CHIF_DROME
ID CHIF_DROME Reviewed; 1711 AA.
AC Q9NK54; Q8MRI8; Q95S82; Q9NK53; Q9U9R4; Q9U9R5; Q9VJL0; Q9VJL1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein chiffon;
GN Name=chif; ORFNames=CG5813;
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] (ISOFORMS A AND B), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=10477296; DOI=10.1242/dev.126.19.4281;
RA Landis G., Tower J.;
RT "The Drosophila chiffon gene is required for chorion gene amplification,
RT and is related to the yeast Dbf4 regulator of DNA replication and cell
RT cycle.";
RL Development 126:4281-4293(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
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] OF 1-712 AND 1506-1695 (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo, and 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-306; SER-307; SER-406;
RP SER-407; SER-417; SER-432; SER-435; SER-467; SER-542; SER-543; SER-544;
RP THR-1081; SER-1091 AND SER-1092, 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: May be involved in initiation of DNA replication; activation
CC of the chorion gene origins. May have a role in eye and thoracic
CC bristle development. {ECO:0000269|PubMed:10477296}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=1;
CC IsoId=Q9NK54-1; Sequence=Displayed;
CC Name=B; Synonyms=2;
CC IsoId=Q9NK54-2; Sequence=VSP_012407;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10477296}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF158178; AAD48779.1; -; mRNA.
DR EMBL; AF158179; AAD48780.1; -; mRNA.
DR EMBL; AE014134; AAF53530.1; -; Genomic_DNA.
DR EMBL; AE014134; AAG22437.1; -; Genomic_DNA.
DR EMBL; AY060919; AAL28467.1; ALT_INIT; mRNA.
DR EMBL; AY119597; AAM50251.1; -; mRNA.
DR RefSeq; NP_001260499.1; NM_001273570.2. [Q9NK54-2]
DR RefSeq; NP_523583.2; NM_078859.4. [Q9NK54-1]
DR RefSeq; NP_723965.1; NM_165156.3. [Q9NK54-2]
DR AlphaFoldDB; Q9NK54; -.
DR BioGRID; 60983; 5.
DR IntAct; Q9NK54; 4.
DR STRING; 7227.FBpp0080396; -.
DR iPTMnet; Q9NK54; -.
DR PaxDb; Q9NK54; -.
DR EnsemblMetazoa; FBtr0080838; FBpp0080396; FBgn0000307. [Q9NK54-1]
DR EnsemblMetazoa; FBtr0080839; FBpp0080397; FBgn0000307. [Q9NK54-2]
DR EnsemblMetazoa; FBtr0321313; FBpp0302856; FBgn0000307. [Q9NK54-2]
DR GeneID; 34974; -.
DR KEGG; dme:Dmel_CG5813; -.
DR UCSC; CG5813-RA; d. melanogaster. [Q9NK54-1]
DR CTD; 34974; -.
DR FlyBase; FBgn0000307; chif.
DR VEuPathDB; VectorBase:FBgn0000307; -.
DR eggNOG; KOG4139; Eukaryota.
DR GeneTree; ENSGT00530000063909; -.
DR HOGENOM; CLU_237730_0_0_1; -.
DR InParanoid; Q9NK54; -.
DR OMA; YEMEPCA; -.
DR PhylomeDB; Q9NK54; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR SignaLink; Q9NK54; -.
DR BioGRID-ORCS; 34974; 1 hit in 3 CRISPR screens.
DR ChiTaRS; chif; fly.
DR GenomeRNAi; 34974; -.
DR PRO; PR:Q9NK54; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000307; Expressed in cleaving embryo and 45 other tissues.
DR ExpressionAtlas; Q9NK54; baseline and differential.
DR Genevisible; Q9NK54; DM.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IDA:FlyBase.
DR GO; GO:0070775; C:H3 histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:FlyBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007304; P:chorion-containing eggshell formation; HMP:FlyBase.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IMP:FlyBase.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:FlyBase.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:FlyBase.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR Gene3D; 6.10.250.3410; -; 1.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA replication; DNA-binding;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1711
FT /note="Protein chiffon"
FT /id="PRO_0000089644"
FT ZN_FING 307..356
FT /note="DBF4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT DNA_BIND 493..505
FT /note="A.T hook"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1081
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1677..1711
FT /note="TCASSSSMRNAWRRTQRRAISAACISAAPSARVPN -> VRVTCRRLRAPFR
FT RFRYRR (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10477296,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_012407"
FT CONFLICT 709
FT /note="I -> K (in Ref. 5; AAM50251)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="E -> K (in Ref. 5; AAM50251)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="L -> F (in Ref. 1; AAD48779/AAD48780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1711 AA; 189218 MW; 4CF179D974817BDA CRC64;
MQPQSDKQSA SRLATTTSHS TAAASATAAT PPKVKVIKSK RPLCHFKFYL DICDHQLAKR
IESDIKALGG HLEFFLSDDI THFVTDKPEV IGGTSGTPGT PSTPGTPTSH YQQNDGSARK
PNQRQSRADA ILSRVRRSTV GVVNSGNSTP TTSLKRSYTI WQTDYAQRFI KRIQTELKQY
LEGKKEGGGG STSASPHHIQ LKKQYVKIES VKRNYRPYYH LIKQPDDWPK IDLSSEDGAF
RLLTKSKTKD KEHSMTRKPL GSRTSQKDKQ AAGEAKPLQH PSLQELKKQS AIPNSPRSNC
REPIDSSEKQ GGVCEICKLE YDILNIHLQS KDHELFAKNS DNFLALDTLI QSSADVNRFL
EEEPVESELD MDVDESLSNE ELQSPRQRPS PALREKSKRI TKGKHSSEKF QGVAVASPQT
PFPGAKKVQG NSPGSLSELQ RQEHPTTAAA TPTTNSGRRK TQNSGLSPPK RAMLPPSSIY
KVVETREECA TPPRGRGRPP NQVDSPSLIV KFQKIRQTEL QRLNGEAENF MFPRTAVPTT
RSSSELPTDV DRQTTSDVRG RYSISSASLD TSTSEAETKE SSGLPTSIRK RAQAVGRRRK
VGGAAAQDVF QRQLSTGSSS SNSNQQRFPS APIQPEEGPQ PQPKPQLKIK IKQEQLVATR
KSSRTATAIV TAATASSHQQ QQLRQTTCRK MANKLEDRMG ELVKPKIKIK KEVIEEQKVK
ELEDLEEILD KELDEEVDSS CSSGSDEDYI AGSQRRITAA PRKSTDTREQ RAARRLSRLT
INRSAGELEL TEVKTSPSKS RTKIQKPSSP TKNKVKQTKA VPPAIDLFFD CSKSERLREM
QYTFESLPSG ELWNRVFLRQ DAGEENYYTY YGSTNYRKLP YEMGPIPMAK TLPAHSCALC
REASEVKQDK GEQIKLEDQK PAPKKEVKKE EEVQSSSSSA TYKNKKLHLL QRYQQEQEQL
QQLEGNSLAT AGAKCDSKAS TPELLEREFA SGSMGDRVQL IERVRSTSSS SCSNSQRSGI
TCRNKQLARI AELPPRKSPR EHASTLALVS CIIRQRQDSQ SKTNSEAEEP PPPVAAPKLK
TPIKQEPVAP SSPRTTRSQA ATPVEELRFA TEISETVKRM RRGQNKYDHS PPAPVPTPAT
SSPVRSRRLT PAARNQSQIY SRRLEFATSQ RESSASALLG KRKRRVNPSV AGTVRPTTQN
LPGTGAYRGV RKLPSKKGLL EYEMETCALK ALDQARQYCN PGFVAWQLDK YLELAGKEYD
IEFDQISPEV ESEGREERLV NTPQTPPPTD CFTSEFDLCD LIMGSAGSGD DDEDVSRGNP
PGSGRRMSNL NLYASYYRKR KSLKSNRTGW PKAQRRRNAG GLGGSRALPD ERINFQKMGL
AELHPIKQEP METEEEQTTT TTTTTTTSAT RGNLLSKDDE DDEGGGNSPS GGSPADDKQN
SREDAVMTPP ATDVDEQAEP QADEMESLPD EDETMADSVD QQQDVEAEIE ATDADVEEEE
EEEDEDEDVF EDAYEEQDMG IQKTEPHEKR ARIPSISVTT PPEDSSQGKK LLLTLHNGQR
LQATSTPSTG QVQQHQRRTP QLNGSLGSCI SPSEKLGDNS DIFTVSSDGL DTDLDLSNTQ
AGDSHEHCPH QTTPKRKFDI SKYAPPNSGK AASSCAAEAA TAAVKSLAIS QFLKKETCAS
SSSMRNAWRR TQRRAISAAC ISAAPSARVP N
