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   17-JUN-2020, entry version 168.
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 mutations 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; 15.
DR   IntAct; Q7Z7M0; 13.
DR   MINT; Q7Z7M0; -.
DR   STRING; 9606.ENSP00000251268; -.
DR   GlyConnect; 1959; -.
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; 100 antibodies.
DR   Ensembl; ENST00000251268; ENSP00000251268; ENSG00000105429. [Q7Z7M0-1]
DR   Ensembl; ENST00000334370; ENSP00000334219; ENSG00000105429. [Q7Z7M0-2]
DR   GeneID; 1954; -.
DR   KEGG; hsa:1954; -.
DR   UCSC; uc002otl.4; human. [Q7Z7M0-1]
DR   CTD; 1954; -.
DR   DisGeNET; 1954; -.
DR   EuPathDB; HostDB:ENSG00000105429.12; -.
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   eggNOG; KOG1388; Eukaryota.
DR   eggNOG; ENOG410YF0N; LUCA.
DR   GeneTree; ENSGT00940000160262; -.
DR   HOGENOM; CLU_000612_0_0_1; -.
DR   InParanoid; Q7Z7M0; -.
DR   KO; K23664; -.
DR   OMA; WMYGGLS; -.
DR   OrthoDB; 49565at2759; -.
DR   PhylomeDB; Q7Z7M0; -.
DR   TreeFam; TF321873; -.
DR   SignaLink; Q7Z7M0; -.
DR   BioGRID-ORCS; 1954; 4 hits in 788 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 tendon of biceps brachii and 203 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:UniProtKB.
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:UniProtKB.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
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:UniProtKB.
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:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd00041; CUB; 1.
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; IPR013032; EGF-like_CS.
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; Laminin_EGF.
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 mutation;
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   COMPBIAS        2528..2564
FT                   /note="Pro-rich"
FT   COMPBIAS        2739..2833
FT                   /note="Gly-rich"
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
//