APLP_DROME
ID APLP_DROME Reviewed; 3351 AA.
AC Q9V496; Q8ST55; Q8T6S6; Q94907;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Apolipophorins {ECO:0000303|PubMed:15062105};
DE AltName: Full=Retinoid- and fatty acid-binding glycoprotein {ECO:0000303|PubMed:8702812};
DE Contains:
DE RecName: Full=Apolipophorin-2;
DE AltName: Full=ApoL2;
DE AltName: Full=Apolipophorin II {ECO:0000303|PubMed:15875013};
DE Short=ApoLII {ECO:0000303|PubMed:15875013};
DE Contains:
DE RecName: Full=Apolipophorin-1;
DE AltName: Full=ApoL1;
DE AltName: Full=Apolipophorin I {ECO:0000303|PubMed:15875013};
DE Short=ApoLI {ECO:0000303|PubMed:15875013};
DE Flags: Precursor;
GN Name=apolpp {ECO:0000312|FlyBase:FBgn0087002};
GN Synonyms=Rfabg {ECO:0000303|PubMed:8702812},
GN RfaBp {ECO:0000312|FlyBase:FBgn0087002};
GN ORFNames=CG11064 {ECO:0000312|FlyBase:FBgn0087002};
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], PROTEIN SEQUENCE OF 26-75; 211-225; 534-568;
RP 606-615; 1788-1803; 2085-2095; 2105-2121; 2161-2171; 2344-2361; 2402-2423;
RP 2827-2831; 2843-2856 AND 2914-2936, FUNCTION, LIPID-BINDING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=8702812; DOI=10.1074/jbc.271.34.20641;
RA Kutty R.K., Kutty G., Kambadur R., Duncan T., Koonin E.V., Rodriguez I.R.,
RA Odenwald W.F., Wiggert B.;
RT "Molecular characterization and developmental expression of a retinoid- and
RT fatty acid-binding glycoprotein from Drosophila: a putative lipophorin.";
RL J. Biol. Chem. 271:20641-20649(1996).
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.
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 [GENOMIC DNA] OF 1373-1716, AND VARIANT TYR-1696.
RC STRAIN=253.27, 253.30, Closs10, Closs19, North7.13, Rio, South1.10, Y10,
RC ZH56, and ZW30;
RX PubMed=11778050; DOI=10.1126/science.1064521;
RA Wang W., Thornton K., Berry A., Long M.;
RT "Nucleotide variation along the Drosophila melanogaster fourth
RT chromosome.";
RL Science 295:134-137(2002).
RN [5]
RP GLYCOSYLATION.
RX PubMed=8031123; DOI=10.1006/abbi.1994.1294;
RA Duncan T., Kutty G., Chader G.J., Wiggert B.;
RT "A glycoprotein binding retinoids and fatty acids is present in
RT Drosophila.";
RL Arch. Biochem. Biophys. 312:158-166(1994).
RN [6]
RP HEME-BINDING.
RX PubMed=10393207;
RA Duncan T., Osawa Y., Kutty R.K., Kutty G., Wiggert B.;
RT "Heme-binding by Drosophila retinoid- and fatty acid-binding glycoprotein
RT (RFABG), a member of the proapolipophorin gene family.";
RL J. Lipid Res. 40:1222-1228(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15062105; DOI=10.1016/j.cub.2004.03.030;
RA Scherfer C., Karlsson C., Loseva O., Bidla G., Goto A., Havemann J.,
RA Dushay M.S., Theopold U.;
RT "Isolation and characterization of hemolymph clotting factors in Drosophila
RT melanogaster by a pullout method.";
RL Curr. Biol. 14:625-629(2004).
RN [8]
RP FUNCTION IN WG AND HH TRANSPORT.
RX PubMed=15875013; DOI=10.1038/nature03504;
RA Panakova D., Sprong H., Marois E., Thiele C., Eaton S.;
RT "Lipoprotein particles are required for Hedgehog and Wingless signalling.";
RL Nature 435:58-65(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2822, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Constitutes the major component of lipophorin, which mediates
CC transport for various types of lipids in hemolymph. Acts by forming
CC lipoprotein particles that bind lipoproteins and lipids. Also involved
CC in the transport of hydrophobic ligands like juvenile hormones,
CC pheromone hydrocarbons and carotenoids. Required for morphogens
CC wingless (wg) and hedgehog (hh) function, probably by acting as
CC vehicles for the movement of wg and hh, explaining how covalently
CC lipidated wg and hh can spread over long distances. May also be
CC involved in transport and/or metabolism of heme.
CC {ECO:0000269|PubMed:15875013, ECO:0000269|PubMed:8702812}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.
CC -!- TISSUE SPECIFICITY: During stage 12, it is highly present throughout
CC the yolk sac. By late stage 14, it localizes in the lateral fat body
CC cells. Starting at stage 14, it localizes to the apodemes. Component of
CC hemolymph clots (at protein level). Expressed in the amniosera.
CC {ECO:0000269|PubMed:8702812}.
CC -!- PTM: May be modified covalently by lipidation.
CC {ECO:0000269|PubMed:8031123}.
CC -!- PTM: Cleaved into 2 chains by furin protease. However, prevention of
CC cleavage does not impair its function (By similarity). {ECO:0000250}.
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DR EMBL; U62892; AAC47284.1; -; mRNA.
DR EMBL; AE014135; AAF59387.2; -; Genomic_DNA.
DR EMBL; AF433843; AAM17994.1; -; Genomic_DNA.
DR EMBL; AF433844; AAM17995.1; -; Genomic_DNA.
DR EMBL; AF433845; AAM17996.1; -; Genomic_DNA.
DR EMBL; AF433846; AAM17997.1; -; Genomic_DNA.
DR EMBL; AF433847; AAM17998.1; -; Genomic_DNA.
DR EMBL; AF433848; AAM17999.1; -; Genomic_DNA.
DR EMBL; AF433849; AAM18000.1; -; Genomic_DNA.
DR EMBL; AF433850; AAM18001.1; -; Genomic_DNA.
DR EMBL; AF433851; AAM18002.1; -; Genomic_DNA.
DR EMBL; AF433852; AAM18003.1; -; Genomic_DNA.
DR PIR; T13812; T13812.
DR RefSeq; NP_001259085.1; NM_001272156.1.
DR RefSeq; NP_001284720.1; NM_001297791.1.
DR RefSeq; NP_001284721.1; NM_001297792.1.
DR RefSeq; NP_524634.2; NM_079895.3.
DR SMR; Q9V496; -.
DR BioGRID; 68653; 55.
DR DIP; DIP-19190N; -.
DR IntAct; Q9V496; 9.
DR STRING; 7227.FBpp0088252; -.
DR GlyGen; Q9V496; 7 sites.
DR iPTMnet; Q9V496; -.
DR PaxDb; Q9V496; -.
DR EnsemblMetazoa; FBtr0089188; FBpp0088252; FBgn0087002.
DR EnsemblMetazoa; FBtr0334627; FBpp0306689; FBgn0087002.
DR EnsemblMetazoa; FBtr0345296; FBpp0311463; FBgn0087002.
DR EnsemblMetazoa; FBtr0345297; FBpp0311464; FBgn0087002.
DR GeneID; 43827; -.
DR KEGG; dme:Dmel_CG11064; -.
DR CTD; 43827; -.
DR FlyBase; FBgn0087002; apolpp.
DR VEuPathDB; VectorBase:FBgn0087002; -.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_225812_0_0_1; -.
DR InParanoid; Q9V496; -.
DR OMA; QGFKYQY; -.
DR OrthoDB; 487693at2759; -.
DR PhylomeDB; Q9V496; -.
DR SignaLink; Q9V496; -.
DR BioGRID-ORCS; 43827; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Rfabg; fly.
DR GenomeRNAi; 43827; -.
DR PRO; PR:Q9V496; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0087002; Expressed in head capsule and 30 other tissues.
DR ExpressionAtlas; Q9V496; baseline and differential.
DR Genevisible; Q9V496; DM.
DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:FlyBase.
DR GO; GO:0005319; F:lipid transporter activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR GO; GO:0006869; P:lipid transport; IDA:FlyBase.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; IDA:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.20.50.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF06448; DUF1081; 1.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Heme; Iron; Lipid transport; Lipid-binding; Lipoprotein;
KW Metal-binding; Reference proteome; Secreted; Signal; Transport;
KW Wnt signaling pathway.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8702812"
FT CHAIN 26..706
FT /note="Apolipophorin-2"
FT /id="PRO_0000041526"
FT CHAIN 707..3351
FT /note="Apolipophorin-1"
FT /id="PRO_0000041527"
FT DOMAIN 43..641
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 2786..2952
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT SITE 706..707
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1979
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT VARIANT 1696
FT /note="S -> Y (in strain: 253.30)"
FT /evidence="ECO:0000269|PubMed:11778050"
FT CONFLICT 2649
FT /note="F -> I (in Ref. 1; AAC47284)"
FT /evidence="ECO:0000305"
FT CONFLICT 2965
FT /note="Q -> E (in Ref. 1; AAC47284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3351 AA; 372677 MW; 3B193D725D011B9E CRC64;
MARMKYNIAL IGILASVLLT IAVNAENACN LGCPKSDNGL LKYIPGNYYD YSFDSILTIG
ASSDVPNDSD DTSLKVSGSA KIFAKGNCGY TLQLSSVKVT NTKESVEKKI LNSIQKPVQF
TLVSGILEPQ ICSDSSDLDY SLNIKRAVVS LLQSGIEAEH EVDVFGMCPT HTSTSKVGNA
NIITKARNLN SCSHREQINS GLVSGKVNEK AGITSSLLLQ ANYIKESRIV NHLIENVQLT
ETYKFIGNTK RNSDISAKVV TILKLKNPSG TKANSPGTGS TVRSLIFQRP ETYTSKNINA
LKTILSDLVD STGDYVKKET AKKFVEFIRL LRQSDSETLL ELAAFPHPNK VLARKVYLDG
LFRTSTAESA RVILKQLSKF DEKEKLLAIL SLNIVKSVDK ETLNQAASQL LPNAPKELYI
AVGNLVAKYC LKNYCQGPEI DAISKKFSDG LKHCKPNTKR EEERIVYILK GLGNAKSLSG
NTVAALSECA STGRSNRIRV AALHAFSKVK CEETLQSKSL ELLKNRNEDS ELRIEAYLSA
ISCPNAEVAN QISEIVNSET VNQVGGFISS NLKAIRDSTD VSRDQQKYHL ANIRVTKTFP
VDYRRYSFNN EVSYKLESLG VGASTDYQII YSQHGFLPRS SRINVTTEFF GTNYNVFEAS
VRQENVEDVL EYYLGPKGLV NKDFDEIVKL IEVGNNGVAA GGRARRSIVD DVSKISKKYK
MYGVKNVQDL NLDVSLKLFG SELAFLSLGD NIPSSLDDII NYFSTSFEKA KQELSSFEKQ
FSSHHLFLDT DLAYPTSIGV PLELVAQGFA ATKVDLAVSL DINAILEQNW QKAKYRLKFV
PSVDINANVQ IGFNAQVLST GLRVVSSAHS ATGSDITVAV ISDGEGFNVD LELPREKLEL
INFNVDTELY VAEQDKQKAI ALKGNKKNKN SQPSEICFNQ LELVGLNICI KSSTSLSEVQ
AGNGNVAERG LSVSEKFHLS RPFNFAVYLT TERKFTFKGI HTQEAFSQKW KLDYSTPGSK
VSHDTTVVYE LGNKPKTFSR LSFDNSQCHF AVEGGINNDK NELVVYGQYE QDKEIKKSKI
GFSKNGNEYK PLIEIQDNNG ISNSINGYHA DGKIVVKKNS NNIERYNFEN FQVSNSNNAH
VAVNGWSDVG TNSLTSELRI SLDHQTFLIK ENLKLENGLY EAGFFINDEH SPENIYGSSI
HLTIADQSYA LKTNGKAAAW SIGSDGSFNF QKLADSNSAR AGSLVENVEI QYKNKQVGGI
KIMSNFDVNK MDVDVEISRE QKIGSIIVKY ESNQRHAQDY SLEASAKINK HSIDVISKCD
FNGNVYVVDN SLVTSWGTLL SAKGEIGQRY SAQDININIQ GNVQISGKDK VTQWILKVIG
TPDKTNSDFR ISRDTSELIK LTSESQHPQD KISFAKLNLI VKNQLTAKGE FRVAKNGKGD
FTASIDTLKT EPKHKLEIES KFHIQSPKYD IDASLTLDGK RKVHLKSENT IEKLKFSTKN
IGEANDKIIA FEANGSLKGE LRGNGEIQGT FIFNAPDGRV IDGSINRKIS TNAKSGLSQG
NIDAQLSDTP FGSNKKRSIS LIGKLDRLNT KTKEFSANSN LVYTAFNGEK SEISYQIKQQ
PNGDAKNIDF SLKAYGNPLP QPFEIAFALG DYSAQHAVVS ITSKYGEIFS VSANGNYNNN
QALEYGLQAN IEIPKSTLKS LEINSHGKVL KSLIGNENAA YNVEFFLDSK TSLGQYARVN
TVWNGTANDG SYDFEAQTNN MESPLKFNGK YHRKQTGNIK DGDLTGKQTY VLNAQYGAQY
VKMDASLGYG AEKVDIAYVI DSSFDSVKDI KVNIRTFKPL DDSTYVVTAL FKQTDKSYGL
DTTFYHSAHK KGVDIRLDLL KEKPIIISSI AELLGDRKGK VLFEILNLAD LDIKINSEAS
YVSIDEFYII VNWSSKKLKL DGYELEARAQ SKNIKIQLKN ENGIIFSGTA TYALKKELNK
TIIDGQGKVQ YQGKALSGNF KLTRQHFDFG TDREVGFSYT FMGNLGSKNG LGTLKITNKE
FNTKFSVCEE KRQCTNLIVQ SIVSIDEQKL DAVEHTTLII VDLRDFGYPY EFELKSQNTR
QGLKYQYHLD SFIITGNNFK YQFTANVQPT SSTIKLALPK RQILFETTQK IPADGSLFGR
YEQTASFFID KLQKPDDVAR FSAIVDVTGT ERVAFNANGK LKFEHPTIRP LSISGQLNGD
VNQQIASAEV IFDIFRLPEQ KVVGNSELRN SRSQNGFNIA YITTVKSAGL QFQYQINSNA
AVDIEAHEYN IGLELNNGEI DVKAISFLNK EKFEISLSES NKHIIYIVGD FSKQNHYAKL
NTKVQILDKN PIEITSEVQP NSAKIILKRQ DFIDGTAEVK LGKEFKVDVI GSGKQLFNGR
VALDATNFLQ TNYFINEDHL NGFWHIVESE INKDSEYISE NIKERLKKSR QVTDKIVKLA
KEAGPDFSKL QGKLLDYKND IVQELEADQS IAPIIDGIRT LFKKIAGIVD DINKAISEIL
EKAQKSIVDI YDKLQALWKD SLLKAWEDFI ITVQKLISTL KTEFIKICTQ SFKDLLSALE
KYGPALKNYG KAIGEIVKPI NDAAQEVIKI VVNAAEGVTH EFKQYVASLP SFESIRNEFN
DKVKVLKLFE KATELTNSLF DQINILPQTP ETSEFLQKLH DYLIAKLKQE HIDNEKYIEE
LGQLLIKAVR SIWVSIRSTY PGSSDHVIDF QSWIGSLTHS FDSLAVLPSI LSFRSSILNC
LLNENWDVVF NKKLLYSWIF FNDFELRGHV VDGKHIFTFD GLNFAYPGNC KYILAQDSVD
NNFTIIGQLT NGKLKSITLI DREGSYFEVA DNLALKLNGN LVEYPQHLSG LHAWRRFYTI
HLYSEYGVGI VCTSDLKVCH ININGFYTSK TRGLLGNGNA EPYDDFLLID GTLAENSAAL
GNDYGVGKCT AIEFDNNQFK SSKRQEMCSE LFGIESTLAF NFITLDSRPY RKACDIALAK
VAEKEKEATA CTFALAYGSA VKQINKWVLL PPRCIKCAGP AGQHDFGDEF TVKLPNNKVD
VVFVVDINVT PGVLSNLIAP AINDIRESLR SRGFSDVQVG VIVFEETKRY PALLTSDGGK
INYKGNVADV KLAGIKSFCD NCVEQIITEK RILDIYNSLK EIVKGIAPQA DEKAFQLALD
YPFRAGAAKS IIGVRSDSLE YKNWWKFVRA QLTGSITKFD GALIHLIAPV KGLSLEGVLS
EKLIGFNSRL VATVDGKDSK KRTKLQFDND MGIDFVLNNG GWVFATQNFE KLKASDQKKM
LNQITSSLAD TLFKTEIVSD CRCLPIHGLH GQHKCVIKSS TFVANKKAKS A
