ID   SRC42_DROME             Reviewed;         517 AA.
AC   Q9V9J3; O18369; Q0E9P0; Q26297; Q94879;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Tyrosine-protein kinase Src42A;
DE            EC=2.7.10.2;
DE   AltName: Full=Tyrosine-protein kinase Src41;
DE            Short=Dsrc41;
GN   Name=Src42A {ECO:0000312|FlyBase:FBgn0264959};
GN   Synonyms=Src41, TK5 {ECO:0000312|FlyBase:FBgn0264959};
GN   ORFNames=CG44128 {ECO:0000312|FlyBase:FBgn0264959};
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;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Canton-S; TISSUE=Pupae;
RX   PubMed=8682295; DOI=10.1101/gad.10.13.1645;
RA   Takahashi F., Endo S., Kojima T., Saigo K.;
RT   "Regulation of cell-cell contacts in developing Drosophila eyes by Dsrc41,
RT   a new, close relative of vertebrate c-src.";
RL   Genes Dev. 10:1645-1656(1996).
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.
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-428.
RX   PubMed=1915852; DOI=10.1016/0014-5793(91)81078-m;
RA   Shishido E., Emori Y., Saigo K.;
RT   "Identification of seven novel protein-tyrosine kinase genes of Drosophila
RT   by the polymerase chain reaction.";
RL   FEBS Lett. 289:235-238(1991).
RN   [6] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-427.
RC   TISSUE=Embryo;
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   [7]
RP   FUNCTION.
RX   PubMed=12014990; DOI=10.1042/bj20020298;
RA   Muda M., Worby C.A., Simonson-Leff N., Clemens J.C., Dixon J.E.;
RT   "Use of double-stranded RNA-mediated interference to determine the
RT   substrates of protein tyrosine kinases and phosphatases.";
RL   Biochem. J. 366:73-77(2002).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF GLY-2.
RX   PubMed=16831834; DOI=10.1242/dev.02467;
RA   Murray M.J., Davidson C.M., Hayward N.M., Brand A.H.;
RT   "The Fes/Fer non-receptor tyrosine kinase cooperates with Src42A to
RT   regulate dorsal closure in Drosophila.";
RL   Development 133:3063-3073(2006).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18432193; DOI=10.1038/nature06901;
RA   Ziegenfuss J.S., Biswas R., Avery M.A., Hong K., Sheehan A.E., Yeung Y.G.,
RA   Stanley E.R., Freeman M.R.;
RT   "Draper-dependent glial phagocytic activity is mediated by Src and Syk
RT   family kinase signalling.";
RL   Nature 453:935-939(2008).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26028435; DOI=10.1016/j.cub.2015.04.037;
RA   Evans I.R., Rodrigues F.S., Armitage E.L., Wood W.;
RT   "Draper/CED-1 mediates an ancient damage response to control inflammatory
RT   blood cell migration in vivo.";
RL   Curr. Biol. 25:1606-1612(2015).
CC   -!- FUNCTION: Required directly or indirectly for the phosphorylation of
CC       drpr which is necessary for the interaction of drpr with shark and
CC       subsequent glial phagocytic activity (PubMed:18432193). Together with
CC       drpr and shark, promotes the migration of macrophages to sites of
CC       wounding as part of a signaling cascade where Src42A detects production
CC       of hydrogen peroxide at wound sites which triggers phosphorylation of
CC       drpr and subsequent recruitment and activation of shark
CC       (PubMed:26028435). Essential for correct eye morphogenesis (ommatidial
CC       R7 neuron formation) which requires the Ras1/MAPK signal transduction
CC       pathway (PubMed:8682295). May be involved in the regulation of
CC       cytoskeleton organization and cell-cell contacts in developing
CC       ommatidia (PubMed:8682295). Involved in phosphorylation of Dscam1, a
CC       cell surface receptor involved in targeting of growing axons during eye
CC       morphogenesis, and its interaction partner the SH2/SH3 adapter protein
CC       dock/dreadlocks (PubMed:12014990). During embryogenesis, involved in
CC       regulation of dorsal closure where it may have a role in activating the
CC       JNK pathway in leading edge cells during this process
CC       (PubMed:16831834). {ECO:0000269|PubMed:12014990,
CC       ECO:0000269|PubMed:16831834, ECO:0000269|PubMed:18432193,
CC       ECO:0000269|PubMed:26028435, ECO:0000269|PubMed:8682295}.
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=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- TISSUE SPECIFICITY: Ubiquitous in early embryos, in stages 13-16
CC       expression is seen in visceral mesoderm, hindgut, brain, anal pads and
CC       ventral ganglions. In larvae, expression is in CNS, wing disk, leg disk
CC       and photoreceptor precursors in the eye-antenna disks posterior to the
CC       morphogenetic furrow. {ECO:0000269|PubMed:8682295}.
CC   -!- DEVELOPMENTAL STAGE: In early embryos expression is very low,
CC       expression increases during embryogenesis. Also expressed in larvae and
CC       pupae. {ECO:0000269|PubMed:8682295}.
CC   -!- DISRUPTION PHENOTYPE: Following epithelial wounding, no migration of
CC       macrophages to wound sites (PubMed:26028435). RNAi-mediated knockdown
CC       in glial cells potently suppresses glial phagocytic activity with drpr
CC       not recruited to severed maxillary palp axons, blockage of glial
CC       hypertrophy, blockage of drpr up-regulation after antennal ablation and
CC       reduced clearance of severed axons in the central nervous system
CC       (PubMed:18432193). {ECO:0000269|PubMed:18432193,
CC       ECO:0000269|PubMed:26028435}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; D42125; BAA07705.1; -; mRNA.
DR   EMBL; AE013599; AAF57295.1; -; Genomic_DNA.
DR   EMBL; AY058652; AAL13881.1; -; mRNA.
DR   EMBL; S55977; AAB19907.1; -; Genomic_DNA.
DR   EMBL; AJ002911; CAA05746.1; -; Genomic_DNA.
DR   RefSeq; NP_476849.1; NM_057501.4.
DR   AlphaFoldDB; Q9V9J3; -.
DR   SMR; Q9V9J3; -.
DR   BioGRID; 61430; 55.
DR   DIP; DIP-22220N; -.
DR   IntAct; Q9V9J3; 3.
DR   MINT; Q9V9J3; -.
DR   STRING; 7227.FBpp0307255; -.
DR   SwissPalm; Q9V9J3; -.
DR   PaxDb; 7227-FBpp0085320; -.
DR   DNASU; 35524; -.
DR   EnsemblMetazoa; FBtr0335275; FBpp0307254; FBgn0264959.
DR   GeneID; 35524; -.
DR   KEGG; dme:Dmel_CG44128; -.
DR   AGR; FB:FBgn0264959; -.
DR   CTD; 35524; -.
DR   FlyBase; FBgn0264959; Src42A.
DR   VEuPathDB; VectorBase:FBgn0264959; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000167963; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; Q9V9J3; -.
DR   OMA; STRDQWE; -.
DR   PhylomeDB; Q9V9J3; -.
DR   BRENDA; 2.7.10.2; 1994.
DR   Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR   SignaLink; Q9V9J3; -.
DR   BioGRID-ORCS; 35524; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Src42A; fly.
DR   GenomeRNAi; 35524; -.
DR   PRO; PR:Q9V9J3; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0264959; Expressed in embryonic/larval hemocyte (Drosophila) and 35 other cell types or tissues.
DR   ExpressionAtlas; Q9V9J3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR   GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR   GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:FlyBase.
DR   GO; GO:0071588; P:hydrogen peroxide mediated signaling pathway; IMP:FlyBase.
DR   GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:FlyBase.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
DR   GO; GO:0106016; P:positive regulation of inflammatory response to wounding; IGI:FlyBase.
DR   GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IDA:FlyBase.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IGI:FlyBase.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd05068; PTKc_Frk_like; 1.
DR   CDD; cd10370; SH2_Src_Src42; 1.
DR   CDD; cd11845; SH3_Src_like; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF373; TYROSINE-PROTEIN KINASE SRC42A; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q9V9J3; DM.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW   Reference proteome; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..517
FT                   /note="Tyrosine-protein kinase Src42A"
FT                   /id="PRO_0000088139"
FT   DOMAIN          63..124
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192,
FT                   ECO:0000305"
FT   DOMAIN          130..222
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191,
FT                   ECO:0000305"
FT   DOMAIN          248..504
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        370
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         254..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         2
FT                   /note="G->D: In Src42A-myri; 63% of mutants die during
FT                   embryogenesis. In embryos, leading edge cell morphology is
FT                   irregular, the actomyosin cable is disrupted and dorsal
FT                   closure is delayed. Stage 16 embryos, which have undergone
FT                   dorsal closure, have an irregular arrangement of epidermal
FT                   cells."
FT                   /evidence="ECO:0000269|PubMed:16831834"
FT   CONFLICT        65
FT                   /note="A -> V (in Ref. 1; BAA07705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        376
FT                   /note="V -> I (in Ref. 5; AAB19907 and 6; CAA05746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381..386
FT                   /note="GNIVKI -> SNVVKM (in Ref. 5; AAB19907)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   517 AA;  59069 MW;  1EF196E4D7AE61E9 CRC64;
     MGNCLTTQKG EPDKPADRIK LDDPPTIGVG VGVPQIPMPS HAGQPPEQIR PVPQIPESET
     AGANAKIFVA LYDYDARTDE DLSFRKGEHL EILNDTQGDW WLARSKKTRS EGYIPSNYVA
     KLKSIEAEPW YFRKIKRIEA EKKLLLPENE HGAFLIRDSE SRHNDYSLSV RDGDTVKHYR
     IRQLDEGGFF IARRTTFRTL QELVEHYSKD SDGLCVNLCK PCVQIEKPVT EGLSHRTRDQ
     WEIDRTSLKF VRKLGSGQFG DVWEGLWNNT TPVAIKTLKS GTMDPKDFLA EAQIMKKLRH
     TKLIQLYAVC TVEEPIYIIT ELMKHGSLLE YLQAIAGKGR SLKMQTLIDM AAQIAAGMAY
     LESQNYIHRD LAARNVLVGD GNIVKIADFG LARLIKEDEY EARVGARFPI KWTAPEAANY
     SKFSIKSDVW SFGILLTELV TYGRIPYPGM TNAEVLTQVE HGYRMPQPPN CEPRLYEIML
     ECWHKDPMRR PTFETLQWKL EDFYTSDQSD YKEAQAY
//