MEGF8_MOUSE
ID MEGF8_MOUSE Reviewed; 2789 AA.
AC P60882; B3GR00; Q80TR3; Q80V41; Q8BMN9; Q8JZW7; Q8K0J3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 8;
DE Short=Multiple EGF-like domains protein 8;
DE AltName: Full=Epidermal growth factor-like protein 4;
DE Short=EGF-like protein 4;
DE Flags: Precursor;
GN Name=Megf8; Synonyms=Egfl4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C3H/HeJ; TISSUE=Brain;
RX PubMed=18821597; DOI=10.1002/dvg.20432;
RA Cota C.D., Liu R.R., Sumberac T.M., Jung S., Vencato D., Millet Y.H.,
RA Gunn T.M.;
RT "Genetic and phenotypic studies of the dark-like mutant mouse.";
RL Genesis 46:562-573(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-1147 AND 1382-2789.
RC TISSUE=Brain, Colon, Mammary tumor, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1391-2789.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1645-2789.
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=29290584; DOI=10.1016/j.devcel.2017.12.003;
RA Pusapati G.V., Kong J.H., Patel B.B., Krishnan A., Sagner A., Kinnebrew M.,
RA Briscoe J., Aravind L., Rohatgi R.;
RT "CRISPR screens uncover genes that regulate target cell sensitivity to the
RT morphogen sonic hedgehog.";
RL Dev. Cell 44:113-129(2018).
CC -!- FUNCTION: Acts as a negative regulator of hedgehog signaling
CC (PubMed:29290584). {ECO:0000269|PubMed:29290584}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highest expression in brain, testis and kidney.
CC {ECO:0000269|PubMed:18821597}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36727.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH51121.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; EU723517; ACE00231.1; -; mRNA.
DR EMBL; BC031185; AAH31185.1; -; mRNA.
DR EMBL; BC036727; AAH36727.1; ALT_SEQ; mRNA.
DR EMBL; BC051121; AAH51121.1; ALT_SEQ; mRNA.
DR EMBL; BC060277; AAH60277.1; -; mRNA.
DR EMBL; AK122377; BAC65659.1; -; mRNA.
DR EMBL; AK030408; BAC26949.1; -; mRNA.
DR CCDS; CCDS52148.1; -.
DR RefSeq; NP_001153872.1; NM_001160400.1.
DR SMR; P60882; -.
DR BioGRID; 234725; 1.
DR STRING; 10090.ENSMUSP00000122192; -.
DR GlyConnect; 2516; 5 N-Linked glycans (5 sites).
DR GlyGen; P60882; 11 sites, 5 N-linked glycans (5 sites).
DR iPTMnet; P60882; -.
DR PhosphoSitePlus; P60882; -.
DR MaxQB; P60882; -.
DR PaxDb; P60882; -.
DR PeptideAtlas; P60882; -.
DR PRIDE; P60882; -.
DR ProteomicsDB; 292215; -.
DR Antibodypedia; 58360; 108 antibodies from 22 providers.
DR Ensembl; ENSMUST00000128119; ENSMUSP00000122192; ENSMUSG00000045039.
DR GeneID; 269878; -.
DR KEGG; mmu:269878; -.
DR UCSC; uc009fsj.2; mouse.
DR CTD; 1954; -.
DR MGI; MGI:2446294; Megf8.
DR VEuPathDB; HostDB:ENSMUSG00000045039; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000160262; -.
DR HOGENOM; CLU_000612_0_0_1; -.
DR InParanoid; P60882; -.
DR OMA; MTPRAAH; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; P60882; -.
DR TreeFam; TF321873; -.
DR BioGRID-ORCS; 269878; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Megf8; mouse.
DR PRO; PR:P60882; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P60882; protein.
DR Bgee; ENSMUSG00000045039; Expressed in otolith organ and 214 other tissues.
DR Genevisible; P60882; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IGI:UniProtKB.
DR GO; GO:0042074; P:cell migration involved in gastrulation; ISO:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; ISO:MGI.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:MGI.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IMP:UniProtKB.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:UniProtKB.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:UniProtKB.
DR GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; ISO:MGI.
DR GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:UniProtKB.
DR GO; GO:0060972; P:left/right pattern formation; IMP:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR Gene3D; 2.120.10.80; -; 4.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00053; Laminin_EGF; 4.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 4.
DR SMART; SM00423; PSI; 9.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Kelch repeat;
KW Laminin EGF-like domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..2789
FT /note="Multiple epidermal growth factor-like domains
FT protein 8"
FT /id="PRO_0000055630"
FT TOPO_DOM 28..2591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2592..2612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2613..2789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..140
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 138..168
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 170..203
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 241..287
FT /note="Kelch 1"
FT REPEAT 290..338
FT /note="Kelch 2"
FT REPEAT 346..399
FT /note="Kelch 3"
FT REPEAT 402..453
FT /note="Kelch 4"
FT REPEAT 459..511
FT /note="Kelch 5"
FT REPEAT 525..575
FT /note="Kelch 6"
FT DOMAIN 561..613
FT /note="PSI 1"
FT DOMAIN 847..899
FT /note="PSI 2"
FT DOMAIN 900..947
FT /note="PSI 3"
FT DOMAIN 1074..1115
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1163..1210
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1211..1261
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1263..1405
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1403..1445
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1522..1570
FT /note="Kelch 7"
FT REPEAT 1580..1629
FT /note="Kelch 8"
FT REPEAT 1632..1679
FT /note="Kelch 9"
FT REPEAT 1685..1735
FT /note="Kelch 10"
FT REPEAT 1740..1787
FT /note="Kelch 11"
FT REPEAT 1796..1841
FT /note="Kelch 12"
FT DOMAIN 1820..1860
FT /note="PSI 4"
FT DOMAIN 1868..1923
FT /note="PSI 5"
FT DOMAIN 2004..2062
FT /note="PSI 6"
FT DOMAIN 2064..2121
FT /note="PSI 7"
FT DOMAIN 2122..2160
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2197..2245
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2324..2387
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 2468..2508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2762..2789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYP0"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..57
FT /evidence="ECO:0000250"
FT DISULFID 142..152
FT /evidence="ECO:0000250"
FT DISULFID 146..158
FT /evidence="ECO:0000250"
FT DISULFID 174..184
FT /evidence="ECO:0000250"
FT DISULFID 178..191
FT /evidence="ECO:0000250"
FT DISULFID 193..202
FT /evidence="ECO:0000250"
FT DISULFID 1078..1091
FT /evidence="ECO:0000250"
FT DISULFID 1085..1100
FT /evidence="ECO:0000250"
FT DISULFID 1102..1114
FT /evidence="ECO:0000250"
FT DISULFID 1163..1171
FT /evidence="ECO:0000250"
FT DISULFID 1165..1179
FT /evidence="ECO:0000250"
FT DISULFID 1182..1191
FT /evidence="ECO:0000250"
FT DISULFID 1194..1208
FT /evidence="ECO:0000250"
FT DISULFID 1211..1224
FT /evidence="ECO:0000250"
FT DISULFID 1213..1231
FT /evidence="ECO:0000250"
FT DISULFID 1233..1242
FT /evidence="ECO:0000250"
FT DISULFID 1245..1259
FT /evidence="ECO:0000250"
FT DISULFID 1263..1302
FT /evidence="ECO:0000250"
FT DISULFID 1336..1367
FT /evidence="ECO:0000250"
FT DISULFID 1407..1421
FT /evidence="ECO:0000250"
FT DISULFID 1415..1433
FT /evidence="ECO:0000250"
FT DISULFID 1435..1444
FT /evidence="ECO:0000250"
FT DISULFID 2126..2139
FT /evidence="ECO:0000250"
FT DISULFID 2133..2148
FT /evidence="ECO:0000250"
FT DISULFID 2197..2205
FT /evidence="ECO:0000250"
FT DISULFID 2199..2214
FT /evidence="ECO:0000250"
FT DISULFID 2217..2226
FT /evidence="ECO:0000250"
FT DISULFID 2229..2243
FT /evidence="ECO:0000250"
FT DISULFID 2324..2333
FT /evidence="ECO:0000250"
FT DISULFID 2326..2341
FT /evidence="ECO:0000250"
FT DISULFID 2343..2368
FT /evidence="ECO:0000250"
FT DISULFID 2371..2385
FT /evidence="ECO:0000250"
FT CONFLICT 540
FT /note="L -> S (in Ref. 2; AAH51121)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="D -> N (in Ref. 2; AAH51121)"
FT /evidence="ECO:0000305"
FT CONFLICT 1391
FT /note="N -> K (in Ref. 3; BAC65659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2789 AA; 297487 MW; 0EF11D3C829FB23D CRC64;
MALGGALALA LALALAVLGP LSLRVLAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPQGPLLA SLSGSTRPPP IEASSGKMLL
HLFSDANYNL LGFNASFRFS LCPGGCQNHG QCKSPGVCVC EPGWGGPDCG LQECSAYCGS
HGTCASTLGP CRCEPGFLGR ACDLHLWENQ GAGWWHSVSA GDPAFSARIG AAGAFLSPPG
LLAVFGGQDL NKALGDLVLY NFSTNTWESW DLTPAPAARH SHVAVAWAGL LVLMGGELAN
GLLTNDVWAF SPLGGGHWEL LAPPASSSSG PPGLAGHAAA LVDDIWLYVS GGRTQHDLFS
SGLFRFRLDH TSRGYWEQVI PAGGRPPAAT GHSMVFHAPS RTLLVHGGHR PSTARFSVRV
NSTELFHVER RVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
MAYKVPPFVF QAPALDYHLD YCSMYTDHSV CSRDPECSWC QGACQAAPPP GTPSGACPAA
SCLGLGRLLS DCQACLAFSS PTAPPRGPGA LGWCVHNESC LPRPEQARCR GEQISGTVGW
WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNASQPDKV SIVRSTTITL TPSPETDVSL
VYRGFIHPLL PGGPGGPGAE DVAVWARAQR LHVLARMARG PDTENMEEVG RWVAQQEKET
RRLQRPGSDR LFPLPGRGNK YAVEIRGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
EPYRSSACTS YSSCLGCLAD QGCGWCLNSA TCHLRQGRAH CEDDGSGESL LVLVPALCPL
CEEHRDCHAC TQDPFCEWHQ STNRKGDAAC SRRGRGRGAL KNPEECPPLC SQRLTCEDCL
ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCGGFL TCHECLQSHE
CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ITHCNRTCLE DCGHGVCSGP PDFTCVCDLG
WTSDLPPPTP APGPPAPRCS RDCGCSFHSH CRRRGPGYCD ECQDWTWGEH CERCRPGSFG
NATGSGGCRP CQCNGHGDPR RGHCDNLTGL CFCQDHTEGA HCQICSPGYY GDPRAGGSCF
RECGGRALLT NVSSVALGSR RFGGLLPPGG GAARAGPGLS YCVWVVSATE ALQPCVPGTL
CPPLTLTFSP DSSTPCTLSY VLAFDGFPRF LDTGVVQSDR SLIAAFCGQR RDRPLTVQAL
SGLLVLHWEA NGSSSWGFNA SVGSARCGSG GPGSCPVPQE CVPQDGAAGA GLCRCPQGWA
GPHCRMALCP ENCNAHTGAG ICNQSLGVCI CAEGFGGPDC ATKLDGGQLV WETLMDSRLS
ADTASRFLHR LGHTMVEGPD ATLWMFGGLG LPQGLLGNLY RYSVSERRWT QMLAGAEDGG
PGPSPRSFHA AAYVPAGRGA MYLLGGLTAG GVTRDFWVLN LTTLQWRQEK PPQNMELPAV
AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATGTWV SGAQSGTPPT GLYGHSAVYH
EATDSLYVFG GFRFHVELAA PSPELYSLHC PDRTWSLLAP SQGAKPRPRL FHASALLGDT
MVVLGGRSDP DEFSSDVLLY QVNCNTWLLP ALTRPAFVGS PMEESVAHAV AAVGSRLYIS
GGFGGVALGR LLALTLPPDP CRLLPSPEAC NQSGACTWCH GACLSGDQAH RLGCGVPPCS
PMPRSPEECR RLRTCSECLA RHPRTLQPGD GEASIPRCKW CTNCPEGACI GRNGSCTSEN
DCRINQREVF WAGNCSEAAC GAADCEQCTR EGKCMWTRQF KRTGETRRIL SVQPTYDWTC
FSHSLLNVSP MPVESSPPLP CPTPCHLLPN CTSCLASKGA DGGWQHCVWS SSLQQCLSPS
YLPLRCMAGG CGRLLRGPES CSLGCAQATQ CALCLRRPHC GWCAWGGQDG GGHCMEGGLS
GPRDGLTCGR PGASWAFLSC PPEDECANGH HDCNETQNCH DQPHGYECSC KTGYTMDNVT
GVCRPVCAQG CVNGSCVEPD HCRCHFGFVG RNCSTECRCN RHSECAGVGA QDHCLLCRNH
TKGSHCEQCL PLFVGSALGG GTCRPCHAFC RGNSHVCVSR KELEMARKEP EKYSLDPEEI
ETWVAEGPSE DEAVCVNCQN NSYGDRCESC LHGYFLLDGK CTKCQCNGHA DTCNEQDGTG
CPCQNNTETG TCQGSSPSDR RDCYKYQCAK CRESFHGSPL GGQQCYRLIS VEQECCLDPT
SQTNCFHEPK RRALGPGRTV LFGVQPKFTN VDIRLTLDVT FGAVDLYVST SYDTFVVRVA
PDTGVHTVHI QPPPPPPPPP PPADGVPRVA ADLGGLGTGS GSGSPVEPRV REVWPRGLIT
YVTVTEPSAV LVVRSVRDRL VITYPHEHHA LKSSRFYLLL LGVGDPNGPG ANGSADSQGL
LFFRQDQAHI DLFVFFSVFF SCFFLFLSLC VLLWKAKQAL DQRQEQRRHL QEMTKMASRP
FAKVTVCFPP DPAGPAPAWK PAGLPPPAFR RSEPFLAPLL LTGAGGPWGP MGGGCCPPAL
PATTAGLRAG PITLEPTEDG MAGVATLLLQ LPGGPHAPNG ACLGSALVTL RHRLHEYCGG
SGGAGGSGHG GGGGRKGLLS QDNLTSMSL
