GenomeNet

Database: UniProt
Entry: A0A0Q9WN73_DROMO
LinkDB: A0A0Q9WN73_DROMO
Original site: A0A0Q9WN73_DROMO 
ID   A0A0Q9WN73_DROMO        Unreviewed;      3970 AA.
AC   A0A0Q9WN73;
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 E {ECO:0000313|EMBL:KRF94152.1};
GN   Name=Dmoj\GI15893 {ECO:0000313|EMBL:KRF94152.1};
GN   ORFNames=Dmoj_GI15893 {ECO:0000313|EMBL:KRF94152.1};
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:KRF94152.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:KRF94152.1, 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; KRF94152.1; -; Genomic_DNA.
DR   RefSeq; XP_015017084.1; XM_015161598.1.
DR   EnsemblMetazoa; FBtr0427624; FBpp0385232; 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; 6.
DR   CDD; cd00096; Ig; 2.
DR   CDD; cd00110; LamG; 3.
DR   CDD; cd00112; LDLa; 11.
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; 11.
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:SF61; CD320 ANTIGEN; 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; 8.
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; 12.
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; 11.
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; 4.
DR   PROSITE; PS50068; LDLRA_2; 12.
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          706..787
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          927..1010
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1074..1246
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1436..1615
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1650..1699
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1720..1767
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1791..1968
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          2039..2138
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2143..2230
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2242..2334
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2349..2433
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2438..2519
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2525..2613
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2635..2717
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2729..2813
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2816..2911
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3084..3171
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3176..3253
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3264..3441
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3439..3475
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3477..3512
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3519..3695
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3731..3767
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3773..3955
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          596..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1696..1717
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        1700..1714
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        468..483
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        503..521
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        515..530
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        531..543
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        538..556
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        550..565
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        570..582
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        577..595
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        589..604
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        645..657
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        652..670
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        807..819
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        814..832
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        826..841
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        847..859
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        854..872
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        866..881
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        890..902
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        897..915
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        909..924
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1669..1678
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1738..1747
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2983..2998
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        3446..3463
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3465..3474
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3481..3491
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3502..3511
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3757..3766
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3928..3955
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   3970 AA;  441254 MW;  8D958E752E957CAF 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 PTDRLTANDC RRDQFFCDES CFDRSILCDG NIDCIDRSDE
     RDCHLHTTRH PLYPPLPCPQ HTCPSGRCYT ESERCDGRRH CEDSSDEANC CASDQFRCRD
     GNCVSQDDVC NGIRQCMDGS DEENCDILQC QHNQFRCRNG QCVSLTARCN GKTDCQDSSD
     ESNCASYRPA SPTTTTTTTA TTTTTTTVAP TTTTVLPVGP LRIICPPTAF RCENGPCIAL
     TARCNGVIDC PFDASDELDC EPITNEIDTS DTSPAGRSQL NLKTYPDSQI IKERYIREGR
     EVIFRCRDEG PARAKVRWTR PGGRPLPVGF SDKGGRLEIP NIRVEDSGTY VCEAVGYPSY
     IQGQQVTVHL TVERFNIDEH ERPPTACTEY QATCMNSECI DKSEICDGVP NCSDGSDEHR
     CSHGRRCQPN QFLCRNTKCV ERTWRCDGED DCGDNSDEES CDPEPSGAPC RYDEFQCSTG
     HCVPKSFHCD GINDCRDGSD EFGCTDPKPL RKPPPMQSLL EGQSLNLTCT GTGVPVPTII
     WRLNWGHVPD QCTFTSSNGR GDLYCPNMQY KDSGAYSCEI MNTRGTIFVT PDTIVKVIPD
     RNQVCEAGFF NMLARSTEEC IKCFCFGVAS SCDSANLFTY AIQPPILSHR VVTVDLTPYQ
     QIVINEGSGH SLLTLHHGVQ FRASDVQYNS RETPYLALPS EYMGNQLKSY GGELRYEVNY
     LGSGRPISGP DAIITGNGFI LTNRVRTQAN ILNKVKISFL PGNWLKPDGR KATREEIMMI
     LANVDNILIR LGYIDSVARE VELTNIAMDS AGTTDQGLGS ASLVEKCNCP PGYIGDSCES
     CAPGFVRQPG GPWLGRCVPF VPELCPAGTF GDPRHGIPCS ECPCPHTGTN NFANGCKLSP
     DNDVICNCHE GYEGRRCESC AAGYQGNPLI PGGACHKTPE SQCNIEGTYN QNADGSCDCK
     ALVTGDRCDT CAQNSFHLNS FTYSGCIECF CSGLQAECTS TSWYREQVSS SFGHSHVPHG
     FQLVRDYTLA SPQSVPFDTL SNEISFRSGS EYSADTLYWS LPAPFLGNKL TAYGGRLNYT
     LSYSPLPGGQ MSRNSAPDVV IKSGEDLTLI HFRKAAVSPS TSNSYAVPII ESAWQRIDGE
     ATNREHLLMA LSKIDAIYIK ATYTTSTMEG SLKQVVMDVA TSNGYGTQRA LEVEECRCPQ
     GYIGLSCERC APGYKRNVEG GLYLGLCEPC ECNGHSTQCD AESGECLSCA DNTEGENCDR
     CAAGYVGDAT RGTPYDCQPD NNGPQPPQPP QPTPDDQREC QWCNRDGTED CRNGVCYCRR
     NVVGARCDQC RPNTFGLASS NPDGCKDCFC SGHSSQCRSA VAYRQLIAID FISNKALITD
     EYGQQMEMDD SNLKKDIPTN MYTYTYPSYS TKYWSLRGNV QGNQLHAYGG YLKYTLVAES
     FGDYQPGNDV VLIGNGVRLV WSRPAKDSQL NEYSVRLSEE EQWLRLDSGS AVPASRHDIM
     SVLVNIEHLL IRATPKIPTT RTSISDVTWE LSLDADQPGA ELVTDIELCQ CPAGYTGNSC
     ENCAPLHYRE ENGQCRSCPC QEENTQSCYL GSSGYVECQC KQNFKGDRCQ DFDYGIPEPS
     TTEQPDNIRS QIIVSISKPQ ITIMPVGGSI SLHCNGRMKW NNNPVVVSWY KQNSQLPNTA
     EISGGVLRLY NMQVPDSGVY ICRAVNNQTS RAYEDMVSIT ITPHSQRSRA QIVNLPQTVT
     FNEYVPNEIN CEVEGNPAPV VIWTRIDGQA DGNTRTDGSR LIFESPRKSD EGRYRCQARN
     DLNVDEKYVQ VYVVGNAPQP QPPARERLYI QPENYNGESG DIIRFVCQST SGAQLHYEWL
     HDGYPLNVPQ SSHVIISGDT LEIRDATTRD NGVYTCVGID LRTHRNYTED ARVYIEERQQ
     PPIGNGVVPR IVRLKEEYVI YQGSDLSITC ESTGSPYPSI KWMKVRDSMP SNVQITGNVL
     RIHNAMIENR GWYVCTAENA LGTDQSNTHI DVEPRERPSV EIEPIRTLTV GEQGVLYCRA
     HGIPEPTVQW RRVDDAPLSS RHIEQHPGYV LINEVQLADS GDYECSAVNS VGRTTGVVTI
     RVIEPPVIEL EPNESLIQYT EGDEVRITCI ASGTPNPTVQ WDDQPVVYAL DNRQVGSNTA
     YLNINRVTQA DAKVYVCKAT NEAGSDERAV RIDVKPKRGD IGDRDGDVER DPYLPQYYPP
     QRPSSDTQRF PTHLGANVTL TCNLDPYLNT KWTRVDGQPL LPNARSEHNK LTITFVEEHN
     LGQYRCNAMD HRGTIVTYLV RELVRSPLPQ ITFRPNIPLE VEADRNVEIY CDVIGARPED
     VKWTTENNRP LPSSVHIEGQ LLRFIAITPA DAGGYSCTAS NEYGNISKIA QVVVRPPATY
     TQQPISMQQQ RREGESIQMR CTVTTQRGEQ RSNTQFHWTR EDRQPLPNNA RADSQILILT
     SLRLEDAGRY ICDSYDINTG QRLPPTYVDL SVQQNNYSLY RGGQDFPCVV LYICADFKLN
     KMTPSKPLAT PPRAPPPSTY ACQATDFKCV SHPHTCIKAS MVCDGIYDCT DHSDEFNCSR
     DLAAKTIGRP TTGVGLGVGV SHGPGNTFKR WKKSWRKHQP WQQQADKQQR VGQPKAKGFF
     AGMTQPSAYL PPSRPTPPPE PVVPRDYSLK LDQQSSKLHV GESTEVECYS SDNSYTDVIW
     ERSDGVPLSA NIQQVGNRLV INQVTAADAG NYVCKCRTDD GDLYTTSYEL AIEEQPHELR
     RPKIVHANVG DQAQLSCGAD ESRQPTYRWS RQYGQMQSGR DLLSSELSLR GVQANDAGSY
     ICTAVYNDGE SVDYPSILVI TGVIPQFSQQ PLSYMSFPTL PDSSFNFNFE ITFRPESANG
     VILFNGQTRG AGDYIALSLK DRYVEFRFDF GGKPMVVRAE QPVELNEWHT ARVHRARRDG
     YIQLDEQHPV AFPTLTQIPQ LELIEDLYIG GVPNWNQLPA EAVAHQTGFV GCISRLTLQG
     RTIELMKDAK LKEGITSCKP CAASPCANGG ICLESQTELA YTCVCQQGWT GRNCAVEGTQ
     CTPGLCGAGR CENTELDMEC LCPLNRTGDR CQYMEHLNEH SLNFKRNSYA AYNTPRVSRI
     NVTLSLRPSS LRDAVLLYTA ESKLPSGDYV ALVLRDGHVE LIINTAARLK PVVVRSQKPL
     PLHRWTRVEL LRRQGESILR VGDEPEQRAK AAGAPRTLSL KTPLYVGGYD RATVKINRDV
     NITERFDGCI SHLYDSMRPI QLLAAIKDAA NLQNCGELNE IGSNDFDGEL PAVPVAPTSN
     SRVAEEQQPY AMSPCANEPC ENGGTCQEVE QQAICACSLG YSGKHCEEHI QVSFNASFRG
     NGYLEVDRSQ FSSEIDQQYT SAVVVFSTSK PNGLLLWWGQ KSGEEFTGQD FIALAVVDGF
     VEYALRLDGE EVVIRNGDTP VDDGQRHIVL VKRADNTAIL EVDRISDSGE TRPTSKKEMH
     LPGNVFIGGI PNISRFTGKR YTHNFNGCIV FVEGDAVGQV NLGKASVSGV NVDTCPVNDE
     ALGGTEPPVV
//
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