ID A0A0B4LFF8_DROME Unreviewed; 2456 AA. AC A0A0B4LFF8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 28-JUN-2023, entry version 63. DE SubName: Full=Rho guanine nucleotide exchange factor 2, isoform H {ECO:0000313|EMBL:AHN56311.1}; GN Name=RhoGEF2 {ECO:0000313|EMBL:AHN56311.1, GN ECO:0000313|FlyBase:FBgn0023172}; GN Synonyms=Dmel\CG9635 {ECO:0000313|EMBL:AHN56311.1}, DRhoGEF GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF {ECO:0000313|EMBL:AHN56311.1}, GN DRhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, DrhoGEF2 GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, GN Gef2 {ECO:0000313|EMBL:AHN56311.1}, l(2)04291 GN {ECO:0000313|EMBL:AHN56311.1}, RG2 {ECO:0000313|EMBL:AHN56311.1}, GN Rho-GEF2 {ECO:0000313|EMBL:AHN56311.1}, RhoGEF GN {ECO:0000313|EMBL:AHN56311.1}, RhoGef2 {ECO:0000313|EMBL:AHN56311.1}, GN rhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, rhogef2 GN {ECO:0000313|EMBL:AHN56311.1}, RhoGF2 {ECO:0000313|EMBL:AHN56311.1}, GN shar {ECO:0000313|EMBL:AHN56311.1}, Su(Rho1)2B GN {ECO:0000313|EMBL:AHN56311.1}, T2 {ECO:0000313|EMBL:AHN56311.1}; GN ORFNames=CG9635 {ECO:0000313|EMBL:AHN56311.1, GN ECO:0000313|FlyBase:FBgn0023172}, Dmel_CG9635 GN {ECO:0000313|EMBL:AHN56311.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., 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 [2] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Membrane {ECO:0000256|ARBA:ARBA00004370}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE013599; AHN56311.1; -; Genomic_DNA. DR RefSeq; NP_001286515.1; NM_001299586.1. DR SMR; A0A0B4LFF8; -. DR EnsemblMetazoa; FBtr0340124; FBpp0309117; FBgn0023172. DR GeneID; 36915; -. DR AGR; FB:FBgn0023172; -. DR CTD; 36915; -. DR FlyBase; FBgn0023172; RhoGEF2. DR VEuPathDB; VectorBase:FBgn0023172; -. DR GeneTree; ENSGT00940000168706; -. DR OrthoDB; 2875542at2759; -. DR BioGRID-ORCS; 36915; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 36915; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0023172; Expressed in eye disc (Drosophila) and 27 other tissues. DR ExpressionAtlas; A0A0B4LFF8; baseline and differential. DR GO; GO:0030478; C:actin cap; IDA:FlyBase. DR GO; GO:0005826; C:actomyosin contractile ring; IDA:FlyBase. DR GO; GO:0045179; C:apical cortex; IDA:FlyBase. DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase. DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase. DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase. DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase. DR GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase. DR GO; GO:0007375; P:anterior midgut invagination; IMP:FlyBase. DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase. DR GO; GO:0007349; P:cellularization; IMP:FlyBase. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase. DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase. DR GO; GO:0007277; P:pole cell development; IMP:FlyBase. DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:FlyBase. DR GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase. DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase. DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase. DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase. DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase. DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase. DR CDD; cd20832; C1_ARHGEF-like; 1. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd13329; PH_RhoGEF; 1. DR CDD; cd08756; RGS_GEF_like; 1. DR CDD; cd00160; RhoGEF; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR041020; PH_16. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR015212; RGS-like_dom. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR044926; RGS_subdomain_2. DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1. DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF17838; PH_16; 1. DR Pfam; PF09128; RGS-like; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0B4LFF8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 260..336 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 1047..1097 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 1435..1630 FT /note="DH" FT /evidence="ECO:0000259|PROSITE:PS50010" FT REGION 1..251 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 343..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..567 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 665..758 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1130..1180 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1247..1300 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1312..1340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1775..1795 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1840..1894 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1912..1943 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2087..2122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2151..2326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2415..2456 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1422..1449 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 2360..2387 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..17 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..68 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..126 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 127..143 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 177..251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..459 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 527..554 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 665..685 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 693..712 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1130..1145 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1163..1180 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1270..1291 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1312..1330 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1775..1792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2169..2186 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2199..2245 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2246..2271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2272..2288 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2291..2326 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2417..2447 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2456 AA; 269559 MW; B958C362CF326394 CRC64; MDDPSIKKRL LDLYTDEHEY DEVQEIPEES SIQPPETSTS HTSTNGSSHS GPGTATGPGA TSAGPSAGAP QSPVIVVDSV PELPAPKQKS VKNSKSKQKQ KQLANKSKIP RSPSLASSLS SLASSLSGHR DRDKDRDKDR ENQNAVPPQT PPLPPSYKQN QMNGDSTAAA GGGVSAPATP TTANNNNASH NNGSIMGGGV QLNQSDNSNP VLQAPGERSS LNLTPLSRDL SGGHTQESTT PATTPSTPSL ALPKNFQYLT LTVRKDSNGY GMKVSGDNPV FVESVKPGGA AEIAGLVAGD MILRVNGHEV RLEKHPTVVG LIKASTTVEL AVKRSQKLTR PSSVSVVTPS TPILSGRDRT ASITGPQPVD SIKRREMETY KIQTLQKMLE QEKLNLERLK SDQNNPSYKL SEANIRKLRE QLHQVGAEQQ RMSHQAESMS QSMHQHTSTP TSQQFFHPHQ QQHRFKETGP TSKGKNKFLI SRSLIEEDVP PPLPQRNPPR QLNLDLKNGN ASPGGSHLVA PVSDLDRATS PQLNRSQQQQ LPSSTDNSPS NAKSKRSKIK TKALSDPKMS TQMFLQMESA SAAGAAGGSI EVDGGPPPLP PRLPGMMTED MSRGSCQNLA QPNSVGTAFN YPLVSTTTAV QNDNLNIAFP LSQRPNIVQQ LQQYQQQQQH QMSGGQATGA LGQTPNLGKN KHRRVGSSPD NMHPRHPDRI TKTTSGSWEI VEKDGESSPP GTPPPPYLSS SHMTVLEDPN ENNRGAAAAG PGVFIESHQF TPMAGASSPI PISLHSSHMH AAQSNDTQKE IISMEDENSD LDEPFIDENG PFNNLTRLLE AENVTFLAIF LNYVISNSDP APLLFYLITE LYKEGTSKDM RKWAYEIHST FLVPRAPLSW YRQDESLARE VDNVLQLEYD KVEILRTVFL RSRKRAKDLI SEQLREFQQK RTAGLGTIYG PTDDKLAEAK TDKLREQIID KYLMPNLHAL IEDENGSPPE DVRKVALCSA LSTVIYRIFN TRPPPSSIVE RVHHFVSRDK SFKSRIMGKN RKMNVRGHPL VLRQYYEVTH CNHCQTIIWG VSPQGYHCTD CKLNIHRQCS KVVDESCPGP LPQAKRLAHN DKISKFMGKI RPRTSDVIGN EKRSRQDEEL DVELTPDRGQ ASIVRQPSDR RPDANISIRS NGNTSCNTSG LNTTDLQSSF HGSCANDSIN PGGGAGCNMD LSTSVASTTP STSGSVAAGL SAFAELNALD TVDKEARRER YSQHPKHKSA PVSVNRSESY KERLSNKRNR NSRRKTSDPS LSSRPNDEQL DLGLSNATYV GSSNSSLSSA GGSESPSTSM EHFAAPGAAG GVQVPPMGLN QNQHPHLLIQ QHAQQYCQQD SFQAGLAGAA GSSAASNSSF WNAGHPLPVA RWTLESEDED DVNEADWSSM VAAEVLAALT DAEKKRQEII NEIYQTERNH VRTLKLLDRL FFLPLYESGL LSQDHLLLLF PPALLSLREI HGAFEQSLKQ RRIEHNHVVN TIGDLLADMF DGQSGVVLCE FAAQFCARQQ IALEALKEKR NKDEMLQKLL KKSESHKACR RLELKDLLPT VLQRLTKYPL LFENLYKVTV RLLPENTTEA EAIQRAVESS KRILVEVNQA VKTAEDAHKL QNIQRKLDRS SYDKEEFKKL DLTQHHLIHD GNLTIKKNPS VQLHGLLFEN MIVLLTKQDD KYYLKNLHTP LSITNKPVSP IMSIDADTLI RQEAADKNSF FLIKMKTSQM LELRAPSSSE CKTWFKHFSD VAARQSKNRS KNASSNHDTS ISDPALAAIP HSNTKESLEL STDTVQPLAA TATLTTTPLA PMLPIATVTP APATNNSNVS SLTGVQLRNP QRDATASESD ADYVNTPKPR SSQNEVNRTM SIRSTGEPIQ KYSANGTEAN DVTLRHSQST RESVRPGSTG EERNSTYGMV GGNSKRDSAS IVCSNNSNNT RTLLMQSPLV DPTAIQVSIS PAHTAEPVLT PGEKLRRLDA SIRNDLLEKQ KIICDIFRLP VEHYDQIVDI AMMPEAPKDS ADIALAAYDQ IQTLTKMLNE YMHVTPEQEV SAVSTAVCGH CHEKEKLRKK VAPSSSFSSS PPPLPPPNRQ HAQAQAQIPP SRLMPKLQTL DLDEVAIHED DDGYCEIDEL RLPAIPSKPH ERPTTPLAPF NTEPKTSQSV IDASKRQSTD AVPEGLLEQE PLEGDKTETK GEDNEVKTVP SDKLSESCNE ERQCVEADIT KEVADPTTSK NEAAASVDEL PSQSREIKTA ENASKSVADK KEDNEETIEE GVASTVDSST QTSPTESPKE TDKLTGGSSS TCGPNRIQHA SVLEPSVPCH ALSSIVTILN EQISMLLPKI NERDMERERL RKENQHLREL LSALHDRQRV DEVKETPFDL KKLMHAEDVE FDDDIDAISN SSLTPTPTPI PTASPSASGQ VETAEAMRIT STEDEE //