ID A0A068YG03_ECHMU Unreviewed; 1462 AA.
AC A0A068YG03;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Fibrillin 1 {ECO:0000313|EMBL:CDS42265.1};
GN ORFNames=EmuJ_000997200 {ECO:0000313|EMBL:CDS42265.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42265.1};
RN [1] {ECO:0000313|EMBL:CDS42265.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS42265.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; LN902842; CDS42265.1; -; Genomic_DNA.
DR STRING; 6211.A0A068YG03; -.
DR eggNOG; KOG1217; Eukaryota.
DR OMA; TSSNHNC; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 19.
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; IPR013111; EGF_extracell.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24040:SF13; FIBROPELLIN-1; 1.
DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF07645; EGF_CA; 11.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 31.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00180; EGF_Lam; 6.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009741747"
FT DOMAIN 218..251
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 350..383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 385..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 460..496
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 610..651
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 685..726
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 760..801
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 835..871
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 953..987
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1031..1064
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1103..1139
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1188..1218
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1294..1336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1340..1372
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1374..1416
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 222..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 241..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 373..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 977..986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1054..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1107..1117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1129..1138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1192..1202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1208..1217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1344..1354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1362..1371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1462 AA; 160379 MW; 28A819D408134315 CRC64;
MFWFTLPLLA LLQISAAINS TTYSEVARLI QQHGEGRENL DVVGLRPPLP SDKFNNNYIE
IPEIIDNAVH EEQFPPAGRL PPGAQWNEEG QYWGYQHSPP RRVAWNEATC VPPYCIPAMC
SDTGTGPLCP QNCVTENCSV GCFPFCIGGS QCIGRVCHCD AFRRQSACNL IRSSDCQNFF
GLSCAFGCFK PATDIPPSGC DCLIPFYVRL QPMCATESLL ACPNNCSNHG ICDHKTGQCM
CKPGFTGPSC SSKDYCFNSL ELPPCEYGCI SLNNSRLCTC PETLVLQPDG VSCGNPCPPG
LTGPQCSYDI DECLTGIHEC EYYCVNTFGS YSCRCLPGMT LNPRNNRTCI GRTCDPPCLP
EQGECITGGV CKCRPGFQGV SCEFDVDECA IGTSGCNHDC INTFGSFRCL CRPGYKLDSR
DNKTCIEKEC SPRCTPGQGE CVEGRCQCKD GFEGRTCEND IDECAAGVHN CQDRCVNTYG
SFRCECRYGY MLDNRDNRSC IPRECIPQCY LGQGVCVEGQ CQCTQGFRGV ACERDVNECQ
EGFHNCEQRC INNHGSFECA CYEGYRPLPT DPSRCERIKC EPECVPGQGV CNGGICQCQE
GFTGRFCERD VDECREGLHN CEQECVNLPG SFQCRCYEGY RPSPHNPNHC EPLTCSPECV
KGQGYCRNGV CECHRGYTGK ACERDVDECY EGTHDCQQRC INTQGSYQCT CDEGYHSVPS
DPRLCEPIRC ELGCVFGQGQ CIQGVCECKE GFTGVACEKD VDECRENRHR CEHNCVNTHG
SYACTCSQGY QPSPYDPRRC EPLRCEPDCV PGQGACYNGV CQCNPGFTGK SCEEDVDECK
LRINECDHTC VNTFGSYECR CDPGYELSLN DSHKCVPGDC MTNCVPGKGD CDKYGRCICR
PGYEGPYCQH EADLCSTGHH ECEHICVSLP GKRHLCRCYS GYIPDPKNPN RCIEFGCQPP
CEIGQGECDI ETKTCKCNSG FEGKRCERNI NECAVDNGGC SNLCVDTHGS YHCECPLGMH
LAPNSTTICV NDELCDPPCW LGRGVCVAAN TCKCNDGFAG KYCEIIQNAC KAFRPCEQEC
VNLGGETYEC RCRTGYVPAQ PNNATACKPS CQVGENCIHG RCVVGQCVCQ PGFAGERCDR
DIDECSGEAG IQVMCQQRCL NTPGWYECQC ESGYELQPDG FSCRRVDNGN KCPGGCLNGG
VCVSRCQCPP GFRGTRCEEV VDVCREEEPC DQVCYSKPDG GYLCACHEGY ELNPNGRTCS
PSEACDPPCV GKAQCLRGRC ICPAGFQGPR CDADIDECAM PAYVHGCAHG CRNVHGSYEC
ICPPGYTQMP DKRTCIMAGS SDDCTRPCRN GGVCRGNNMC SCTRGFEGSD CSQDIDECVT
LAPCDPDFGT CINRYGGYEC VCQPGYILLL DGRHCIQEAR ARQAPHLVFR GHGVKGISLG
TRVESGSSLR DSHLSTLKRW LR
//
