ID B4PQW4_DROYA Unreviewed; 2137 AA.
AC B4PQW4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=Dyak\GE24970 {ECO:0000313|EMBL:EDW96288.2};
GN ORFNames=Dyak_GE24970 {ECO:0000313|EMBL:EDW96288.2};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW96288.2, ECO:0000313|Proteomes:UP000002282};
RN [1] {ECO:0000313|EMBL:EDW96288.2, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
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).
RN [2] {ECO:0000313|EMBL:EDW96288.2, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CM000160; EDW96288.2; -; Genomic_DNA.
DR RefSeq; XP_002096576.2; XM_002096540.2.
DR EnsemblMetazoa; FBtr0271488; FBpp0269980; FBgn0242064.
DR GeneID; 6535960; -.
DR KEGG; dya:Dyak_GE24970; -.
DR eggNOG; KOG4258; Eukaryota.
DR HOGENOM; CLU_000288_166_2_1; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000002282; Chromosome 3R.
DR GO; GO:0005899; C:insulin receptor complex; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0043559; F:insulin binding; IEA:EnsemblMetazoa.
DR GO; GO:0005009; F:insulin receptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0007411; P:axon guidance; IEA:EnsemblMetazoa.
DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblMetazoa.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IEA:EnsemblMetazoa.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IEA:EnsemblMetazoa.
DR GO; GO:0008585; P:female gonad development; IEA:EnsemblMetazoa.
DR GO; GO:0060180; P:female mating behavior; IEA:EnsemblMetazoa.
DR GO; GO:0030707; P:follicle cell of egg chamber development; IEA:EnsemblMetazoa.
DR GO; GO:0007390; P:germ-band shortening; IEA:EnsemblMetazoa.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0042593; P:glucose homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0007446; P:imaginal disc growth; IEA:EnsemblMetazoa.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0007626; P:locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0048542; P:lymph gland development; IEA:EnsemblMetazoa.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IEA:EnsemblMetazoa.
DR GO; GO:0035264; P:multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:EnsemblMetazoa.
DR GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:0061964; P:negative regulation of entry into reproductive diapause; IEA:EnsemblMetazoa.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IEA:EnsemblMetazoa.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; IEA:EnsemblMetazoa.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:EnsemblMetazoa.
DR GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblMetazoa.
DR GO; GO:0070346; P:positive regulation of fat cell proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0010884; P:positive regulation of lipid storage; IEA:EnsemblMetazoa.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:EnsemblMetazoa.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IEA:EnsemblMetazoa.
DR GO; GO:0046622; P:positive regulation of organ growth; IEA:EnsemblMetazoa.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:EnsemblMetazoa.
DR GO; GO:0007285; P:primary spermatocyte growth; IEA:EnsemblMetazoa.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0034059; P:response to anoxia; IEA:EnsemblMetazoa.
DR GO; GO:0042220; P:response to cocaine; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:EnsemblMetazoa.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00064; FU; 1.
DR CDD; cd05032; PTKc_InsR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF525; INSULIN-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDW96288.2};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1201..1296
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1362..1650
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 226..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2054
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2073..2117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2137 AA; 238942 MW; 6512C0CC6FF8BF43 CRC64;
MYNMPRGVTK SKSKRGKIKM ENDMATTTTT CTLGHICVLC RQEMLLDTCC CQQAVEAVDI
SASSDETYSS SNSSSKSSNN SSCQARSEIS SKQVWFLSHD DIVLCRRPKF EEVETTGKKR
DVKCSGHQCS NECNDGSTKN NRHQREKFNI FSNCHNILRT LQSLLLLMFN CGIFNKRRRR
QHQHKQQQQQ QQQVHVNYTK FLWLLQTLAA ATTRLSLSPK NYNHQQLQHN HQLPRATPQQ
KQQHIGEHKS SYYKRNYYYT PWISILLCIL LANTLAIQAV VLPGHTQHLL HNDIADGVDK
NALALTDTHS RWPRSESTQT MRLSQNVKPC KSMDIRNMVA HFNQLENCTV IEGFLLIDLI
NDASPLNRTF PKLTEVTDYI IIYRVTGLHS LSKIFPNLSV IRGNKLFDGY ALVVYSNFDL
MDLGLHKLRS ITRGGVRIEK NHKLCYDRTI DWLEILAENE TQLVVLTENG KEKECRLSKC
PGEIKIEEGH DSAAIEGELS ASCQLHNNRR LCWNSKLCQT KCPEKCRNNC IDDHTCCSQD
CLGGCVIDKN GNESCISCRN VSFNNICMDT CPKGYYQFDS RCVTASECTT LTKFETNNVY
SGIPYNGQCI THCPTGYQKS ENKRMCEPCP GGKCDKECSS GLIDSLERAR EFHGCTIITG
TEPLTISIKR ESGAHVMDEL KYGLAAVHKI QSSLMVHLTY GLKSLKFFQS LTEISGDPPM
DADKYALYVL DNRDLDELWA PNQTVFIRKG GVFFHFNPKL CVSTINQLLP MLASSPKFFE
KSDVGADSNG NRGSCGTAVL NVTLQSVGAN SAMLNVTTKV EIGEPQKPSN ATIVFKDPRA
FIGFVFYHMI DPYGNSTKSS DDPCDDRWKV SSPDKSGIMV FSNLIPYTNY SYYVRTMAIS
SELTNAESDV KNFRTNPGRP SKVTEVVATA ISDSKINVTW SYLDKPYGVL TRFFLKAKLI
NRPTRNNNRD YCTEPLVKAM ENDLPATTPT KKTPDPSAGD CKCVEGSKKT SSQEYDDRKV
QAGMEFENAL QNFIFVPNIR KSKNGSTDKS DGAEDAALDS NAIPNGGATN TSRQRRDLAL
EPELDDVEGS VLLRHVRSIT DDSDAFFEKD DENTYKDEEL LSSNRQFYEV FAKELPPNQT
HFVFEKLRHF TRYAIFVVAC REEIPSEKLR DSTFKKSLCS DYDTVFQTTK RKKFADLVMD
LKVDLEHANN TESPVRVRWT PPVDPNGEIV TYEVVYKLLK PDQLEEGKCI PAADFNQTAG
YLIKLNEGPY SFRVRANSIA GYGDFTKVEH IKVEPPPSYA KVFFWLLGIG LSVLIVSLFG
YVCYLHKRKV PSNDLHMNTE VNPFYASMQY IPDDWEVLRE NIIQLSPLGQ GSFGMVYEGI
LKSFPPSGLD RECAIKTVNE NATDRERTNF LSEASVMKEF DTYHVVRLLG VCSRGQPALV
VMELMKKGDL KSYLRAHRPE ERDEAMITYL NRIGVTGNVQ PPTYGRIYQM AIEIADGMAY
LAAKKFVHRD LAARNCMVAD DLTVKIGDFG MTRDIYETDY YRKGTKGLLP VRWMPPESLR
DGVYSSASDV FSFGVVLWEM ATLAAQPYQG LSNEQVLRYV IDGGVMERPE NCPEFLHKLM
QRCWHHRSSA RPSFLDIIAY LESQCPNSKF KDVSFYHSEA GLQHREKERK ERNQLDAFAA
VPLDQDLQDR EQQEDATTPL RMGDYQPNSS LDQPPESPIA MVDDQGTHLP FSLPSGFIAS
STPDGQTAMP TAFQNIPATQ GDISAAYVLP DTDALDGDRG YEIYDPSPKC AELPTSRSGS
TGGGGKLSGE QHLLPRRGRQ PAIMSSSMPD DVIGGSSLQP STASAASSNA SSHTGRQSLK
KTVADTVRNK ANFINRHLFN HKRTGSNTSH KSNASNAPST SSNTNLTSHP VAMGNLGTIE
SGGSGSAGSY TGTPRFYTPT ATPGGGSGMA ISDNPNYRLL DESIASEQAT ILTTSSPNPN
YEMMRPTGSL VSLTYPNYIP RNEAPVQMAG VTISHNPNYQ PMQAPLNARQ SQSSSDEDNE
QEEDDEDEDD DVDDEHVEHI KMERMPLSRP RQRALPSKTQ PPRSRSVSQT RKSPTNPNSG
VGATGAGNRS NLLKENWLRP ASTPRPPPPN GFIGREA
//
