GenomeNet

Database: UniProt
Entry: B4IY60_DROGR
LinkDB: B4IY60_DROGR
Original site: B4IY60_DROGR 
ID   B4IY60_DROGR            Unreviewed;      3702 AA.
AC   B4IY60;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   05-JUN-2019, entry version 85.
DE   SubName: Full=GH16286 {ECO:0000313|EMBL:EDV96510.1};
GN   Name=Dgri\GH16286 {ECO:0000313|EMBL:EDV96510.1};
GN   ORFNames=Dgri_GH16286 {ECO:0000313|EMBL:EDV96510.1};
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN   [1] {ECO:0000313|EMBL:EDV96510.1, ECO:0000313|Proteomes:UP000001070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
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.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   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.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   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.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   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.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   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.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   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.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   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
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   EMBL; CH916366; EDV96510.1; -; Genomic_DNA.
DR   RefSeq; XP_001984162.1; XM_001984126.1.
DR   SMR; B4IY60; -.
DR   STRING; 7222.FBpp0150192; -.
DR   EnsemblMetazoa; FBtr0151700; FBpp0150192; FBgn0123757.
DR   GeneID; 6556915; -.
DR   KEGG; dgr:Dgri_GH16286; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410YNSE; LUCA.
DR   InParanoid; B4IY60; -.
DR   KO; K06240; -.
DR   OMA; WVAPPSY; -.
DR   OrthoDB; 2342at2759; -.
DR   PhylomeDB; B4IY60; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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   Gene3D; 2.60.120.1490; -; 1.
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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
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   SMART; SM00181; EGF; 11.
DR   SMART; SM00180; EGF_Lam; 21.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 7.
DR   PROSITE; PS50027; EGF_LAM_2; 21.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001070};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001070};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27   3702       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002810991.
FT   DOMAIN       24    276       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      277    336       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      337    406       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      407    451       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      452    497       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      498    543       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      544    589       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      590    634       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      635    678       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      679    733       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      734    786       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      787    831       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1376   1421       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1422   1466       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1467   1514       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1515   1565       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1593   1776       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1810   1859       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1860   1917       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1918   1970       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1971   2017       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2018   2064       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2065   2112       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2673   2870       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2877   3048       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3055   3223       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3339   3518       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     3524   3699       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     3256   3301       Disordered. {ECO:0000256|MobiDB-lite:
FT                                B4IY60}.
FT   COILED     2178   2198       {ECO:0000256|SAM:Coils}.
FT   COILED     2648   2675       {ECO:0000256|SAM:Coils}.
FT   DISULFID    302    311       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    374    383       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    427    436       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    452    464       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    454    471       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    473    482       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    498    510       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    500    517       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    519    528       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    544    556       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    546    563       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    565    574       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    590    602       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    610    619       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    635    647       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    654    663       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    704    713       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    757    766       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    787    799       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    789    806       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    808    817       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1376   1388       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1378   1395       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1397   1406       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1439   1448       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1490   1499       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1515   1527       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1517   1534       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1536   1545       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1829   1838       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1888   1897       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1942   1951       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1954   1968       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1990   1999       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2038   2047       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2087   2096       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   3196   3223       {ECO:0000256|PROSITE-ProRule:PRU00122}.
FT   DISULFID   3672   3699       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3702 AA;  411230 MW;  97F5FC2F0FB9F70C CRC64;
     MGSGAAPFCA MGVAFALCLL VALCNAELTP PYFNLATGRK IHATATCGED TDGPELYCKL
     VGANTENDHI DYSVIQGQVC DHCDPNSPEK NHPPENAIDG TGSWWQSPPL SRGMKFNEVN
     LTIDFEQEFH VAYLFIRMGN SPRPGLWTLE KSTDYGKTWT PWQHFSDTPA DCQTYFGKDT
     YKAITQDDDV MCTMEYSKIV PLENGEIPVL LLNGRPSSTN YFNSTVLQEW TRATNVRIRL
     LRTKNLLGHL MSVARQDPTV TRRYFYSIKD ISIGGRCMCN GHADTCDVKD PISPVRILAC
     RCQHHTCGIQ CNQCCPGFEQ KKWRQNTNAR PFNCEPCNCH GHTNDCMYDE DVNRKGLSLD
     IHGHYDGGGV CKNCQHNTEG TNCNKCKPKY YRPRGKYWNE TDVCSPCNCD FFYSTGHCEE
     ETGKCECRAA FQPPNCDSCS YGYYGYPQCR ECECNLNGTN GYNCEAVNGI CPCKTNFAGA
     LCKECAESYY GFPECKACQC NKLGSINNDC DIVSGNCTCL SNWGGAQCER CKDGYYNEPT
     CTYCDCDHQG TESEICSKAS GQCICREGFG GSRCDRCLPG YYNYPSCKPC NCSTTGSSAI
     TCDNTGKCNC LINYSGKLCN MCSAGFYNYP ECLACNCNEH GSEGVTCNEN GCFCKPNFDG
     RQCERCKESF YNFPACEDCN CDPAGVIEQF AGCGSVPVGE LCKCKERVTG RICNECKPLY
     WNLTVSNADG CQECDCYIDG TVSGLDTCAP KSGKCHCKPH TMGRQCHECR DGTFDLDGSS
     LFGCKDCSCD VGGSWKSECD KISGQCKCHP RVTGRACTQP LTTHYFPTLH QFQYEYEDGS
     QPSGAQVRYQ YDDAIFPDFS SKGYAVFNDI QNEVRNDLTV FKSSVYRIVI RYKNPNEKNV
     TASILIQSEN PLEVDQTVKV LLRPTTEPEF VTVSGPKGNV PSAVVLDPGR YMFTTKANKN
     VMLDYFVLLP AAYYEASILT RHIANPCELG NMELCRHYKY ANVNVFEPAT TPFIIGANGK
     PTNPTEVYTD SEHLQIVSHV GDIPVLSNTQ KELNYIVDVP RSGRYIFVID YISERNFAVP
     YDVNLRLGND PDSHSSVYLY PCLYSTVCRT PINDDGREKA FYINKDDLQP VTIYADNDDI
     YRVPIISVTA IPVEQWSIDY INPSPVCVIH NQQCATPKFR SVPDSKKIEF ETDHEDRIAT
     NKPPYAAFDE RVKLVHLDNR QDGSIVIESK VSEPHRYVIL VKYYQPNHPK YQLTYTLTAG
     KNQYDGKFDI QHCPSSSGCR GVIRPTGDDW WFDIEDDFKF TLTNPRAQGV WLDYLVVVPL
     DQYNDDLLVE ETFDQTKEFI KNCGHDHYHI THNASEFCKS AVFSLTADYN SGALSCNCDY
     AGSTSFECHP FGGQCQCRKN VIGRQCTACR TGYYGFPDCK VCDCPSTAMC EATTGECMCP
     PNVIGALCDK CAPNTYGFHQ VIGCEECNCN YMGIANGKQQ CDMLNGSCEC RDNIVGRACD
     GCAHGFYDFP RCSRCTCHKP GTELEVCNKI DGSCFCKENV LGRDCDQCKD GTYNLRDDNP
     EGCTTCFCFG KTSRCDSAYL RVYNVSLMRE KAVYSADFHA KNIEFELWEL SPNELVLNET
     TLQADFSIRE SSDQRVAYFG VLDYLLNQNS HISAYGGDLG YTLYFTSGFV GNAIVAPDVI
     LLSADHILVH QSYEQPSSNL PFKNRLQMVE TNFQTQTGKS VSRADFMMAL RDLKTIFIRA
     NYWEQTLNTQ LSDVYLTLAD EDADGTGEYQ FLAVEHCHCP AGYTGHSCED CAPGYHRLNN
     GPYGGYCVPC DCNGHAETCD CATGICKDCQ HSTRGDHCEH CVAGYYGNAT YGTPHDCMIC
     ACPLPYDSNN FAIGCEISES GTEIHCECMR GYTGPRCEAC ANGFFGSPET PGDFCKPCEC
     SGNINPNEQG SCDTRTGECL RCLNNTSGMA CNLCAPGFYG DAINLKNCQS CDCDEVGTLQ
     CDPAVGKCKC HENVIGERCD RCKPDHYGFD SGTGCRACDC GAASNSTQCD EHTGHCFCKP
     GVTGRQCDRC TVDHWRYEKD GCTPCNCNEG YSRAGTGCNP HTGQCVCLPG VIGDRCEACP
     NRWVLTEDGC MECNNCHHAL LDVTDKLRYQ IDGVLQDFQT VTMAFFTSQK LNYYDQLAED
     LEPKVRALEP NSVNLMPSQE LNSELEAASK AYAKQVNQTL GNAFDIRQRS GVLLKNVSAV
     HEEALNSVDQ AKAAIVAVDS LSQNLEATAS TKIDAALEQA QRILNAINST QIELQSNELG
     LDKGRQLYED ITQLVEPIQL QNLSLNALKN DIGEFSDKLE DLYNWSAQSQ SQSGDVEVIN
     VVNSRSYNNS KFDTVSEQQQ GAENNIKEAG NFLINGDLTL DQIDTKLVAL RGALQELKSV
     NKDVDEYLPE RDMQHQEADE LTLKAELHAA ELDVRAKDLA NQYADMTASA EPAIQAATAY
     STIVEAVKAA KQFSEDAINA AGNANEKSDG IQERAGSADM ESAELLQKAR QALVKVQDDL
     EPRLNGSAGK VEGISHQNAA TDNQLKDINI LIKKLPAETQ RDMWKSSNSN ASDALDILQD
     VLEILKPVSS QTPKELDKAR NISRLVDITN KDISQANNQL DNVVISIPTL EDRANDIDKQ
     QQNFGEKSQQ LGDDIEQLKR QLETARRTAN SIQVGVKFTP STVLELKTPE KTPLLATKTK
     LSTFFRTKNP DGFLLYLGND NKTIQKNNDF VAMEIVNGYP IMTIDLGNGP ERIGSSKYVA
     DGNWYEAIIN RVGSKAELTI REQLPNGTVT NHVVDKNLVG TNNVLHVDRN SRLFVGGYPG
     ASDFNVPDDI TTTPFTGEME NLRIGDENVG LWNFVYGEDN NQGVRERDKL LDEQKPVTGL
     RFKGNGYAQL NTRQINFRAR SSIQFRFKAE RDASNGLLFF YGRDNYMAIQ MVRGAIIFLY
     KLGDATFTLG NQDRYNDNQW HHVNAERDGR SGVLKIDDIL ISQRTETQAG DMQLPKLKRM
     YFGGFPGRRN HTDLVEQDFD GCIDNVVISH YNLDLTQNVN ATGVVEGCAP KYSTTLSYLP
     EEYGFLRIAN ISSQNNFYVV LRFKTLQPNG VLFYAANHGQ SANIGLTLDG GYLKLHSMDS
     ELTIDNRQYN DGEDHVVTVQ HNENELRLSV DDDEDKRIGF VQPLEIEGGD IFFGGLPDNF
     IPPKGAISNL AYFVGCISDV TVNGEIINFA DSAEKKGGNI NGCTQDNLAY EAGMLPTYYP
     SGANEVEPPP NMHIHTNAKP TTTTTTTTTS RPTPSLRTTT PTTTRTTTTT TSTTTTTTES
     PASMKDLLVK PQPKLNLPSH PSCKLPISPN YDVDFIEAGY RFYSLQEQYL VFNKLPGFMS
     EQYDMSMSIR TNYPNGILFY AASQESNDFI AVHLLDGRVH HLVRVGNTVQ ANITSEQELL
     DGEWHTVQFV RTNSRISLSI DGIEQEGSVD LYSEQDISPP SLITFPVYVG GITRFLEVEL
     KNQFNFDSNP YYNGCIRDIK VNGLALDEAP TEHHVVPCSD QVESGVFFHQ DKGYVKLFDR
     FMVGADVTIS FDFRPRDPNG LLFSVHGKSS YLILELINNT VTFTVKSDAK NTVVTNYTLP
     DNASYCDGKW RNVLAIKSKF VITIAVDHVS SQPGLGNDSS AITKTHRPLF MGGHHAFNKA
     PGIKTRKTFS GCMKNVKINN KDISITKNLI YGDIWQGVCP LN
//
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