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ID 7LESS_DROME Reviewed; 2554 AA.
AC P13368; Q9TYI0; Q9U5V7; Q9VZ36;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-APR-2018, entry version 172.
DE RecName: Full=Protein sevenless;
DE EC=2.7.10.1;
GN Name=sev; Synonyms=HD-265; ORFNames=CG18085;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP LYS-2242.
RC STRAIN=Canton-S;
RX PubMed=2840202; DOI=10.1016/0092-8674(88)90193-6;
RA Basler K., Hafen E.;
RT "Control of photoreceptor cell fate by the sevenless protein requires
RT a functional tyrosine kinase domain.";
RL Cell 54:299-311(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=3138161; DOI=10.1101/gad.2.6.620;
RA Bowtell D.L.L., Simon M.A., Rubin G.M.;
RT "Nucleotide sequence and structure of the sevenless gene of Drosophila
RT melanogaster.";
RL Genes Dev. 2:620-634(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2349-2408.
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [6]
RP IDENTIFICATION OF FN-III REPEATS.
RX PubMed=2317871; DOI=10.1016/0092-8674(90)90209-W;
RA Norton P.A., Hynes R.O., Ress D.J.G.;
RT "Sevenless: seven found?";
RL Cell 61:15-16(1990).
RN [7]
RP INTERACTION WITH DAB.
RX PubMed=9671493; DOI=10.1128/MCB.18.8.4844;
RA Le N., Simon M.A.;
RT "Disabled is a putative adaptor protein that functions during
RT signaling by the sevenless receptor tyrosine kinase.";
RL Mol. Cell. Biol. 18:4844-4854(1998).
CC -!- FUNCTION: Receptor for an extracellular signal required to
CC instruct a cell to differentiate into an R7 photoreceptor. The
CC ligand for sev is the boss (bride of sevenless) protein on the
CC surface of the neighboring R8 cell. {ECO:0000269|PubMed:2840202}.
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC ProRule:PRU10028}.
CC -!- SUBUNIT: May form a complex with drk and Sos. Binds the
CC phosphotyrosine interaction domain (PID) of Dab.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: It is unclear whether the potential membrane spanning
CC region near the N-terminus is present as a transmembrane domain in
CC the native protein or serves as a cleaved signal sequence.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31960.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
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DR EMBL; J03158; AAA28882.1; -; Genomic_DNA.
DR EMBL; X13666; CAA31960.1; ALT_INIT; mRNA.
DR EMBL; X13666; CAB55310.1; -; mRNA.
DR EMBL; AE014298; AAF47992.2; -; Genomic_DNA.
DR EMBL; AJ002917; CAA05752.1; -; Genomic_DNA.
DR PIR; A28912; TVFF7L.
DR RefSeq; NP_511114.2; NM_078559.3.
DR ProteinModelPortal; P13368; -.
DR BioGrid; 58454; 44.
DR IntAct; P13368; 10.
DR STRING; 7227.FBpp0073249; -.
DR PaxDb; P13368; -.
DR PRIDE; P13368; -.
DR GeneID; 32039; -.
DR KEGG; dme:Dmel_CG18085; -.
DR UCSC; CG18085-RA; d. melanogaster.
DR CTD; 32039; -.
DR FlyBase; FBgn0003366; sev.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; ENOG410XPVX; LUCA.
DR InParanoid; P13368; -.
DR KO; K05088; -.
DR OrthoDB; EOG091G003T; -.
DR PhylomeDB; P13368; -.
DR BRENDA; 2.7.10.1; 1994.
DR SignaLink; P13368; -.
DR ChiTaRS; sev; fly.
DR GenomeRNAi; 32039; -.
DR PRO; PR:P13368; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003366; -.
DR ExpressionAtlas; P13368; differential.
DR Genevisible; P13368; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; TAS:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:FlyBase.
DR GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0045678; P:positive regulation of R7 cell differentiation; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; NAS:FlyBase.
DR GO; GO:0045467; P:R7 cell development; NAS:FlyBase.
DR GO; GO:0045466; P:R7 cell differentiation; TAS:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; NAS:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 7.
DR SMART; SM00135; LY; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 7.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Sensory transduction; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase; Vision.
FT CHAIN 1 2554 Protein sevenless.
FT /FTId=PRO_0000058928.
FT TOPO_DOM 1 2123 Extracellular. {ECO:0000255}.
FT TRANSMEM 2124 2147 Helical. {ECO:0000255}.
FT TOPO_DOM 2148 2554 Cytoplasmic. {ECO:0000255}.
FT DOMAIN 440 533 Fibronectin type-III 1.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 824 924 Fibronectin type-III 2.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT REPEAT 1010 1053 LDL-receptor class B.
FT {ECO:0000269|PubMed:2317871}.
FT DOMAIN 1202 1290 Fibronectin type-III 3.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 1294 1397 Fibronectin type-III 4.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 1801 1901 Fibronectin type-III 5.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 1902 1988 Fibronectin type-III 6.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 1995 2117 Fibronectin type-III 7.
FT {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT DOMAIN 2209 2485 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT NP_BIND 2215 2223 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT COMPBIAS 58 64 Poly-Ser.
FT COMPBIAS 112 118 Poly-Leu.
FT COMPBIAS 166 169 Poly-Ala.
FT COMPBIAS 2034 2046 Arg-rich.
FT ACT_SITE 2343 2343 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028}.
FT BINDING 2242 2242 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT MOD_RES 2380 2380 Phosphotyrosine; by autocatalysis.
FT {ECO:0000250}.
FT CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 617 617 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 647 647 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 966 966 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1228 1228 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1313 1313 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1353 1353 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1550 1550 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1557 1557 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1639 1639 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1725 1725 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1756 1756 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1804 1804 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1889 1889 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1947 1947 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2073 2073 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT MUTAGEN 2242 2242 K->M: Inactivates the protein.
FT {ECO:0000269|PubMed:2840202}.
FT CONFLICT 392 392 V -> M (in Ref. 1; AAA28882).
FT {ECO:0000305}.
FT CONFLICT 663 663 A -> T (in Ref. 3; AAF47992).
FT {ECO:0000305}.
FT CONFLICT 1703 1703 N -> H (in Ref. 3; AAF47992).
FT {ECO:0000305}.
FT CONFLICT 1730 1731 RG -> KE (in Ref. 3; AAF47992).
FT {ECO:0000305}.
FT CONFLICT 1741 1741 V -> M (in Ref. 3; AAF47992).
FT {ECO:0000305}.
FT CONFLICT 1823 1823 E -> Q (in Ref. 2; CAA31960/CAB55310).
FT {ECO:0000305}.
FT CONFLICT 2271 2271 C -> R (in Ref. 1; AAA28882).
FT {ECO:0000305}.
SQ SEQUENCE 2554 AA; 287025 MW; 09E238A0F27684F8 CRC64;
MTMFWQQNVD HQSDEQDKQA KGAAPTKRLN ISFNVKIAVN VNTKMTTTHI NQQAPGTSSS
SSNSQNASPS KIVVRQQSSS FDLRQQLARL GRQLASGQDG HGGISTILII NLLLLILLSI
CCDVCRSHNY TVHQSPEPVS KDQMRLLRPK LDSDVVEKVA IWHKHAAAAP PSIVEGIAIS
SRPQSTMAHH PDDRDRDRDP SEEQHGVDER MVLERVTRDC VQRCIVEEDL FLDEFGIQCE
KADNGEKCYK TRCTKGCAQW YRALKELESC QEACLSLQFY PYDMPCIGAC EMAQRDYWHL
QRLAISHLVE RTQPQLERAP RADGQSTPLT IRWAMHFPEH YLASRPFNIQ YQFVDHHGEE
LDLEQEDQDA SGETGSSAWF NLADYDCDEY YVCEILEALI PYTQYRFRFE LPFGENRDEV
LYSPATPAYQ TPPEGAPISA PVIEHLMGLD DSHLAVHWHP GRFTNGPIEG YRLRLSSSEG
NATSEQLVPA GRGSYIFSQL QAGTNYTLAL SMINKQGEGP VAKGFVQTHS ARNEKPAKDL
TESVLLVGRR AVMWQSLEPA GENSMIYQSQ EELADIAWSK REQQLWLLNV HGELRSLKFE
SGQMVSPAQQ LKLDLGNISS GRWVPRRLSF DWLHHRLYFA MESPERNQSS FQIISTDLLG
ESAQKVGESF DLPVEQLEVD ALNGWIFWRN EESLWRQDLH GRMIHRLLRI RQPGWFLVQP
QHFIIHLMLP QEGKFLEISY DGGFKHPLPL PPPSNGAGNG PASSHWQSFA LLGRSLLLPD
SGQLILVEQQ GQAASPSASW PLKNLPDCWA VILLVPESQP LTSAGGKPHS LKALLGAQAA
KISWKEPERN PYQSADAARS WSYELEVLDV ASQSAFSIRN IRGPIFGLQR LQPDNLYQLR
VRAINVDGEP GEWTEPLAAR TWPLGPHRLR WASRQGSVIH TNELGEGLEV QQEQLERLPG
PMTMVNESVG YYVTGDGLLH CINLVHSQWG CPISEPLQHV GSVTYDWRGG RVYWTDLARN
CVVRMDPWSG SRELLPVFEA NFLALDPRQG HLYYATSSQL SRHGSTPDEA VTYYRVNGLE
GSIASFVLDT QQDQLFWLVK GSGALRLYRA PLTAGGDSLQ MIQQIKGVFQ AVPDSLQLLR
PLGALLWLER SGRRARLVRL AAPLDVMELP TPDQASPASA LQLLDPQPLP PRDEGVIPMT
VLPDSVRLDD GHWDDFHVRW QPSTSGGNHS VSYRLLLEFG QRLQTLDLST PFARLTQLPQ
AQLQLKISIT PRTAWRSGDT TRVQLTTPPV APSQPRRLRV FVERLATALQ EANVSAVLRW
DAPEQGQEAP MQALEYHISC WVGSELHEEL RLNQSALEAR VEHLQPDQTY HFQVEARVAA
TGAAAGAASH ALHVAPEVQA VPRVLYANAE FIGELDLDTR NRRRLVHTAS PVEHLVGIEG
EQRLLWVNEH VELLTHVPGS APAKLARMRA EVLALAVDWI QRIVYWAELD ATAPQAAIIY
RLDLCNFEGK ILQGERVWST PRGRLLKDLV ALPQAQSLIW LEYEQGSPRN GSLRGRNLTD
GSELEWATVQ PLIRLHAGSL EPGSETLNLV DNQGKLCVYD VARQLCTASA LRAQLNLLGE
DSIAGQLAQD SGYLYAVKNW SIRAYGRRRQ QLEYTVELEP EEVRLLQAHN YQAYPPKNCL
LLPSSGGSLL KATDCEEQRC LLNLPMITAS EDCPLPIPGV RYQLNLTLAR GPGSEEHDHG
VEPLGQWLLG AGESLNLTDL LPFTRYRVSG ILSSFYQKKL ALPTLVLAPL ELLTASATPS
PPRNFSVRVL SPRELEVSWL PPEQLRSESV YYTLHWQQEL DGENVQDRRE WEAHERRLET
AGTHRLTGIK PGSGYSLWVQ AHATPTKSNS SERLHVRSFA ELPELQLLEL GPYSLSLTWA
GTPDPLGSLQ LECRSSAEQL RRNVAGNHTK MVVEPLQPRT RYQCRLLLGY AATPGAPLYH
GTAEVYETLG DAPSQPGKPQ LEHIAEEVFR VTWTAARGNG APIALYNLEA LQARSDIRRR
RRRRRRNSGG SLEQLPWAEE PVVVEDQWLD FCNTTELSCI VKSLHSSRLL LFRVRARSLE
HGWGPYSEES ERVAEPFVSP EKRGSLVLAI IAPAAIVSSC VLALVLVRKV QKRRLRAKKL
LQQSRPSIWS NLSTLQTQQQ LMAVRNRAFS TTLSDADIAL LPQINWSQLK LLRFLGSGAF
GEVYEGQLKT EDSEEPQRVA IKSLRKGASE FAELLQEAQL MSNFKHENIV CLVGICFDTE
SISLIMEHME AGDLLSYLRA ARATSTQEPQ PTAGLSLSEL LAMCIDVANG CSYLEDMHFV
HRDLACRNCL VTESTGSTDR RRTVKIGDFG LARDIYKSDY YRKEGEGLLP VRWMSPESLV
DGLFTTQSDV WAFGVLCWEI LTLGQQPYAA RNNFEVLAHV KEGGRLQQPP MCTEKLYSLL
LLCWRTDPWE RPSFRRCYNT LHAISTDLRR TQMASATADT VVSCSRPEFK VRFDGQPLEE
HREHNERPED ENLTLREVPL KDKQLYANEG VSRL
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