CIC_DROME
ID CIC_DROME Reviewed; 1832 AA.
AC Q9U1H0; A8JR51; B5RIQ9; Q29R05; Q9VDN9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Putative transcription factor capicua;
DE AltName: Full=Protein fettucine;
GN Name=cic; Synonyms=fet; ORFNames=CG43122;
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), FUNCTION, INTERACTION WITH GRO,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Embryo;
RX PubMed=10652276;
RA Jimenez G., Guichet A., Ephrussi A., Casanova J.;
RT "Relief of gene repression by torso RTK signaling: role of capicua in
RT Drosophila terminal and dorsoventral patterning.";
RL Genes Dev. 14:224-231(2000).
RN [2]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11714680; DOI=10.1242/dev.128.22.4553;
RA Goff D.J., Nilson L.A., Morisato D.;
RT "Establishment of dorsal-ventral polarity of the Drosophila egg requires
RT capicua action in ovarian follicle cells.";
RL Development 128:4553-4562(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11861482; DOI=10.1242/dev.129.4.993;
RA Roch F., Jimenez G., Casanova J.;
RT "EGFR signalling inhibits capicua-dependent repression during specification
RT of Drosophila wing veins.";
RL Development 129:993-1002(2002).
RN [7]
RP FUNCTION.
RX PubMed=15510215; DOI=10.1038/sj.emboj.7600457;
RA Cinnamon E., Gur-Wahnon D., Helman A., St Johnston D., Jimenez G.,
RA Paroush Z.;
RT "Capicua integrates input from two maternal systems in Drosophila terminal
RT patterning.";
RL EMBO J. 23:4571-4582(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-49 AND THR-1716, AND
RP 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: Transcriptional repressor required for the specification of
CC numerous cell types during embryonic development. Required for terminal
CC patterning of early embryos. May associate with gro to repress tll and
CC hkb, restricting their expression to embryonic terminal poles where
CC they initiate correct development of head and tail structures. Required
CC for dorsoventral patterning of oocytes and early embryos. Cooperates
CC with dl to repress zen and other dorsal specific genes within the
CC embryo and promotes expression of the ventralizing factor pip in
CC ovarian follicle cells. Required during wing development for the
CC specification of intervein areas, where it mediates localized
CC repression of vein specific genes such as aos, dpp and vvl.
CC {ECO:0000269|PubMed:10652276, ECO:0000269|PubMed:11714680,
CC ECO:0000269|PubMed:11861482, ECO:0000269|PubMed:15510215}.
CC -!- SUBUNIT: Interacts with gro. {ECO:0000269|PubMed:10652276}.
CC -!- INTERACTION:
CC Q9U1H0; P40417: rl; NbExp=3; IntAct=EBI-98330, EBI-867790;
CC Q9U1H0; P28482: MAPK1; Xeno; NbExp=2; IntAct=EBI-98330, EBI-959949;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:10652276, ECO:0000269|PubMed:11714680,
CC ECO:0000269|PubMed:11861482}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9U1H0-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9U1H0-2; Sequence=VSP_036477;
CC -!- TISSUE SPECIFICITY: Expressed in the central region of embryos. Also
CC expressed in ovarian follicle cells, the wing imaginal disks and the
CC wing pouch. {ECO:0000269|PubMed:10652276, ECO:0000269|PubMed:11714680,
CC ECO:0000269|PubMed:11861482}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in stage 1-3 blastoderm
CC embryos. {ECO:0000269|PubMed:10652276}.
CC -!- INDUCTION: Subject to local inactivation by the RAS-RAF-MAPK signal
CC transduction pathway, which leads to relief of target gene repression.
CC This pathway may be locally activated by a variety of ligands and
CC receptor tyrosine kinases (RTKs) according to the developmental stage
CC and tissue. In terminal patterning, activation of tor by the locally
CC processed ligand trk may promote cic inactivation specifically at the
CC embryonic terminal poles. In the developing wing, activation of Egfr by
CC vn may lead to cic inactivation specifically in prospective vein
CC tissue. {ECO:0000269|PubMed:10652276, ECO:0000269|PubMed:11861482}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC86297.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ252268; CAB66144.1; -; mRNA.
DR EMBL; AE014297; AAF55751.3; -; Genomic_DNA.
DR EMBL; AE014297; ABW08708.1; -; Genomic_DNA.
DR EMBL; BT044183; ACH92248.1; -; mRNA.
DR EMBL; BT024235; ABC86297.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001097843.1; NM_001104373.2. [Q9U1H0-1]
DR RefSeq; NP_524992.1; NM_080253.4. [Q9U1H0-2]
DR AlphaFoldDB; Q9U1H0; -.
DR SMR; Q9U1H0; -.
DR BioGRID; 72791; 14.
DR DIP; DIP-23664N; -.
DR IntAct; Q9U1H0; 14.
DR MINT; Q9U1H0; -.
DR iPTMnet; Q9U1H0; -.
DR PaxDb; Q9U1H0; -.
DR PRIDE; Q9U1H0; -.
DR DNASU; 53560; -.
DR EnsemblMetazoa; FBtr0305026; FBpp0293563; FBgn0262582. [Q9U1H0-2]
DR EnsemblMetazoa; FBtr0305027; FBpp0293564; FBgn0262582. [Q9U1H0-1]
DR GeneID; 53560; -.
DR KEGG; dme:Dmel_CG43122; -.
DR UCSC; CG5067-RB; d. melanogaster.
DR CTD; 23152; -.
DR FlyBase; FBgn0262582; cic.
DR VEuPathDB; VectorBase:FBgn0262582; -.
DR eggNOG; KOG2746; Eukaryota.
DR GeneTree; ENSGT00940000159960; -.
DR HOGENOM; CLU_002375_0_0_1; -.
DR InParanoid; Q9U1H0; -.
DR SignaLink; Q9U1H0; -.
DR BioGRID-ORCS; 53560; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 53560; -.
DR PRO; PR:Q9U1H0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0262582; Expressed in cleaving embryo and 31 other tissues.
DR ExpressionAtlas; Q9U1H0; baseline and differential.
DR Genevisible; Q9U1H0; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0048592; P:eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; IMP:FlyBase.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IGI:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IDA:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1832
FT /note="Putative transcription factor capicua"
FT /id="PRO_0000048600"
FT DNA_BIND 490..558
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 66..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..1832
FT /note="Interaction with gro"
FT REGION 874..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..938
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 887..1315
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10652276, ECO:0000303|Ref.4"
FT /id="VSP_036477"
SQ SEQUENCE 1832 AA; 195662 MW; 1D2A2A8537BFB4D8 CRC64;
MNAFQDFELG AKLYLQCLLS LSSSRSATPS YTSPVNHAGA SPLNAIAHSP VNVSATHRQN
FFTPIANQSQ QQQQQQPVAV PLDSKWKTTP SPVLYNANNN SSNNNTSSSN NNNNSNWEVG
SNSNTHVAAT AAATSTVGAQ PLPPQTTPVS LVMHAPPPQQ QPLQQQHHHH QPPPPPPASL
PAPSAPPTSG SSSSHNSVGH ATSVIRISSS QQQHQQQQQH QQQAHPHVVV SGGQTFHPVI
VDATQLSVPL PPTTVSFHQP NTPTSTAASV ASMSQDKMLA KNGYNAPWFK LLPHMTPMSK
ASPAPVTPTL TTSASSYNVV MMQQQQQHQQ LQQQQQLQQQ QQSPPQMPLN HNNNHLIVSA
PLSSPGKPLN CSMNDAKVAA AAAAAAVANQ RQKQQQEEPD DQLDDDVFET TTPGISANSK
KQTAAMRLPT HNSNIRKLEE CHDDGAAGAP ATSAAKRRSQ SLSALQQQQQ QQQQAGAAGT
AAGQPANKKI RRPMNAFMIF SKKHRKMVHK KHPNQDNRTV SKILGEWWYA LKPEQKAQYH
ELASSVKDAH FKLHPEWKWC SKDRRKSSTS TATPGGKASG AAGTGDAKQR LVSVDGSDSL
EHDMCPSTPG GSGSCGGQGI SSDLQGDIIP LTIDNYNSTC DEAPTTISMK GNGNGKLMKN
ELPSDEDEQM LVVEEEQQQQ TVKKIDLHCR ERVNDSDMDD TPFDYRKQQP EANQRSAEEH
STSGANGQAI NAPPLSGGER EITLKPKAIK AHPVLESNML PYTQMSIYTQ YTSPKNPIGV
TPFQPTGGAF KSMPISPKGS GGKPEDAGSL QAHIKQEDIK QEPPSPYKLN NGSGSASGGG
VVSAPPPNSG SVGAIFNFNV PTATALSQKQ FHYPMHHPHR SPTDLRDEEA DREEITQGTK
SGESSEKDKP ALDDQERDEV EEEDEDEEDD DEDDEDDEQF MQELASVNAS AGFDDLVPYA
MPKVVITPTP TPPPVATIVT PIKRKQFTIV RSLTPLQPSN SPHQQLKHLH QRRGETPPTV
ITRVPTPTIN HFTIIRTQQH PHTHPHNTPP PLFFKQKVQG SPVIATVTTS TLSSSSSNPA
NNEAPNKFSN FPTQHQPTTT TTISCNTNNN ATPIIRKLLT LQEGAELGGS HKGTGRAAIL
YDALVLDTLH GQDEEEEEDE GNAEKQENPK VAGKEQVTTS QPATMLLITD VNAYNQQHVA
GNAATPVSGA ATLRPVSFIS INACNKITLP ANARILTAAT ATSTAAGAAV TSQAGATLTV
MTKASAATNH SSSNASDITI TAASAAPVPT SGSSIVMINS TTNPSTSSNS TSCSAAAHQA
CVPSSPAGMG LGHAANIATP PASAPAQIMG GGPASQKMFF AMTHPYTLLQ RSHQPGTPSL
EHLQLDAFAP GGYTLRNHNG LSSLPPPVSA QPTMLLHGYP PSHGVEPPAR SPSYKSMPST
PKSATYLMSA PPERGMDGGM SGCASAAASG GDESDIDADG QQFILAPTPA QLGRAPLQRR
KNLSQSKSES NVSFGANLGA SNGQHISRKL HSPTMMESSS PIIGHVNSSN LSSALPTPTS
STTTPNSDEQ LPLTPTTSSS NSNLNQQQPK SPMKGAPGST AAALKKKNDE MNNSVLKQVD
FEKKYKALPQ FQPEDCQSPS AIAVPSSPRV YGTNYRKKNT APPPVQKLMC EDDSIDEPAS
APPTTTQRFF GPDFNNELKE LESSDQTGRS PRTPKTPLQS ARSDASEKGH RKVLETRRSL
VLQLFAEHGN FPTAQATMAF QSKHSDVFPR KQDLQLKIRE VRQKLLGQAS CTPHSAGPNT
PSDSNSSSTT LSASSTSLNM QTTSAADVFQ YY
