HEP_DROME
ID HEP_DROME Reviewed; 1178 AA.
AC Q23977; O18411; Q8SZ04; Q8SZZ1; Q9I7S3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase hemipterous;
DE Short=MAPKK;
DE EC=2.7.12.2;
GN Name=hep; Synonyms=hem, MKK7; ORFNames=CG4353;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=8521475; DOI=10.1016/0092-8674(95)90123-x;
RA Glise B., Bourbon H., Noselli S.;
RT "Hemipterous encodes a novel Drosophila MAP kinase kinase, required for
RT epithelial cell sheet movement.";
RL Cell 83:451-461(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND FUNCTION.
RX PubMed=9207092; DOI=10.1073/pnas.94.14.7337;
RA Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
RT "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun
RT NH2-terminal kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997).
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., 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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [6]
RP FUNCTION.
RX PubMed=8946915; DOI=10.1101/gad.10.21.2745;
RA Sluss H.K., Han Z., Barrett T., Davis R.J., Ip Y.T.;
RT "A JNK signal transduction pathway that mediates morphogenesis and an
RT immune response in Drosophila.";
RL Genes Dev. 10:2745-2758(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-662; SER-1150 AND
RP SER-1154, 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: Required for the epithelial cell sheet movement called dorsal
CC closure (DC), which allows establishment of the dorsal epidermis.
CC Controls the expression in the dorsal epithelium edges of another
CC dorsal closure gene, puckered (puc). Phosphorylates and activates the
CC MAP kinase bsk; bsk signal transduction pathway mediates an immune
CC response and morphogenesis. {ECO:0000269|PubMed:8521475,
CC ECO:0000269|PubMed:8946915, ECO:0000269|PubMed:9207092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2;
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=2.7.12.2;
CC -!- INTERACTION:
CC Q23977; Q9W0K0: Aplip1; NbExp=2; IntAct=EBI-74214, EBI-74120;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q23977-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q23977-3; Sequence=VSP_015107, VSP_015108;
CC -!- PTM: MAPKK is itself dependent on Ser/Thr phosphorylation for activity
CC catalyzed by MAP kinase kinase kinases. {ECO:0000250}.
CC -!- PTM: Weakly autophosphorylated. {ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48832.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL48832.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; U05240; AAC46944.1; -; mRNA.
DR EMBL; U93032; AAB63449.1; -; mRNA.
DR EMBL; AE014298; AAF48222.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09646.1; -; Genomic_DNA.
DR EMBL; AY069695; AAL39840.1; -; mRNA.
DR EMBL; AY071210; AAL48832.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001259501.1; NM_001272572.2. [Q23977-3]
DR RefSeq; NP_511142.2; NM_078587.3. [Q23977-3]
DR RefSeq; NP_727661.1; NM_167346.2. [Q23977-1]
DR AlphaFoldDB; Q23977; -.
DR SMR; Q23977; -.
DR BioGRID; 58642; 75.
DR DIP; DIP-30870N; -.
DR IntAct; Q23977; 3.
DR STRING; 7227.FBpp0073578; -.
DR iPTMnet; Q23977; -.
DR PaxDb; Q23977; -.
DR PRIDE; Q23977; -.
DR DNASU; 32256; -.
DR EnsemblMetazoa; FBtr0073747; FBpp0073578; FBgn0010303. [Q23977-1]
DR EnsemblMetazoa; FBtr0073748; FBpp0073579; FBgn0010303. [Q23977-3]
DR EnsemblMetazoa; FBtr0330397; FBpp0303423; FBgn0010303. [Q23977-3]
DR GeneID; 32256; -.
DR KEGG; dme:Dmel_CG4353; -.
DR CTD; 32256; -.
DR FlyBase; FBgn0010303; hep.
DR VEuPathDB; VectorBase:FBgn0010303; -.
DR eggNOG; KOG0983; Eukaryota.
DR InParanoid; Q23977; -.
DR OMA; CMELMET; -.
DR PhylomeDB; Q23977; -.
DR BRENDA; 2.7.12.2; 1994.
DR Reactome; R-DME-209397; Formation of the cytosolic BSK 'scaffolding complex'.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex.
DR SignaLink; Q23977; -.
DR BioGRID-ORCS; 32256; 0 hits in 3 CRISPR screens.
DR ChiTaRS; hep; fly.
DR GenomeRNAi; 32256; -.
DR PRO; PR:Q23977; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010303; Expressed in brain and 25 other tissues.
DR ExpressionAtlas; Q23977; baseline and differential.
DR Genevisible; Q23977; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008545; F:JUN kinase kinase activity; IDA:FlyBase.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:Reactome.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IDA:FlyBase.
DR GO; GO:0034769; P:basement membrane disassembly; IMP:FlyBase.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:FlyBase.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IMP:FlyBase.
DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:FlyBase.
DR GO; GO:0046844; P:chorion micropyle formation; IMP:FlyBase.
DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:FlyBase.
DR GO; GO:0007561; P:imaginal disc eversion; IMP:FlyBase.
DR GO; GO:0046528; P:imaginal disc fusion; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:UniProtKB.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0007254; P:JNK cascade; IDA:FlyBase.
DR GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
DR GO; GO:0048666; P:neuron development; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1178
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase hemipterous"
FT /id="PRO_0000085992"
FT DOMAIN 197..456
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 74..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 203..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 489..492
FT /note="ATAT -> LPNS (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8521475,
FT ECO:0000303|PubMed:9207092"
FT /id="VSP_015107"
FT VAR_SEQ 493..1178
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8521475,
FT ECO:0000303|PubMed:9207092"
FT /id="VSP_015108"
FT CONFLICT 71
FT /note="G -> S (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..97
FT /note="PFGSA -> LRSP (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> R (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> R (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..121
FT /note="TFGG -> LRW (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..150
FT /note="GLNR -> DVEC (in Ref. 1; AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..489
FT /note="RLRANGDPTLQRA -> DCGQWRSNAPEVT (in Ref. 1;
FT AAC46944)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="D -> G (in Ref. 5; AAL48832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1178 AA; 125108 MW; 79A2987068EC1870 CRC64;
MSTIEFETIG SRLQSLEAKL QAQNESHDQI VLSGARGPVV SGSVPSARVP PLATSASAAT
SATHAPSLGA GSVSGSGISI AQRPAPPVPH ATPFGSASAS SSSSSASAFA SAAPATGTFG
GTYTPPTTRV SRATPTLPML SSGPGGGLNR TRPVILPLPT PPHPPVSETD MKLKIIMEQT
GKLNINGRQY PTDINDLKHL GDLGNGTSGN VVKMMHLSSN TIIAVKQMRR TGNAEENKRI
LMDLDVVLKS HDCKYIVKCL GCFVRDPDVW ICMELMSMCF DKLLKLSKKP VPEQILGKVT
VATVNALSYL KDKHGVIHRD VKPSNILIDE RGNIKLCDFG ISGRLVDSKA NTRSAGCAAY
MAPERIDPKK PKYDIRADVW SLGITLVELA TARSPYEGCN TDFEVLTKVL DSEPPCLPYG
EGYNFSQQFR DFVIKCLTKN HQDRPKYPEL LAQPFIRIYE SAKVDVPNWF QSIKDNRLRA
NGDPTLQRAT ATGSAIGSGA GSLAGSGSGS AGGAVKYGRA TTYAGQSPTN PQKTIKPTQI
PSYQQQQSQF FMQSATQLPQ TTTTTPTATT NCFGGSGNGN GRGNGSGGSG NGSGSSSSAS
PLSPPSAGIG DLNRLYRKSP FMQRKLSNGS HHPHYKYNDE SPKKESMFSS IGQSILRNLT
TSPFSQKKHN STATTIPLPH NNQTLITDAA TAAAAAATAT TPPNIAATVL TTTPTTTPTW
RLPTENSQAY DSCDSSSNAT TTTLNLGLSS PSPSLPRKQF PTESPTLQLT SQQQQQPQRL
QPGNQSPIVL QRFYHQQNQL REKEAAERYQ QQRQQPPVGV TSTNPFHSNY VPPPPSTHST
SSQSSTQSTC SQIAINPASI SPSSGSGTGN MAGLGIGSAP ASGLGAAGHF GAGGTGEQLQ
YQPLPIAAEA TGTSPTLQSR SPEQQSDYGG NGNMVASKLS KLYARRQLLG QSSSSGASNS
SLDGCSREQH DAGWFNTLAG AMKRQFATYV KTQLNSTATS PVASSMDRDQ EPVHPQPPAY
RSVVNNGSGG KSYYYRTLSA ASSSSNTSQS TSPTTEPLPG GGTSSFLRRY ASSGPGGSIS
TPPSPHILAG LDRRHRSPDP PPRYNRGQSP LLLRKNLLEL SGQPPGSPLL HRRYVSASPP
LPPPRRGSES VPGSPQHFRT RIHYTPEPQR RIYRTIDQ
