ID B4KEJ3_DROMO Unreviewed; 3389 AA.
AC B4KEJ3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Laminin subunit alpha-1 {ECO:0008006|Google:ProtNLM};
GN Name=Dmoj\GI12813 {ECO:0000313|EMBL:EDW11872.2};
GN ORFNames=Dmoj_GI12813 {ECO:0000313|EMBL:EDW11872.2};
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:EDW11872.2, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:EDW11872.2, 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 -!- 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; CH933807; EDW11872.2; -; Genomic_DNA.
DR RefSeq; XP_002002430.2; XM_002002394.2.
DR SMR; B4KEJ3; -.
DR EnsemblMetazoa; FBtr0163538; FBpp0162030; FBgn0135570.
DR GeneID; 6576440; -.
DR KEGG; dmo:Dmoj_GI12813; -.
DR eggNOG; KOG1836; Eukaryota.
DR HOGENOM; CLU_000301_0_0_1; -.
DR InParanoid; B4KEJ3; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000009192; 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007502; P:digestive tract mesoderm development; IEA:EnsemblMetazoa.
DR GO; GO:0010669; P:epithelial structure maintenance; IEA:EnsemblMetazoa.
DR GO; GO:0008406; P:gonad development; IEA:EnsemblMetazoa.
DR CDD; cd00055; EGF_Lam; 16.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR PANTHER; PTHR10574:SF448; WING BLISTER, ISOFORM B; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 15.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 172..423
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 533..576
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 577..625
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 646..840
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 878..927
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1000..1043
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1044..1090
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1091..1136
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1169..1217
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1218..1265
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1313..1358
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1359..1413
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1454..1646
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1689..1736
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1737..1791
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1792..1839
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2599..2787
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2791..3010
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3022..3200
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3205..3383
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 87..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2290..2327
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 553..562
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 596..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 897..906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1044..1056
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1046..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1065..1074
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1113..1122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1169..1181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1171..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1190..1199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1218..1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1220..1237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1239..1248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1313..1325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1315..1332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1334..1343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1384..1393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1708..1717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1720..1734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1761..1770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1792..1804
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1794..1811
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1813..1822
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3356..3383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3389 AA; 377028 MW; 27919ADBF6F8520F CRC64;
MKVKIKERKL SSCAKCCLIL PTTTMLFLIL LPCLLTVQVE GRRAKQLKQR LVVLPPAQML
KEYSTETLNA SSVEQLEASI VSWTGERISQ RKSSSTSRGG QSTRRRKTKS GLLIESNIGS
SESDMAAASS EIRNGKKSKQ RGRNGRLQRT DGKSNANEMR LRNTQQADEA ISAGGLYPPL
FNVAPRASIT VNATCGQNGA EEYCKLVDAY PHRNWAKHCG TCNAHSSDRA KQRPIESLIS
PSSSFEESWW QSPTLQGGRQ FEYVTITLDL KQTYQIFFVM LKSANSPRPA SWILEKSIDG
ITYEPWQYFG LSDADCKRRY NRSGRNGKYI FKNDTEVICS TQYSKPLPLE NGELHVSLLK
NRPGAQEQTP ELMRFITARF MRIRLQGMHS TANLDNSVDW LLDSQSLEKR SFYSLKQLRV
SARLDCHGHA NRTQDVDAGN AYSLLQCACQ HNTCGLQCDE CCPLFQDRAW SPGGECEICQ
CNGHAQSCSY DAFLERGICQ ECGNNTAGNE CEFCAGGFYR ELGAAPTEPC LPCACNPQRS
EGSCAPVGGA CHCLEGFQGP HCEECAPNYY GDDCRRCECD SRGTVPGSAC AGSCQCKAHV
QGDTCSECAV GYFDLSEQKA EGCSRCWCSH VSETCHSAKL QTLAFETLND WRLTDIQRAQ
AIAVAVDAET KRLIFGNELD EVEAIYWQAP AGYLGNRLTS YGARLQLQLS WVVMRGDTSG
KPTTGPNVIL CAKNGLKIAY ADESYEGLEL ALNVPLTEHG WYHVPPAVKD IKTRLRRTEG
GDYHGEPVTR AQFLSVLVSL DALLIRAAYH TDQVETSLEH AVIYSGGLEL GGQATSQVEQ
CVCPAGYTGL SCESCAFGYK RIYENTTDHR LLGKCIPCPC NGHSNSCDLQ SGNCGDCMHN
TYGERCERCQ LGFYGNPLQG TPHDCKRCAC PLLEDSNNFS PSCQLKSYNY MDLNPQFELI
EHAEYICTQC PEGYTGDHCQ VCDDGYYGNP LKLGNRCRRC ECDGGPCNVT TGACITCHGN
TEGWHCERCK RGYWGDPAVG CEPCHCHPEG SESGLCDSTD GQCLCRPRFA GQKCNECDVG
YAHVERQCVP CNCDALGAAV LGNCNATTGQ CICKEGVMGV KCSECLDGYF GMNVNAEQLE
DLAALRLAEN DGDWELVNEN DETVACEDCQ CSPVGSLSTA CDKRTGQCSC LLNVAGRRCD
KCKPGHWNLT QGVGCHDCQC DPHGARGHEC NPWTGQCDCK IGVGGRHCNE CTEGFYGFST
DGCQRCAACA AEGQVCDPLN GRCICPKYTR GLGCGQCVPG TWGWQARLGC RECECDHIGS
IGQQCATVGG QCQCREGYAG RTCNSCAVGY FGYPECRRCG CDVEGSFTRA DGLIACDSNG
QCPCKSLVVG LKCDTCMQST FGLSALNPEG CTRCFCFGRA AECEQSELSW GHIRMPEARN
LSVQQLRPQH VPNGDFEYIV VVQMAGSVSY REDAEIQRMN DLSLVPRSTG NVSIGAYTQF
YQPLYFQLPP QFYGDRTTSY GGYLYFSLIT DGAQMPLERK ILSQYPLVQL HAHTKLVLDF
YEHEEFEYSL NVTHRVPLHE SYWKYHQNNQ AVDRGTLMAA LQNVKHIFLR AFAFADFQQV
VLHSVHMDAA IYVQGSTNLL AKGVEQCKCP KRFAGLSCQD PGRSFYRWRN TSDMESVFIE
DLIGRAAPCH CNGRSNDCDR ETGVCLNCRD NSGGAHCQHC ADGYYGDPNS RHGCQACPCP
ETNRNFARGC NVREGEVSCV CKPGYTGRLC EHCQPGYFGS PMQYPNSSCQ ACECHVVGIR
AEGCDAQTGQ CHCREGVTGL KCDKCMAARH HLQDQGCRLC DNCTLLLLDY VELVGHKLRR
GLHNMDLTGI PAPYLKLSEY ERAYKEWRTR QQDVSQARQL LLGYDVGALL KMDAHAENNK
FQSRKALATI GKRQHALQSM QESALVLQQD VRKMRGEQMQ TLQDLRNYGT AAHHLSLPTA
LKQARFYLEA IQQHHHVVQD IRSSSDCAWQ LFYATGNASD AAYDQRARLE MLWRDLNQTN
YRVADMRLHL DRTQDVESEA DDVLEHVRNL SGHVAEQYQE LSALDQHIQQ QLNPDQTELG
YKNLRTSIEH QLQLNEQRRQ LAAAAAQLNA TLLVELELQR EVRKHWLPKA EKHATRLLER
SNEYAKQFQP TRNAARIAML ASSAHSNISL AIAAAQQASL LAKERVFEAQ RTLYPSDGSS
MIERAKHSLQ RSKQLQREAL QQMQKSTVLK GKLQQQQQQV EGIKRTIFET GQRSNNITSQ
LQLLRNSSAR RNAQQSMKLA QHTSDEMRQE LRKAKELQQS IQHMRKSFAM LEPDWEIKLG
MAEENISLTK TNLRLGNVSL SYIEQQAAKE QQIFEQWNNS MASQLQQLRD QIAKARHAAE
AIDVSLESLG PKCSRSYLPV SYGLSTSNSL RLSFSLANHM GNSPLLLVQG SEGRHITLEL
YKRHVRLIWY LGGSTATITH PLEVQTRDPK YDDAWYHVEA NRTLNLGSLL VRRMNNFGSL
MPGSPVTGST DSEHTRFYQT HDERILLGGQ ASKDQTPGLN VVVHQVEVDN KPLGIWNFIS
SEGRCGGAMI GARESSASSV ARHFNGLGYA QLKKTRPRPY RKNLFALQMT FRTLDENALL
FLAVDDKNNR SVSVTLSRGR IMFRIDYGDE SKLEINTTKK YNTGQWIKIE AAREFSTRRS
TENGMLRVNN DRPISGAPTL PVKSHMLPDL SKAVYYLGGV PPGFTSGTTK APGADNPFLG
CMMDVQVNGE TYDPLESSTY FGVESSCKDM ITKAGFSGNG YLELPSQSLR KRANAALVFR
TLQADCLLLL AAYPPEVLAD YDAKDIKGNY SMSLVDGQLQ VWINSGRSFI KMSSNASQLN
DGELHVINLS KTGRRLELMV DDELQEVRTL TGSPSLISLP QDAGGLYIGG APPHEIYTPL
APTFVKLEGA VRDVVFNNRT INFNDALTFV NVQIGRNGPV MGSPKGALYD VLLKTEPMIG
KSFTASPEGC KRIGSYSYEP NAFKFGDELY SYSQLKLPER HFWQRNFQLS FEFRSFYPNG
MLYLSPGSKE KPKHYVTLLL KDGQLVLIVR GRRREELLLT AKLNDGEWHR VTIGCHDRKV
TLSVEIGRTD QKTSAQMKVP KKIGASQLML VGGLPQAPVK VPSELYMRLE PFKGCLRRFS
INNSTQDLAR PGKHANVGQC FPKVERGSYF PGDAYAIYKR NFHVAKYLEL ELEFRTSELS
GILLSVSEPN NFPSLSLELS NGNIVFSCDL GDGVPFRVES TLPDKYALCD NKWHNISALY
DGEQIALRID QLPATISMSS QRNAGKVQTR SPLYIGGLPD IAPSGCLLSR DNFKGCIRNV
SIRNERRDWI DMDDLHNVLL SECLVSSDD
//
