GenomeNet

Database: UniProt
Entry: B4H185_DROPE
LinkDB: B4H185_DROPE
Original site: B4H185_DROPE 
ID   B4H185_DROPE            Unreviewed;      3708 AA.
AC   B4H185;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=GL22528 {ECO:0000313|EMBL:EDW30062.1};
GN   Name=Dper\GL22528 {ECO:0000313|EMBL:EDW30062.1};
GN   ORFNames=Dper_GL22528 {ECO:0000313|EMBL:EDW30062.1};
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN   [1] {ECO:0000313|EMBL:EDW30062.1, ECO:0000313|Proteomes:UP000008744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49
RC   {ECO:0000313|Proteomes:UP000008744};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   EMBL; CH479202; EDW30062.1; -; Genomic_DNA.
DR   RefSeq; XP_002024614.1; XM_002024578.1.
DR   STRING; 7234.B4H185; -.
DR   EnsemblMetazoa; FBtr0188143; FBpp0186635; FBgn0160120.
DR   GeneID; 6599465; -.
DR   KEGG; dpe:6599465; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   HOGENOM; CLU_000301_1_0_1; -.
DR   OMA; GECKCLT; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; B4H185; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0036062; C:presynaptic periactive zone; IEA:EnsemblMetazoa.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IEA:EnsemblMetazoa.
DR   GO; GO:0071711; P:basement membrane organization; IEA:EnsemblMetazoa.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:EnsemblMetazoa.
DR   GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IEA:EnsemblMetazoa.
DR   GO; GO:0007507; P:heart development; IEA:EnsemblMetazoa.
DR   GO; GO:0035011; P:melanotic encapsulation of foreign target; IEA:EnsemblMetazoa.
DR   GO; GO:0007498; P:mesoderm development; IEA:EnsemblMetazoa.
DR   GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:EnsemblMetazoa.
DR   CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR   CDD; cd00055; EGF_Lam; 21.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.10.25.10; Laminin; 21.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 21.
DR   Pfam; PF02210; Laminin_G_2; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00180; EGF_Lam; 22.
DR   SMART; SM01411; Ephrin_rec_like; 4.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 19.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..3708
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002804622"
FT   DOMAIN          20..272
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          448..494
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          495..540
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          541..586
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          587..631
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          632..681
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          732..784
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1375..1420
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1421..1465
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1466..1513
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1514..1564
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1592..1777
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1811..1918
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1919..1971
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1972..2018
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2019..2065
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2066..2113
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2674..2871
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2879..3050
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3055..3225
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3340..3519
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3530..3705
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          3244..3289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2222..2249
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2381..2443
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2600..2676
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        3258..3289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        448..460
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        470..479
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        495..507
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        497..514
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        516..525
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        541..553
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        543..560
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        562..571
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        587..599
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        607..616
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        632..644
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        652..661
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        755..764
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1375..1387
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1377..1394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1396..1405
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1438..1447
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1489..1498
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1514..1526
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1516..1533
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1535..1544
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1889..1898
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1943..1952
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1955..1969
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1991..2000
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2039..2048
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2066..2078
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2068..2085
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2087..2096
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        3198..3225
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT   DISULFID        3678..3705
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   3708 AA;  411222 MW;  1068ADC709A03282 CRC64;
     MGLPVPVGVA LCLLLAIAQC QAELTPPYFN LATGRKIFAT ATCGEDTDGP ELYCKLVGAN
     TENDHIDYSV IQGQVCDVCD PNVPDKNHPP ENAIDGTEAW WQSPPLSRGM KYNEVDLTIN
     FEQEFHVAYL FIRMGNSPRP GLWTLEKSVD YGKTWTPWQH FSDTPADCET YFGKDTYKPI
     SRDDDVICTT EYSKIVPLEN GEIPVMLLNE RPSSTNYFNS SVLQEWTRAT NVRIRLLRTK
     NLLGHLMSVA RQDPTVTRRY FYSIKDISIG GRCMCNGHAD TCDVKDPKSA VRILACRCQH
     HTCGIQCNEC CPGFEQKKWR QNTNARPFNC EPCNCHGHST ECKYDEDVNR KGLSLDIHGH
     YDGGGVCQNC QHNTVGINCN KCKPKYYRPK GKHWNDTDVC SPCQCDFFYS TGHCEEETGN
     CECRAAFQPP NCDSCAYGYY GYPNCRECEC NLNGTNGYHC EAESGQQCPC KINFAGSYCK
     QCAEGYYGFP ECKACECNQI GSITNDCNVT TGECKCLTNF GGDNCERCKH GYYNYPACSY
     CDCDNQGTES EICNKQSGQC ICREGFGGPR CDQCLPGFYN YPDCKPCNCS STGSSAITCD
     NTGKCNCLNN FAGKQCTLCS AGYYSYPDCL PCHCDSHGSQ GVTCNADGQC LCQPNFDGRQ
     CDSCKESFYN FPRCDDCNCD PAGVIDKFSG CGSVPVGELC KCKERVYGHI CDECNHLYWN
     LNISNPDGCE NCDCWTDGTI SGLDTCASKS GQCPCKPHTQ GRRCKECRDG TFDLDSSSLF
     GCKDCQCDVG GSWASVCDKT SGQCKCHPRV TGRACTQPLT THYFPTLHQF QYEYEDGALP
     SGTQVRYDYD EQKFPGFSSK GYVVFNTIQN EVRNELTVFK SSLYRIVLRY VNPNDENVTA
     TILIQSDNPQ EVDQNVKVLL QPTKQPQFVT VSGPKGLKPS AIVLDPGPRY VFTTKASKNV
     MLDYFVLLPA AYYEASILTR QISNPCELGN MELCRHYKYA SVEVFEPASV PFLIGSNGKA
     AKPAEVYSDP EHLQIVSHVG DVPVLSRSQP ELNYIVDVPH SGRYIFVIDY ISHRNFTNTY
     YVNLRLKNDP DSETSVLLYP CLYSTVCRTS VNDDGLEKSF YISKEDLQPV TIYADISDEY
     RVPIISVTAI PVEQWSIDYI NPSPVCVIHN QQCSTPKFVS VPDSKKIEFE TDHEDRIATN
     KPPYAVLDER VKLVHLDSNQ EGTIVIDSKV AEPDRYVILV KYYQPDNPKY QVYFTLTAAK
     NQYDGHFDIQ HCPSSSGCRG VIRPGGEYDW FDIDDEFHFT ITNDRPQGVW LDYLVVVPLK
     QYNEDLLVEE TFDQTKEFIK NCGHDDFHIT HNASEFCKKA VFSVTADYNS GALACNCDYA
     GSTSFECRPF GGQCQCKPNV IERQCGTCRS RYYGFPDCKP CECPTSAMCE PTTGECMCPP
     NVIGDLCEKC APNTYGFHQV IGCEECNCNY LGIANGNTQC DMFNGTCECR DNIEGRACDV
     CAHGYYQFPR CDQCSCHTPG TELEVCDKID GSCFCKKNVV GRDCDQCVDG TYNLQDSNPD
     GCTTCFCFGK TSRCDSAYLR VYNVSLLRQV SISTAEFNHN NKTIEFELWA VTPEELQLNE
     TTLQADFTSR EVSDERPAYF GVLDYLLNQN SHISSYGGDL AYTLHFTSGF DGKSIVAPDV
     ILMGKDKVLV HQSYEQPSRN MPFTNRLQMV ESNFQTHAGK TVSRADFMMV LRDLKAIYIR
     ANYWEQTLVT HISDVYLSLA DEDADGTAEY QFLAVERCSC PPGYVGHSCE DCAPGYYRDP
     NGPYGGYCIP CECNGHSETC DCATGICTGC QHGTQGEHCE DCVSGYYGNA TNGTPIDCMI
     CACPLPFDSN NFATSCEISE SGNEIHCECR PGYTGPRCES CANGFYGNPE NVGDVCKPCD
     CSGNINPEDQ GSCDTRTGEC LRCLNNTFGA ACNLCAPGFY GDAVKLKNCQ SCDCDDLGTL
     ECDPFVGKCT CHENVIGERC DRCKADHYGF ESGLGCRACD CGAASNSTQC DAHTGHCACK
     PGVTGRQCDR CAVDHWKYQK EGCTPCNCNQ GYSRGFGCNP NTGKCQCLPG VIGDRCDACP
     NRWVLIKDEG CQECNNCHHA LLDVTDKMRY QIDSVLADFG SVTLAFFTSQ KLNYYDSLAD
     ELAPKIKALD PTSVDLNPSK KSNSDLEADA KSYAKQVNQT LANALDIRDR SSSTLGNITS
     AYDEALKSAD QAREAIAAVE ALSKNLETAA STKIDAALEQ AQHILGQIND TQIQLVANEQ
     VLEKSRLLYD EVDALVQPIK EQNRSLNALK NDIGEFSDKL EDLFNWSDQS ETQSAEVERL
     NVVNKQSFDN SKFATVSEQQ QEAETNIQDA GNYLINGDLT LNQIGQKLDN LRDALEELKS
     VNKNVDEDLP LRDEQHQEAE QLTAQAEMRA AELAIKAQDL AEQYTDMTAH AEPAIKAATA
     YSGIVEAVDA GQQFSQDAIT AAGNATQITD GIEERAGQAY SESADLLQKA RQSLQKVQDD
     LEPRLNSSGG KVQQISQRNN ATEQQLKDIN ILIAQLPAAA QRDMWKSSNA NASDALEILK
     NVLEILEPVS AQTPKELEKA HNINRDLDLT NKDISQANNQ LDNVEGSVSK LVELAEDVED
     QQQRVATQTL QLGQDIENLK RQVETARQMA NNIKVGVKFR PSTVLELKTP EKAKLLATRT
     NLSTFFRTNE KSGFLFFLGN DNATAQKNKD FVAVEIVNGY PILTIDLGNG PQRITNDKYV
     SDGKWYQAVV DRVGSVAKLT IREQLPNGEV VEHQSDPKQL EGSQNILHVD RNSRLFVGGY
     PAAPDFAAPE DITANYFNGD IEDLRIGDEN VGLWNFVYGE DNAEGVRERD VLLEKKKPVT
     GLRFKGKGFV QLNATYNFKS RSTIKFNFKA DKDSSNGLLF FYGRDKHYMS IELVDGAVFF
     NIKLGNGGVS SGSSNRYNDN KWHTVEAGRD GRTGLLKVDD ILLFHETAPA EADEELPKLR
     RMYFGGYPRR FNNSEIVRQN FDGCIDDVII SGIVVDLTEY VNGTGVEEGC PERFSTVLSF
     APNEYGFLRS HNISSDNNLH LNLRFKTLQP KGILFYATNN DQSSAIGLTL DDGYLKLRSQ
     GSELVIDQRP FNDGEDHVVT VQHNAGELRL SVDDEEEERL GSPEPLQIEA GDIFFGGLPD
     NYQTPRGALS TLAYFVGCIS DVTVNDEIIN FANSAEKKNG NINGCPPDIL AYEPDLLPNY
     YPSGANELEP PSPGRITTHK PLATSAPTTT STTTTTTTTT TTTPATITST TVRPTPAEAA
     EIVPQKTLTT RPTPKMNQPS DKRCKLPVEP NYDVDFETAG YRFYSLREQR LEINSLPVKL
     KSHHDVSISF RTEHPNGLLF YASSKQKDDF VAVYLLDGRV TYQLRVGAGL TANITSEAEL
     NDGKWHTVEI VRTAPRVSLI IDQTMQPGSV EVSQERSPPV FSVEMPIFVG GITKFVESEL
     RRHTYFGGNT SYFNGCLTDI KFDGVALETE PTKYSVVPCS EQVERGVFFH SSSNQTTPPY
     VKLFERFTVG AEMAISFDFR PREPNGLVFS VHGKNSYAIL ELVDNELFFT VKSDAKSTLV
     TNFTLPANES FCDGKTRHVQ AIKSKFVINI AVDFVSSNPA VGNESSALTK TNRPLFMGGH
     HAFQKAPGIK TKKTFKGCIS NVEINKKAIR ITPNMIAGDI WQGHCPLN
//
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