GenomeNet

Database: UniProt
Entry: B4H8M4_DROPE
LinkDB: B4H8M4_DROPE
Original site: B4H8M4_DROPE 
ID   B4H8M4_DROPE            Unreviewed;      3826 AA.
AC   B4H8M4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=GL25437 {ECO:0000313|EMBL:EDW35067.1};
GN   Name=Dper\GL25437 {ECO:0000313|EMBL:EDW35067.1};
GN   ORFNames=Dper_GL25437 {ECO:0000313|EMBL:EDW35067.1};
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN   [1] {ECO:0000313|EMBL:EDW35067.1, ECO:0000313|Proteomes:UP000008744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49
RC   {ECO:0000313|Proteomes:UP000008744};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SIMILARITY: Belongs to the thrombospondin family.
CC       {ECO:0000256|ARBA:ARBA00009456}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; CH479224; EDW35067.1; -; Genomic_DNA.
DR   RefSeq; XP_002027203.1; XM_002027167.1.
DR   STRING; 7234.B4H8M4; -.
DR   EnsemblMetazoa; FBtr0191052; FBpp0189544; FBgn0163021.
DR   eggNOG; KOG1216; Eukaryota.
DR   HOGENOM; CLU_000204_0_0_1; -.
DR   OMA; PQYICEC; -.
DR   PhylomeDB; B4H8M4; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   CDD; cd00057; FA58C; 2.
DR   CDD; cd19941; TIL; 7.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012111; Hml.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR   PANTHER; PTHR11339:SF373; HEMOLECTIN, ISOFORM A; 1.
DR   Pfam; PF08742; C8; 5.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF01826; TIL; 3.
DR   Pfam; PF00094; VWD; 5.
DR   PIRSF; PIRSF036569; Hml; 1.
DR   SMART; SM00832; C8; 5.
DR   SMART; SM00494; ChtBD2; 1.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00231; FA58C; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00214; VWC; 4.
DR   SMART; SM00215; VWC_out; 2.
DR   SMART; SM00216; VWD; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 4.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   PROSITE; PS51233; VWFD; 5.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..3826
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002808329"
FT   DOMAIN          174..205
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          458..633
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          824..1010
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          1311..1494
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          1834..1901
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          2050..2203
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          2231..2380
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          2680..2860
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          3012..3210
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          3368..3436
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          3737..3797
FT                   /note="CTCK"
FT                   /evidence="ECO:0000259|PROSITE:PS01225"
FT   DISULFID        177..187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        195..204
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3737..3791
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
FT   DISULFID        3741..3793
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00039"
SQ   SEQUENCE   3826 AA;  424812 MW;  ED0896D4AD97E493 CRC64;
     MAKKVIFLSV WLLLISHVWA EEGDLVMNDE DDEDINPLVQ AVPDAVDNEV GRDERHISFS
     LRNAPAVSAR YSYAGSGGGG AEYGGGIKTS ASAGGYGNQG NFYGNGGQSL AAYGKCSALE
     LPMNVHSECH NGRCKVSCPA GYSFGQDIQV LEMFCSNDGW IIGNSIFSVV PPCQAQCQPP
     CQNNGICLSA GVCQCPENYY GPACQQKKSV CASFPKAPKN SKVACMNNVC HAECMRGFQF
     PDGSAITNIE CRNGQWKHAK TGLSKPPDCG PTCDPACTNG GQCISFNVCQ CSKMFRGGHC
     QYNIASCNVT NTNFNGNYKC AYDLEEARCT FNCPQVPGLK VQGRLDIEYK CNYQQGQYLP
     SPLPKCIFPP GYTIRSSTST QKVTQQAGRV YHGGFSGEMA YEIRTEREKL LALLAKYRDL
     ERRSEWWSSE ETVVTPGRYS LYQSSELDVV IDKTPRPALC TTWGGINMKT FDGLVFKAPL
     SCSHTLITDK VSGTFDIILK ACPYGSGYGC AHSLKVLWQS VLYTFENLNG TIQLSTPIKK
     LPMSVQVMGM KVMPVAQHVQ IDLESVGLKL DWDHHQYVSV QAGPQMWGKV GGLCGSLDGD
     SNTDFVSRTG KKVETVKAFA DAWRVQDRSE MCLVENSAEL DFGMESCEQS RLQKAVSVCE
     RLLANEKLGD CIKPFNYEAL IRTCMADYCN CANREHPESC NCDAIAMLAK ECAFKGIKLE
     HGWRNLEICP ISCGFGRVYQ ACGPNVEPTC DSDVALSPTR DTCNEGCFCP EGTVQYKDAC
     ITRELCPCTL RGKEFKPEST VKKNCNTCTC KNGQWRCTDD KCGARCGAIG DPHYQTFDGK
     RYDFMGKCSY HLLKTPNMSV EAENVACSGA VSEALSFAAP DDPSCTKSVT IRFVLRDGTP
     SVIKLDQGLT TIVNDKPIAK LPKMLGLGEV LIRRASSTFL TVEFADGIRV WWDGVSRVYI
     DAPPSWRGQT QGLCGTFNSN TQDDFLTPEG DVETAVEPFA DKWRTKDTCQ FKAETHQGPH
     PCTLNPERKA QAEKHCDWIL QDIFQDCHFM VEPEQFYEDC LYDTCACKDE LSKCFCPILS
     AYGTECMRQG VKTGWRMTVK ECAVKCPMGQ IFDECGDGCA LTCDDLPSKG SCNRECVEGC
     RCPHGEYIND QGECVPKQKC HCSFDGMTFR PGYKEVRPGE KFLDLCTCQD GVWDCQDAEP
     GDKDKYPPSS ELRSKCTKQP FAEFTKCAPK EPKTCKNMDK YMADSTECLP GCVCMEGYVY
     DTSRLACVLP TNCSCHHAGK SYDDGEKIKE DCNLCVCQAG NWKCSENGCE STCSVWGDSH
     FSTFDGHDFD FQGACDYVLA KGVFEHGDGF SITIQNVLCG TMGVTCSKSL EISLSGHAQE
     SLILSADSAY STDPNKTPIK KLRDSVNSKG HNAFHIYKAG VFVVVEVIPL KLQVKWDEGT
     RVYVKLGNEW RHKVSGLCGN YNGNGLDDMQ TPSLGLETSP MLFGHSWKLQ PHCSAPVAPI
     DACKSHPERE TWAQLKCGAL KSELFEQCHS EVPLERYWKR CIFDTCACDQ GGDCECLCTA
     IAAYADACAQ KGINIRWRSQ HFCPMQCDPH CSDYKSCTPA CAVETCDNFL DQGIAERMCN
     RENCLEGCHI KPCDDGFIYL NDTYRECVPK AECKPVCMVR NGKTYYEGDI TYTDSCATCR
     CSKRKEICSG VKCNQPTLTT PAHSAPLVEG TTEAVPLATQ NQTKCVKGWT RWCDKDKDTS
     DKSVRLNDEE KVPRYDRMEN VYGTCLKEYM TKVECRVKDT YEAPEQMDEN VVCNLEEGLR
     CTGKCHDYEL RAFCQCDQEP LPPIPKPTER PQIGLTCDAG VVEYKDFPGD CHKFLHCQPK
     GVEGGWIYVE QTCGEYMMFN PTMFICDHIA TVQELKPSCG KKPQPEPESE PIKQCPEGKA
     WTDCANQCEH TCHYYGSILR KRGLCQPGEH CKPGCVDKLR PDCRMLGKYW RDEDTCVHAD
     ECPCMDKAEH YVQPHKPVFG EFEVCQCIDN AFSCVPNKPD PIPERPLEEV PELQLLEPIF
     PVTLTPPLHC ASDRLIPKIE NGPHSVADSI FNASSQLAPE HGPTKARLTK YNPRGSWSPN
     INDQMQYLEL NFGRPEPFYG VVMAGSPDFD SYVTLFKILH SHDGVAYHYL VDETEKPQMF
     NGPLDSRAPV QTLFKVPIEA SSLRIYPLKW HGSIAMRVEL LICGDKEEPR TTISIPPTST
     EHPAHLQEME CTDQMGVDDG KMYADQVQSS SVWQLPKPAK KPALLDLLKL STPLSWRPLS
     NTPNEFVEFD FLEPRNISGF VTKGGTDGWV TGYKVLFSKK KPTWNTVLSP SGQPRIFEAN
     VDGETERKHH FKKPILTQFL KVVPAKWERN INMRIEPLGC FKPYPEIKRQ VPVDNSPPTK
     CNICDGIASP QSSSSDCPCQ SQLALFWDGN SCVQHNLCPC VENYVSYPIG NKFENSACEE
     CVCVLGGHKN CKPKKCPPCQ DAKLRPVITS DCFCKCEPCP KQQRLCPSSG DCIPEVLWCN
     GVQDCADDED SSCRDSFTVE PDIKREKNET EIITCPAPVC PPQMKIKIIE KKTRKMSKMF
     SFSKQVSIVD DGVTITKTKF VSSKEQVLSM PTQELDFQVE EQCDEFTCVP IPSKLVDKNE
     TISCTEPKCP EKYDVELDMS TAKAGDCLKY TCVLRPNKDD VCEISGKSFT TFDGTLFKYG
     PCSHILARDI HNGSWSISVH QQCTDESRKI CHKVITIQDI QAGNELILLP HLKLKFNGFE
     FTVQQLINSP ICKASFVVSQ PGKTLLAVST KYGFWVQLDD IGIVKVGISS KFIRTVDGLC
     GFYNGNPRDD KRSPEGQIIA NTENFGDSWY DKRVPKDQCG DLKCSREMQA KALQLCNIIH
     HPTFARCHKA VNYKQFLNNY CLEAACDCMM ANNGDPAACK CNILESFVKK CLSVNPLVQL
     RTWRAVAQCE ITCPSPLVHT DCYKRRCEPS CDNVHGDDCP VLPDTCFPGC YCPEGTVRKG
     PNCVPISDCK DCVCNAMGAS NYMTYDRKSF SFNGNCTYLL SRDVVLPGVH TFQVYVSMDD
     CKKLGQSSPV DGGSCAKSLH ILNGDHVIHV QRVPLKPKSL QVLVDGFEVK QMPYKDSWIS
     LRQVVGKDLV LSLPESHVEL TASFADLIFS LGVPSIKYGS KMEGLCGDCN GNAANDLQPN
     PAKKKPGVDV IQSWQADEPR LGLTDAQKCL SEDVPKEQCI PLPPEKDPCL QFYNGELFGK
     CPLVVDPISY VSACQQDICK PGNTQQGVCV ALAAYAKECN QYGICTTWRR PQLCPYECPS
     DMVYESCGCA KTCDTVKAMS EYDAVSLKSQ TVIQTVKSDE MCINSERFEG CFCPSGQVLD
     AGKCVPEMAC SKCDDGVHLL GEKWPKDKCT DCQCDENGKT SCVQKKCQVE ENICAEDYKP
     QIIITKEECC PRYRCVPEPK DPTKLCLAPM MPVCGPGQFK KQKNDVNGCP QYICECKPKE
     ECEVLKPPRE LLPGEELVKI EEGCCPTQKI VCKPELCPKP PISCPERFYE VKTTKEVDAC
     CSTHSCLPPK NLCIVQYELD DSSKFTKQVG EKWTHAKDVC KRETCSYGPD GNAQVLSTLE
     KCSTDCAPGF SYQSLDKSKC CGKCIQSSCV FEQKLYGAND LWKSADNCTL YSCLKKDNQL
     MVTSSKEICP DVAGCLSHLL YQDGCCKRCK LEPLVEDKST CLPVSLAESQ TKEILKFSKS
     GHGVCVNAEP IKGFTDCQGA CSSGSKYNTL TGMHEKFCTC CSIKSHHPIS VKMVCQDGHT
     YSQRHEVPAN CGCSPCSELS DPPIDVRMLP DVQYPLLKLL GNHQDN
//
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