MEGF8_RAT
ID MEGF8_RAT Reviewed; 2788 AA.
AC Q9QYP0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 23-FEB-2022, entry version 124.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1915-2788, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Acts as a negative regulator of hedgehog signaling.
CC {ECO:0000250|UniProtKB:P60882}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:9693030}.
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DR EMBL; AABR03001918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03001941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03004237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB011534; BAA88689.1; -; mRNA.
DR SMR; Q9QYP0; -.
DR IntAct; Q9QYP0; 1.
DR STRING; 10116.ENSRNOP00000027831; -.
DR GlyGen; Q9QYP0; 6 sites.
DR iPTMnet; Q9QYP0; -.
DR PhosphoSitePlus; Q9QYP0; -.
DR PaxDb; Q9QYP0; -.
DR PRIDE; Q9QYP0; -.
DR UCSC; RGD:621190; rat.
DR RGD; 621190; Megf8.
DR eggNOG; KOG1388; Eukaryota.
DR InParanoid; Q9QYP0; -.
DR PhylomeDB; Q9QYP0; -.
DR TreeFam; TF321873; -.
DR PRO; PR:Q9QYP0; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:CAFA.
DR GO; GO:0060972; P:left/right pattern formation; ISS:CAFA.
DR GO; GO:0035108; P:limb morphogenesis; ISO:RGD.
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; -; 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; 3.
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..2788
FT /note="Multiple epidermal growth factor-like domains
FT protein 8"
FT /id="PRO_0000055631"
FT TOPO_DOM 28..2590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2591..2611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2612..2788
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..1678
FT /note="Kelch 9"
FT REPEAT 1684..1734
FT /note="Kelch 10"
FT REPEAT 1739..1786
FT /note="Kelch 11"
FT REPEAT 1795..1840
FT /note="Kelch 12"
FT DOMAIN 1819..1859
FT /note="PSI 4"
FT DOMAIN 1867..1922
FT /note="PSI 5"
FT DOMAIN 2003..2061
FT /note="PSI 6"
FT DOMAIN 2063..2120
FT /note="PSI 7"
FT DOMAIN 2121..2159
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2196..2244
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2323..2386
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 2465..2507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2761..2788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2467..2485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1353
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
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 1271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2172
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 2125..2138
FT /evidence="ECO:0000250"
FT DISULFID 2132..2147
FT /evidence="ECO:0000250"
FT DISULFID 2196..2204
FT /evidence="ECO:0000250"
FT DISULFID 2198..2213
FT /evidence="ECO:0000250"
FT DISULFID 2216..2225
FT /evidence="ECO:0000250"
FT DISULFID 2228..2242
FT /evidence="ECO:0000250"
SQ SEQUENCE 2788 AA; 297554 MW; 0CFB8141F3E03C10 CRC64;
MALGGALAAA LALAFAVLGP LSHKVLAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPQGPLLA SLSGSTRPPP IEASSGKMLL
HLFSDANYNL LGFNASFRFS LCPGGCQNHG QCKSPGVCVC EPGWGGPDCG LQECSAYCGS
HGTCASTLGP CRCEPGFLGR ACDLHLWENQ GAGWWHSVSA GDPAFSARVG AAGAFLSPPG
LLAVFGGQDL NKALGDLVLY NFSTNTWESW DLTPAPAARH SHVAVAWAGF LVLMGGELAN
GLLTNDVWAF SPLGGGHWEL LAPPASSSSG PPGLAGHAAA LVDDIWLYVS GGRTQHDLFS
SGLFRFRLDH TSRGYWEQVI PAGGRPPAAT GHSMVFHAPS RTLLVHGGHR PSTARFSVRV
NSTELFHVDR RVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
MAYKVPPFVF QAPALDYHLD YCSMYTDHSV CSRDPECSWC QGACQSAPPP GTPSGACPAA
SCLGLGRLLS DCQACLAFSS PTAPPRGPGT LGWCVHNESC LPRPEQARCR GEQISGTVGW
WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNASQPDKV SIVRSTTITL TPSAETDVSL
VYRGFIYPML PGGPGGPGAE DVAVWARAQR LHVLARMARG PDTENMEEVG RWVAQQEKET
RRLQRPGSSR LFPLPGRGNK YAVEIRGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
EPYRSLACSS YSSCLGCLAD QGCGWCLNSA TCHLRQGRAH CEDDGNGESL LVLVPALCPL
CEEHRDCHAC TQDPFCEWHQ STNRKGDAAC SRRGRGRGAL KNPEECPPLC SQRLTCEDCL
ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCHGFL TCHECLQSHE
CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ITHCNRTCLE DCGHGVCSGP PDFTCVCDLG
WTSDLPPPTP APGPPAPRCS RDCGCNFHSH CRRRGPGYCD ECQDWTWGEH CERCRPGSFG
NATGSGGCRP CQCNGHGDPR RGHCDNLSGL CFCQDHTEGA HCQICSPGYY GDPRAGGSCF
RECGGRALLT NVSSVALGSR RFGGLLPPGG GTARAGPGLS YCVWVVSATE ALQPCAPGTL
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 GITCDFWVLN LTTLQWRQEK APQSIELPAV
AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATTWVS GAQSGTPPTG LYGHSAVYHE
ATDSLYVFGG FRFHVELAAP SPELYSLHCP DRTWSLLAPS QGAKPRPRLF HASALLGDTM
VVLGGRSDPD EFSSDVLLYQ VNCNTWLLPD LTRPAFVGSP MEESVAHAVA AVGSRLYISG
GFGGVALGRL LALTLPPDPC RLLPSPEACN QSGACTWCHG ACLSGDQAHR LGCGVPPCSP
MPRSPEECRR LRTCSECLAR HPRTLQPGDG EASVPRCKWC TNCPEGACIG RNGSCTSEND
CRINQREVFW AGNCSEAACG AADCEQCTRE GKCMWTRQFK RTGETRRILS VQPTYDWTCF
SHSLLNVSPM PVESSPPLPC PTPCHLLPNC TSCLASKGAD GGWQHCVWSS SLQQCLSPSY
LPLRCMAGGC GRLLRGPESC SLGCAQATQC ALCLRRPHCG WCAWGGQDGG GHCMEGGLSG
PRDGLTCGRP GASWAFLSCP PEDECANGHH DCNETQNCHD QPHGYECSCK TGYTMDNVTG
VCRPVCAQGC VNGSCVEPDH CRCHFGFVGR NCSTECRCNR HSECAGVGAR DHCLLCRNHT
KGSHCEQCLP LFVGSALGGG TCRPCHAFCR GNSHVCVSRK ELEMARREPE KYSLDPEEIE
AWVAEGPSED EAVCVNCQNN SYGDRCESCL HGYFLLDGKC TKCQCNGHAD TCNEQDGTGC
PCQNNTETGV CQGSSPSDRR DCYKYQCAKC RESFHGSPLG GQQCYRLISV EQECCLDPTS
QTNCFHEPKR RALGPGRTVL FGVQPKFTNV DIRLTLDVTF GAVDLYVSTS YDTFVVRVAP
DTGVHTVHIQ PPPPPPPPPP PADGVPRVAS DLGGLGTGSG SGSPVEPRVR EVWPRGLITY
VTVTEPSAVL VVRSVRDRLV ITYPHEHHAL KSSRFYLLLL GVGDPNGPGA NGSADSQGLL
FFRQDQAHID LFVFFSVFFS CFFLFLSLCV LLWKAKQALD QRQEQRRHLQ EMTKMASRPF
AKVTVCFPPD PAGPAPAWKP AGLPPPAFRR SEPFLAPLLL TGAGGPWGPM GGGCCPPALP
ATTAGLRAGP ITLEPTEDGM AGVATLLLQL PGGPHAPNGA CLGSALVTLR HRLHEYCGGS
GGAGGSGHGG GGGRKGLLSQ DNLTSMSL
