ID FOSLA_DROME Reviewed; 755 AA.
AC P21525; A8MPI0; Q400M6; Q400M7; Q53YJ8; Q8T9E2; Q9BH37; Q9NBW7; Q9VAH5;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 27-MAR-2024, entry version 199.
DE RecName: Full=Transcription factor kayak, isoforms A/B/F;
DE AltName: Full=AP-1;
DE AltName: Full=Fos-related antigen;
DE Short=Dfos;
DE Short=dFra;
GN Name=kay; Synonyms=Fra; ORFNames=CG15509;
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 A), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP INTERACTION WITH JRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2116361; DOI=10.1101/gad.4.5.822;
RA Perkins K.K., Admon A., Patel N., Tjian R.;
RT "The Drosophila Fos-related AP-1 protein is a developmentally regulated
RT transcription factor.";
RL Genes Dev. 4:822-834(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Embryo;
RA Nairz K., Hafen E.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=11470538; DOI=10.1016/s0378-1119(01)00514-5;
RA Rousseau E., Goldstein E.S.;
RT "The gene structure of the Drosophila melanogaster homolog of the human
RT proto-oncogene fos.";
RL Gene 272:315-322(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), ALTERNATIVE PROMOTER USAGE,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18571877; DOI=10.1016/j.gene.2008.05.001;
RA Hudson S.G., Goldstein E.S.;
RT "The gene structure of the Drosophila melanogaster proto-oncogene, kayak,
RT and its nested gene, fos-intronic gene.";
RL Gene 420:76-81(2008).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP 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: Developmentally regulated transcription factor AP-1 binds and
CC recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role
CC in the function or determination of a particular subset of cells in the
CC developing embryo. It is able to carry out its function either
CC independently of or in conjunction with Jra.
CC {ECO:0000269|PubMed:2116361}.
CC -!- SUBUNIT: Homodimer. Heterodimer with Jra. The kay-Jra heterodimer binds
CC more stably to the AP-1 site than either of the two proteins alone.
CC -!- INTERACTION:
CC P21525; P18289: Jra; NbExp=3; IntAct=EBI-195448, EBI-159948;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:2116361}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=F;
CC IsoId=P21525-5; Sequence=Displayed;
CC Name=A; Synonyms=beta;
CC IsoId=P21525-2; Sequence=VSP_017891;
CC Name=B; Synonyms=gamma;
CC IsoId=P21525-3; Sequence=VSP_017892;
CC Name=D; Synonyms=alpha;
CC IsoId=A8MPH9-1; Sequence=External;
CC Name=sro; Synonyms=shroud;
CC IsoId=A8MPH9-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Early expression in the embryo is mesodermal and
CC some of this expression is localized to a region surrounding the
CC cephalic furrow. Later in embryonic development expression is
CC ectodermal, corresponding to muscle attachment sites. Also observed in
CC part of the mid- and hindgut and in the anal pad.
CC {ECO:0000269|PubMed:2116361}.
CC -!- DEVELOPMENTAL STAGE: Isoform A and isoform B are expressed both
CC maternally and zygotically. Zygotically expressed throughout
CC embryogenesis, until second larval instar. Isoform A is more highly
CC expressed than isoform B. {ECO:0000269|PubMed:18571877,
CC ECO:0000269|PubMed:2116361}.
CC -!- DISRUPTION PHENOTYPE: Loss of isoform A causes embryonic lethality.
CC {ECO:0000269|PubMed:18571877}.
CC -!- MISCELLANEOUS: Mammals typically have four copies of fos, Drosophila
CC has a single gene with multiple transcription start sites giving rise
CC to multiple protein isoforms.
CC -!- MISCELLANEOUS: [Isoform A]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {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; X54143; CAA38082.1; -; mRNA.
DR EMBL; AF238310; AAF69496.1; -; mRNA.
DR EMBL; AY574373; AAS87366.1; -; mRNA.
DR EMBL; AH010388; AAK11268.2; -; mRNA.
DR EMBL; AF332660; AAK11267.2; -; mRNA.
DR EMBL; DQ858476; ABI74758.1; -; mRNA.
DR EMBL; AE014297; AAZ83992.1; -; Genomic_DNA.
DR EMBL; AE014297; AAZ83993.1; -; Genomic_DNA.
DR EMBL; AE014297; AAZ83994.2; -; Genomic_DNA.
DR EMBL; AY069805; AAL39950.1; -; mRNA.
DR PIR; A35847; A35847.
DR RefSeq; NP_001027577.2; NM_001032405.4. [P21525-5]
DR RefSeq; NP_001027578.1; NM_001032406.2. [P21525-3]
DR RefSeq; NP_001027579.1; NM_001032407.3. [P21525-2]
DR AlphaFoldDB; P21525; -.
DR SMR; P21525; -.
DR BioGRID; 533679; 67.
DR DIP; DIP-22245N; -.
DR IntAct; P21525; 2.
DR STRING; 7227.FBpp0288515; -.
DR iPTMnet; P21525; -.
DR PaxDb; 7227-FBpp0288515; -.
DR DNASU; 3772082; -.
DR EnsemblMetazoa; FBtr0099989; FBpp0084844; FBgn0001297. [P21525-2]
DR EnsemblMetazoa; FBtr0099990; FBpp0084846; FBgn0001297. [P21525-3]
DR EnsemblMetazoa; FBtr0290076; FBpp0288515; FBgn0001297. [P21525-5]
DR GeneID; 3772082; -.
DR KEGG; dme:Dmel_CG33956; -.
DR AGR; FB:FBgn0001297; -.
DR CTD; 3772082; -.
DR FlyBase; FBgn0001297; kay.
DR VEuPathDB; VectorBase:FBgn0001297; -.
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; P21525; -.
DR OMA; HMSTLMT; -.
DR OrthoDB; 5399209at2759; -.
DR PhylomeDB; P21525; -.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-209409; Formation of the nuclear AP-1 transcription factor 'scaffolding complex'.
DR Reactome; R-DME-209425; Transcriptional activtion by AP-1 transcription factor.
DR SignaLink; P21525; -.
DR BioGRID-ORCS; 3772082; 2 hits in 3 CRISPR screens.
DR ChiTaRS; kay; fly.
DR GenomeRNAi; 3772082; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001297; Expressed in wing disc and 50 other cell types or tissues.
DR ExpressionAtlas; P21525; baseline and differential.
DR Genevisible; P21525; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0048674; P:collateral sprouting of injured axon; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:BHF-UCL.
DR GO; GO:0007297; P:follicle cell of egg chamber migration; IMP:FlyBase.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; HMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR CDD; cd14721; bZIP_Fos; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR23351:SF24; TRANSCRIPTION FACTOR KAYAK, ISOFORMS A_B_F; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative promoter usage; Alternative splicing;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..755
FT /note="Transcription factor kayak, isoforms A/B/F"
FT /id="PRO_0000076478"
FT DOMAIN 418..481
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 23..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 446..453
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 510..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..234
FT /note="MKNLNGRTHNACYHPYYHQSLHFAQQQQQQQQHHLQQQQQHMQQQQQQQQAP
FT QQQLRHQQRQLPTQPAYQQSQSVAHNAFPLRSSSNNYGHVASSAYAASSGSHNSNNAAA
FT MAAVCQMQNFFNQQQQQQQQLEFNNNCMPINYYQQQQQQHYPSESQSSASGWNPETPGQ
FT AQLALTATTCNTTAAATCNTTAAATTSTTATSAAAGSDNNHSDNFAMDASEIATFLANE
FT LFLQQ -> MKVKVERTTKKPAIRKPEDPDPAEEDRVKMVQDDPEDQENQAVDEEELDF
FT LPADLSAAISTATTKIATPTRNLI (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11470538,
FT ECO:0000303|PubMed:2116361, ECO:0000303|Ref.2"
FT /id="VSP_017891"
FT VAR_SEQ 1..234
FT /note="MKNLNGRTHNACYHPYYHQSLHFAQQQQQQQQHHLQQQQQHMQQQQQQQQAP
FT QQQLRHQQRQLPTQPAYQQSQSVAHNAFPLRSSSNNYGHVASSAYAASSGSHNSNNAAA
FT MAAVCQMQNFFNQQQQQQQQLEFNNNCMPINYYQQQQQQHYPSESQSSASGWNPETPGQ
FT AQLALTATTCNTTAAATCNTTAAATTSTTATSAAAGSDNNHSDNFAMDASEIATFLANE
FT LFLQQ -> MTLDSYNIFNDEYLFNMPLSPLPKV (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:18571877"
FT /id="VSP_017892"
FT CONFLICT 613
FT /note="A -> P (in Ref. 1; CAA38082)"
FT /evidence="ECO:0000305"
FT CONFLICT P21525-2:19
FT /note="D -> N (in Ref. 3; AAK11267/AAK11268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 80579 MW; 6E21F0460B626DAA CRC64;
MKNLNGRTHN ACYHPYYHQS LHFAQQQQQQ QQHHLQQQQQ HMQQQQQQQQ APQQQLRHQQ
RQLPTQPAYQ QSQSVAHNAF PLRSSSNNYG HVASSAYAAS SGSHNSNNAA AMAAVCQMQN
FFNQQQQQQQ QLEFNNNCMP INYYQQQQQQ HYPSESQSSA SGWNPETPGQ AQLALTATTC
NTTAAATCNT TAAATTSTTA TSAAAGSDNN HSDNFAMDAS EIATFLANEL FLQQLGNFET
GQSVLTLTTP TLTPTTTRNI EDTLGHLLSD TQTDRVAGCA GFAVPKVLPN AIDVLGMGIP
TGVSSLPLQQ TFDLSLGQGS ESEDSNASYN DTQMNEEQDT TDTSSAHTDS TSYQAGHIMA
GSVNGGGVNN FSNVLAAVSS SRGSASVGSS NANTSNTPAR RGGGRRPNRS TNMTPEEEQK
RAVRRERNKQ AAARCRKRRV DQTNELTEEV EQLEKRGESM RKEIEVLTNS KNQLEYLLAT
HRATCQKIRS DMLSVVTCNG LIAPAGLLSA GSSGSGASSH HNHNSNDSSN GTITGMDATL
NSTGRSNSPL DLKPAANIDS LLMHIKDEPL DGAIDSGSSL DQDGPPPSKR ITLPPMSTMP
HVHLSTILTP TGASSGSLQT PITSTAPGGF GSAFPVTSNG SSINNINSIG NNMNSPTLNA
HNKVPKERPN TLAFQRPLGQ MHLTMANNKA GGPTQIQGVP IQTPSTGTFN FDSLMDGGTG
LTPVSGPLVP NSSSTNKHPL ELPTPTAEPS KLVSL
//
