRALEVEEC RCPQGYIGLS CERCAPGYKR
NVEGGLYLGL CEPCECNGHS TQCDAESGEC LSCADNTEGE NCDRCAAGYV GDATRGTPYD
CQPDNNGPQP PQPPQPTPDD QRECQWCNRD GTEDCRNGVC YCRRNVVGAR CDQCRPNTFG
LASSNPDGCK DCFCSGHSSQ CRSAVAYRQL IAIDFISNKA LITDEYGQQM EMDDSNLKKD
IPTNMYTYTY PSYSTKYWSL RGNVQGNQLH AYGGYLKYTL VAESFGDYQP GNDVVLIGNG
VRLVWSRPAK DSQLNEYSVR LSEEEQWLRL DSGSAVPASR HDIMSVLVNI EHLLIRATPK
IPTTRTSISD VTWELSLDAD QPGAELVTDI ELCQCPAGYT GNSCENCAPL HYREENGQCR
SCPCQEENTQ SCYLGSSGYV ECQCKQNFKG DRCQDFDYGI PEPSTTEQPD NIRSQIIVSI
SKPQITIMPV GGSISLHCNG RMKWNNNPVV VSWYKQNSQL PNTAEISGGV LRLYNMQVPD
SGVYICRAVN NQTSRAYEDM VSITITPHSQ RSRAQIVNLP QTVTFNEYVP NEINCEVEGN
PAPVVIWTRI DGQADGNTRT DGSRLIFESP RKSDEGRYRC QARNDLNVDE KYVQVYVVGN
APQPQPPARE RLYIQPENYN GESGDIIRFV CQSTSGAQLH YEWLHDGYPL NVPQSSHVII
SGDTLEIRDA TTRDNGVYTC VGIDLRTHRN YTEDARVYIE ERQQPPIGNG VVPRIVRLKE
EYVIYQGSDL SITCESTGSP YPSIKWMKVR DSMPSNVQIT GNVLRIHNAM IENRGWYVCT
AENALGTDQS NTHIDVEPRE RPSVEIEPIR TLTVGEQGVL YCRAHGIPEP TVQWRRVDDA
PLSSRHIEQH PGYVLINEVQ LADSGDYECS AVNSVGRTTG VVTIRVIEPP VIELEPNESL
IQYTEGDEVR ITCIASGTPN PTVQWDDQPV VYALDNRQVG SNTAYLNINR VTQADAKVYV
CKATNEAGSD ERAVRIDVKP KRGDIGDRDG DVERDPYLPQ YYPPQRPSSD TQRFPTHLGA
NVTLTCNLDP YLNTKWTRVD GQPLLPNARS EHNKLTITFV EEHNLGQYRC NAMDHRGTIV
TYLVRELVRS PLPQITFRPN IPLEVEADRN VEIYCDVIGA RPEDVKWTTE NNRPLPSSVH
IEGQLLRFIA ITPADAGGYS CTASNEYGNI SKIAQVVVRP PATYTQQPIS MQQQRREGES
IQMRCTVTTQ RGEQRSNTQF HWTREDRQPL PNNARADSQI LILTSLRLED AGRYICDSYD
INTGQRLPPT YVDLSVQQNN YSLYRGGQDF PCVVLYICAD FKLNKMTPSK PLATPPRAPP
PSTYACQATD FKCVSHPHTC IKASMVCDGI YDCTDHSDEF NCSRDLAAKT IGRPTTGVGL
GVGVSHGPGN TFKRWKKSWR KHQPWQQQAD KQQRVGQPKA KGFFAGMTQP SAYLPPSRPT
PPPEPVVPRD YSLKLDQQSS KLHVGESTEV ECYSSDNSYT DVIWERSDGV PLSANIQQVG
NRLVINQVTA ADAGNYVCKC RTDDGDLYTT SYELAIEEQP HELRRPKIVH ANVGDQAQLS
CGADESRQPT YRWSRQYGQM QSGRDLLSSE LSLRGVQAND AGSYICTAVY NDGESVDYPS
ILVITGVIPQ FSQQPLSYMS FPTLPDSSFN FNFEITFRPE SANGVILFNG QTRGAGDYIA
LSLKDRYVEF RFDFGGKPMV VRAEQPVELN EWHTARVHRA RRDGYIQLDE QHPVAFPTLT
QIPQLELIED LYIGGVPNWN QLPAEAVAHQ TGFVGCISRL TLQGRTIELM KDAKLKEGIT
SCKPCAASPC ANGGICLESQ TELAYTCVCQ QGWTGRNCAV EGTQCTPGLC GAGRCENTEL
DMECLCPLNR TGDRCQYMEH LNEHSLNFKR NSYAAYNTPR VSRINVTLSL RPSSLRDAVL
LYTAESKLPS GDYVALVLRD GHVELIINTA ARLKPVVVRS QKPLPLHRWT RVELLRRQGE
SILRVGDEPE QRAKAAGAPR TLSLKTPLYV GGYDRATVKI NRDVNITERF DGCISHLYDS
MRPIQLLAAI KDAANLQNCG ELNEIGSNDF DGELPAVPVA PTSNSRVAEE QQPYAMSPCA
NEPCENGGTC QEVEQQAICA CSLGYSGKHC EEHIQVSFNA SFRGNGYLEV DRSQFSSEID
QQYTSAVVVF STSKPNGLLL WWGQKSGEEF TGQDFIALAV VDGFVEYALR LDGEEVVIRN
GDTPVDDGQR HIVLVKRADN TAILEVDRIS DSGETRPTSK KEMHLPGNVF IGGIPNISRF
TGKRYTHNFN GCIVFVEGDA VGQVNLGKAS VSGVNVDTCP VNDEALGGTE PPVV
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