C3G_DROME
ID C3G_DROME Reviewed; 1571 AA.
AC O77086; Q1ECB6; Q7YU30; Q86B63; Q9W3W3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Guanine nucleotide-releasing factor 2;
DE AltName: Full=CRK SH3-binding GNRP;
DE Short=DC3G;
GN Name=C3G; ORFNames=CG42328;
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:0000312|EMBL:AAF46200.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Eye imaginal disk;
RX PubMed=9878058; DOI=10.1093/emboj/18.1.145;
RA Ishimaru S., Gaul U., Hanafusa H.;
RT "Activation of the Drosophila C3G leads to cell fate changes and
RT overproliferation during development, mediated by the RAS-MAPK pathway and
RT RAP1.";
RL EMBO J. 18:145-155(1999).
RN [2] {ECO:0000305}
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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., 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.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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., Stapleton M.,
RA Yamada C., 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:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1036-1571.
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496; SER-523; THR-524;
RP SER-526 AND SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Guanine nucleotide-releasing protein that binds to SH3 domain
CC of Crk. Transduces signals from Crk to activate RAS. Also involved in
CC MAPK activation. {ECO:0000269|PubMed:9878058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=O77086-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O77086-2; Sequence=VSP_001823;
CC Name=C;
CC IsoId=O77086-3; Sequence=VSP_035657, VSP_035658, VSP_001823;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878058}.
CC -!- DEVELOPMENTAL STAGE: Throughout development.
CC {ECO:0000269|PubMed:9878058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35280.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM29360.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ22488.1; Type=Frameshift; Evidence={ECO:0000305};
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; AF053358; AAC35280.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAF46200.2; -; Genomic_DNA.
DR EMBL; AE014298; AAO41635.1; -; Genomic_DNA.
DR EMBL; BT010019; AAQ22488.1; ALT_FRAME; mRNA.
DR EMBL; BT025818; ABF85718.1; -; mRNA.
DR EMBL; AY113355; AAM29360.1; ALT_FRAME; mRNA.
DR PIR; T13052; T13052.
DR RefSeq; NP_572350.2; NM_132122.5. [O77086-1]
DR RefSeq; NP_788867.1; NM_176694.3. [O77086-2]
DR AlphaFoldDB; O77086; -.
DR SMR; O77086; -.
DR BioGRID; 58103; 10.
DR IntAct; O77086; 5.
DR STRING; 7227.FBpp0289753; -.
DR iPTMnet; O77086; -.
DR PaxDb; O77086; -.
DR PRIDE; O77086; -.
DR DNASU; 31618; -.
DR EnsemblMetazoa; FBtr0299791; FBpp0289069; FBgn0259228. [O77086-2]
DR EnsemblMetazoa; FBtr0300526; FBpp0289753; FBgn0259228. [O77086-1]
DR GeneID; 31618; -.
DR KEGG; dme:Dmel_CG42328; -.
DR UCSC; CG42328-RB; d. melanogaster.
DR CTD; 31618; -.
DR FlyBase; FBgn0259228; C3G.
DR VEuPathDB; VectorBase:FBgn0259228; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000156235; -.
DR InParanoid; O77086; -.
DR OMA; IMAYMEI; -.
DR PhylomeDB; O77086; -.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR SignaLink; O77086; -.
DR BioGRID-ORCS; 31618; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31618; -.
DR PRO; PR:O77086; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0259228; Expressed in eye disc (Drosophila) and 31 other tissues.
DR ExpressionAtlas; O77086; baseline and differential.
DR Genevisible; O77086; DM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:FlyBase.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW SH3-binding.
FT CHAIN 1..1571
FT /note="Guanine nucleotide-releasing factor 2"
FT /id="PRO_0000068860"
FT DOMAIN 1170..1292
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 1339..1564
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 28..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 546..556
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 820..831
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 924..935
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 986..997
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 54..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 524
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2..67
FT /note="PQFDESFLSDCALADRWHFYSYTVKQLPPHPSPKPNRNRNPYPSGASHDDHQ
FT HQLHHHHHQQHHHN -> RVLNTELRLRFKNRKPRPFNRAASADDAMDLGSGVGVGTGI
FT ANGAGIGVGATIMPLDQLNGATSMN (in isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035657"
FT VAR_SEQ 68..171
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035658"
FT VAR_SEQ 668..718
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:9878058, ECO:0000303|Ref.4"
FT /id="VSP_001823"
FT CONFLICT 19
FT /note="H -> Y (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> S (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="E -> V (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> T (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="A -> AGA (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> A (in Ref. 4; AAQ22488)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..453
FT /note="RYSG -> HYRR (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="V -> I (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="L -> Q (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="T -> TT (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="V -> A (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="S -> N (in Ref. 1; AAC35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="M -> L (in Ref. 1; AAC35280 and 5; AAM29360)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="A -> P (in Ref. 1; AAC35280 and 5; AAM29360)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="V -> E (in Ref. 4; AAQ22488)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="S -> G (in Ref. 1; AAC35280 and 5; AAM29360)"
FT /evidence="ECO:0000305"
FT CONFLICT 1379
FT /note="N -> S (in Ref. 4; AAQ22488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1571 AA; 172071 MW; 4D4EEEB3E58F9207 CRC64;
MPQFDESFLS DCALADRWHF YSYTVKQLPP HPSPKPNRNR NPYPSGASHD DHQHQLHHHH
HQQHHHNHHR LWKTQRQSWS PRDTNNNHSL TSNNCNCNSS NTCNSISATG NTLHSIKFHR
RRKYKKLARL ALSTPAIPLQ MDVDVDVNVT VDREFDMEMD TPVPLKNAVC HGSISSPSTP
GTCSSGIGVG GGGCSSSSNN SINSGSYSTA CTPPPPTHQH HSQHQQLQGT PGGSSRVGGA
GAGGGGGVPP APPSAGSSGH KNSLKGTKLA RRARSFKDDL IEKISLMRTT NNTLGRSHSP
HSPRTKHGTK APPTTEEVLR STQTLETHVK DISNALKHFR DVILKKKLEV LPGNGTVILE
TIASMYSVIQ TYTLNENSAI MSSATLQVYQ SLGKLIKLCD EVMLSEDSGE CASLSNENVR
EVIDLLEDAV RNLVTLAQGK LKEQDQCAFR YSGSGLGGIG AAAEIMGAVT ASPGASVPGT
GVMRVSAAES AAQRTSLPDI ALTPKERDIL EQHNVNPMRG SHSTESILRD TSPPPKPPLP
NRASNPPPLP PKRRSQPSAS AGTVGVGCSS STSTSNQASP LPYAQSHNIS LNSDLDCSSN
ISLLNYGVDR LSVRSRSPDE NSQCSFDSAL NHSREEEDQQ QQHQHLRSFP KLAAMMDEDM
DKMVSYSAAI DDKTQTPLST GGGIAGVAGG TGGAGEGVAA AASGDGETNS NRHSNESGFV
SMREFRTSTQ TTDYSVQSST KSSSSNSEIA FSISESTAVG SSSEYQQISQ LVSHSQRHIS
SSSSSCTTTT TSSSTTTGYG SSEVEQLQQQ QQQQTTTTPA DLAPALPPKS IQRSSLTRHD
SPGVGDELDE VQSSSGWASH RSSQSEVAEL RQLSPLHHLN HHPHTASAGQ LQQWHSKHHS
LIEGPRLQLA GSGSCSAFDQ RHLDQEPPPL PIKKKHILAY MEICSASTRS IEQHRHTMHA
CNISRNISHS QTMNIMPMSK ELSPELEMPP ALPPKNYKQR KATSMVASPT LQPVIVTTPP
PSPKPTLGEN GSTGRPDSRM ATVCEELNDA VASEDAMPEP RSPVLDSNEN VSAVDDGQTF
YCHSHQLPAA EMEMSEDASS ADNQPITTPQ VLEEQEEPTA ESRPLVAVHE SVKPANVDED
EEAERADMLI NMLEEVNITR YLILKKREED GPEVKGGYID ALIVHASRVQ KVADNAFCEA
FITTFRTFIQ PIDVIEKLTH RYTYFFCQVQ DNKQKAAKET FALLVRVVND LTSTDLTSQL
LSLLVEFVYQ LVCSGQLYLA KLLRNKFVEK VTLYKEPKVY GFVGELGGAG SVGGAGIAGS
GGCSGTAGGG NQPSLLDLKS LEIAEQMTLL DAELFTKIEI PEVLLFAKDQ CEEKSPNLNK
FTEHFNKMSY WARSKILRLQ DAKEREKHVN KFIKIMKHLR KMNNYNSYLA LLSALDSGPI
RRLEWQKGIT EEVRSFCALI DSSSSFRAYR QALAETNPPC IPYIGLILQD LTFVHVGNQD
YLSKGVINFS KRWQQYNIID NMKRFKKCAY PFRRNERIIR FFDNFKDFMG EEEMWQISEK
IKPRGRRPVN Y
