MEGF8_HUMAN
ID MEGF8_HUMAN Reviewed; 2845 AA.
AC Q7Z7M0; A8KAY0; O75097;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
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=C19orf49, EGFL4, KIAA0817;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP SEQUENCE REVISION.
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 416-2845 (ISOFORM 1).
RA Shan Y.X., Yu L.;
RT "Cloning, characterization and location of a novel human gene containing an
RT EGF domain.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1271.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP VARIANTS CRPT2 ARG-199; HIS-1566 AND GLY-2434.
RX PubMed=23063620; DOI=10.1016/j.ajhg.2012.08.027;
RA Twigg S.R., Lloyd D., Jenkins D., Elcioglu N.E., Cooper C.D., Al-Sannaa N.,
RA Annagur A., Gillessen-Kaesbach G., Huning I., Knight S.J., Goodship J.A.,
RA Keavney B.D., Beales P.L., Gileadi O., McGowan S.J., Wilkie A.O.;
RT "Mutations in multidomain protein MEGF8 identify a Carpenter syndrome
RT subtype associated with defective lateralization.";
RL Am. J. Hum. Genet. 91:897-905(2012).
CC -!- FUNCTION: Acts as a negative regulator of hedgehog signaling.
CC {ECO:0000250|UniProtKB:P60882}.
CC -!- INTERACTION:
CC Q7Z7M0; O15265: ATXN7; NbExp=2; IntAct=EBI-947617, EBI-708350;
CC Q7Z7M0; O00555: CACNA1A; NbExp=2; IntAct=EBI-947617, EBI-766279;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z7M0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7M0-2; Sequence=VSP_036067;
CC -!- DISEASE: Carpenter syndrome 2 (CRPT2) [MIM:614976]: An autosomal
CC recessive multiple congenital malformation disorder characterized by
CC multisuture craniosynostosis and polysyndactyly of the hands and feet,
CC in association with abnormal left-right patterning and other features,
CC most commonly obesity, umbilical hernia, cryptorchidism, and congenital
CC heart disease. {ECO:0000269|PubMed:23063620}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35084.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA32469.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011541; BAA32469.2; ALT_INIT; mRNA.
DR EMBL; AC011497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC153880; AAI53881.1; -; mRNA.
DR EMBL; AY280362; AAP35084.1; ALT_INIT; mRNA.
DR CCDS; CCDS12604.2; -. [Q7Z7M0-2]
DR CCDS; CCDS62693.1; -. [Q7Z7M0-1]
DR PIR; T00209; T00209.
DR RefSeq; NP_001258867.1; NM_001271938.1. [Q7Z7M0-1]
DR RefSeq; NP_001401.2; NM_001410.2. [Q7Z7M0-2]
DR SMR; Q7Z7M0; -.
DR BioGRID; 108274; 77.
DR IntAct; Q7Z7M0; 14.
DR MINT; Q7Z7M0; -.
DR STRING; 9606.ENSP00000251268; -.
DR GlyConnect; 1959; 13 N-Linked glycans (5 sites).
DR GlyGen; Q7Z7M0; 14 sites, 14 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7M0; -.
DR PhosphoSitePlus; Q7Z7M0; -.
DR BioMuta; MEGF8; -.
DR DMDM; 218511690; -.
DR EPD; Q7Z7M0; -.
DR jPOST; Q7Z7M0; -.
DR MassIVE; Q7Z7M0; -.
DR PaxDb; Q7Z7M0; -.
DR PeptideAtlas; Q7Z7M0; -.
DR PRIDE; Q7Z7M0; -.
DR ProteomicsDB; 69567; -. [Q7Z7M0-1]
DR ProteomicsDB; 69568; -. [Q7Z7M0-2]
DR Antibodypedia; 58360; 108 antibodies from 22 providers.
DR DNASU; 1954; -.
DR Ensembl; ENST00000251268.11; ENSP00000251268.5; ENSG00000105429.13. [Q7Z7M0-1]
DR Ensembl; ENST00000334370.8; ENSP00000334219.4; ENSG00000105429.13. [Q7Z7M0-2]
DR GeneID; 1954; -.
DR KEGG; hsa:1954; -.
DR MANE-Select; ENST00000251268.11; ENSP00000251268.5; NM_001271938.2; NP_001258867.1.
DR UCSC; uc002otl.4; human. [Q7Z7M0-1]
DR CTD; 1954; -.
DR DisGeNET; 1954; -.
DR GeneCards; MEGF8; -.
DR HGNC; HGNC:3233; MEGF8.
DR HPA; ENSG00000105429; Low tissue specificity.
DR MalaCards; MEGF8; -.
DR MIM; 604267; gene.
DR MIM; 614976; phenotype.
DR neXtProt; NX_Q7Z7M0; -.
DR OpenTargets; ENSG00000105429; -.
DR Orphanet; 65759; Carpenter syndrome.
DR PharmGKB; PA27666; -.
DR VEuPathDB; HostDB:ENSG00000105429; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000160262; -.
DR HOGENOM; CLU_000612_0_0_1; -.
DR InParanoid; Q7Z7M0; -.
DR OMA; MTPRAAH; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; Q7Z7M0; -.
DR TreeFam; TF321873; -.
DR PathwayCommons; Q7Z7M0; -.
DR SignaLink; Q7Z7M0; -.
DR BioGRID-ORCS; 1954; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; MEGF8; human.
DR GenomeRNAi; 1954; -.
DR Pharos; Q7Z7M0; Tbio.
DR PRO; PR:Q7Z7M0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7Z7M0; protein.
DR Bgee; ENSG00000105429; Expressed in cortical plate and 174 other tissues.
DR ExpressionAtlas; Q7Z7M0; baseline and differential.
DR Genevisible; Q7Z7M0; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:CAFA.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:UniProtKB.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISS:UniProtKB.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:CAFA.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:CAFA.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISS:CAFA.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:CAFA.
DR GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:CAFA.
DR GO; GO:0060972; P:left/right pattern formation; IMP:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:CAFA.
DR GO; GO:0010468; P:regulation of gene expression; ISS:CAFA.
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; -; 5.
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; 3.
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; 3.
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; 4.
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 Alternative splicing; Calcium; Craniosynostosis; Disease variant;
KW 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..2845
FT /note="Multiple epidermal growth factor-like domains
FT protein 8"
FT /id="PRO_0000055629"
FT TOPO_DOM 28..2647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2648..2668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2669..2845
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..1626
FT /note="Kelch 8"
FT REPEAT 1632..1679
FT /note="Kelch 9"
FT REPEAT 1685..1735
FT /note="Kelch 10"
FT REPEAT 1796..1843
FT /note="Kelch 11"
FT REPEAT 1852..1898
FT /note="Kelch 12"
FT DOMAIN 1876..1916
FT /note="PSI 4"
FT DOMAIN 1924..1979
FT /note="PSI 5"
FT DOMAIN 2060..2118
FT /note="PSI 6"
FT DOMAIN 2120..2177
FT /note="PSI 7"
FT DOMAIN 2178..2216
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2253..2301
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2380..2443
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1726..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2523..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2817..2845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2526..2543
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 217
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 1271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 2066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2229
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 2182..2195
FT /evidence="ECO:0000250"
FT DISULFID 2189..2204
FT /evidence="ECO:0000250"
FT DISULFID 2253..2261
FT /evidence="ECO:0000250"
FT DISULFID 2255..2270
FT /evidence="ECO:0000250"
FT DISULFID 2273..2282
FT /evidence="ECO:0000250"
FT DISULFID 2285..2299
FT /evidence="ECO:0000250"
FT DISULFID 2380..2389
FT /evidence="ECO:0000250"
FT DISULFID 2382..2397
FT /evidence="ECO:0000250"
FT DISULFID 2399..2424
FT /evidence="ECO:0000250"
FT DISULFID 2427..2441
FT /evidence="ECO:0000250"
FT VAR_SEQ 700..766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9693030"
FT /id="VSP_036067"
FT VARIANT 199
FT /note="G -> R (in CRPT2)"
FT /evidence="ECO:0000269|PubMed:23063620"
FT /id="VAR_069305"
FT VARIANT 1566
FT /note="R -> H (in CRPT2; dbSNP:rs397515427)"
FT /evidence="ECO:0000269|PubMed:23063620"
FT /id="VAR_069306"
FT VARIANT 2434
FT /note="S -> G (in CRPT2; dbSNP:rs397515428)"
FT /evidence="ECO:0000269|PubMed:23063620"
FT /id="VAR_069307"
SQ SEQUENCE 2845 AA; 303100 MW; DDBF0EE07511587D CRC64;
MALGKVLAMA LVLALAVLGS LSPGARAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPRGPLLA SLSGSTRPPP IEASSGKMLL
HLFSDANYNL LGFNASFRFS LCPGGCQSHG QCQPPGVCAC EPGWGGPDCG LQECSAYCGS
HGTCASPLGP CRCEPGFLGR ACDLHLWENQ GAGWWHNVSA RDPAFSARIG AAGAFLSPPG
LLAVFGGQDL NNALGDLVLY NFSANTWESW DLSPAPAARH SHVAVAWAGS LVLMGGELAD
GSLTNDVWAF SPLGRGHWEL LAPPASSSSG PPGLAGHAAA LVDDVWLYVS GGRTPHDLFS
SGLFRFRLDS TSGGYWEQVI PAGGRPPAAT GHSMVFHAPS RALLVHGGHR PSTARFSVRV
NSTELFHVDR HVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
MAYKVPPFVF QAPAPDYHLD YCSMYTDHSV CSRDPECSWC QGACQAAPPP GTPLGACPAA
SCLGLGRLLG DCQACLAFSS PTAPPRGPGT LGWCVHNESC LPRPEQARCR GEQISGTVGW
WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNTSQPDKV SIVRSTTITL TPSAETDVSL
VYRGFIYPML PGGPGGPGAE DVAVWTRAQR LHVLARMARG PDTENMEEVG RWVAHQEKET
RRLQRPGSAR LFPLPGRDHK YAVEIQGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
EPYRSSSCTS YSSCLGCLAD QGCGWCLTSA TCHLRQGGAH CGDDGAGGSL LVLVPTLCPL
CEEHRDCHAC TQDPFCEWHQ STSRKGDAAC SRRGRGRGAL KSPEECPPLC SQRLTCEDCL
ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCDGFL TCHECLQSHE
CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ISHCNRTCLE DCGHGVCSGP PDFTCVCDLG
WTSDLPPPTP APGPPAPRCS RDCGCSFHSH CRKRGPGFCD ECQDWTWGEH CERCRPGSFG
NATGSRGCRP CQCNGHGDPR RGHCDNLSGL CFCQDHTEGA HCQLCSPGYY GDPRAGGSCF
RECGGRALLT NVSSVALGSR RVGGLLPPGG GAARAGPGLS YCVWVVSATE ELQPCAPGTL
CPPLTLTFSP DSSTPCTLSY VLAFDGFPRF LDTGVVQSDR SLIAAFCGQR RDRPLTVQAL
SGLLVLHWEA NGSSSWGFNA SVGSARCGSG GPGSCPVPQE CVPQDGAAGA GLCRCPQGWA
GPHCRMALCP ENCNAHTGAG TCNQSLGVCI CAEGFGGPDC ATKLDGGQLV WETLMDSRLS
ADTASRFLHR LGHTMVDGPD ATLWMFGGLG LPQGLLGNLY RYSVSERRWT QMLAGAEDGG
PGPSPRSFHA AAYVPAGRGA MYLLGGLTAG GVTRDFWVLN LTTLQWRQEK APQTVELPAV
AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATGTWV SGAQSGTPPT GLYGHSAVYH
EATDSLYVFG GFRFHVELAA PSPELYSLHC PDRTWSLLAP SQGAKRDRMR NVRGSSRGLG
QVPGEQPGSW GFREVRKKMA LWAALAGTGG FLEEISPHLK EPRPRLFHAS ALLGDTMVVL
GGRSDPDEFS SDVLLYQVNC NAWLLPDLTR SASVGPPMEE SVAHAVAAVG SRLYISGGFG
GVALGRLLAL TLPPDPCRLL SSPEACNQSG ACTWCHGACL SGDQAHRLGC GGSPCSPMPR
SPEECRRLRT CSECLARHPR TLQPGDGEAS TPRCKWCTNC PEGACIGRNG SCTSENDCRI
NQREVFWAGN CSEAACGAAD CEQCTREGKC MWTRQFKRTG ETRRILSVQP TYDWTCFSHS
LLNVSPMPVE SSPPLPCPTP CHLLPNCTSC LDSKGADGGW QHCVWSSSLQ QCLSPSYLPL
RCMAGGCGRL LRGPESCSLG CAQATQCALC LRRPHCGWCA WGGQDGGGRC MEGGLSGPRD
GLTCGRPGAS WAFLSCPPED ECANGHHDCN ETQNCHDQPH GYECSCKTGY TMDNMTGLCR
PVCAQGCVNG SCVEPDHCRC HFGFVGRNCS TECRCNRHSE CAGVGARDHC LLCRNHTKGS
HCEQCLPLFV GSAVGGGTCR PCHAFCRGNS HICISRKELQ MSKGEPKKYS LDPEEIENWV
TEGPSEDEAV CVNCQNNSYG EKCESCLQGY FLLDGKCTKC QCNGHADTCN EQDGTGCPCQ
NNTETGTCQG SSPSDRRDCY KYQCAKCRES FHGSPLGGQQ CYRLISVEQE CCLDPTSQTN
CFHEPKRRAL GPGRTVLFGV QPKFTNVDIR LTLDVTFGAV DLYVSTSYDT FVVRVAPDTG
VHTVHIQPPP APPPPPPPAD GGPRGAGDPG GAGASSGPGA PAEPRVREVW PRGLITYVTV
TEPSAVLVVR GVRDRLVITY PHEHHALKSS RFYLLLLGVG DPSGPGANGS ADSQGLLFFR
QDQAHIDLFV FFSVFFSCFF LFLSLCVLLW KAKQALDQRQ EQRRHLQEMT KMASRPFAKV
TVCFPPDPTA PASAWKPAGL PPPAFRRSEP FLAPLLLTGA GGPWGPMGGG CCPPAIPATT
AGLRAGPITL EPTEDGMAGV ATLLLQLPGG PHAPNGACLG SALVTLRHRL HEYCGGGGGA
GGSGHGTGAG RKGLLSQDNL TSMSL
