GenomeNet

Database: UniProt
Entry: A0A068YKN2_ECHMU
LinkDB: A0A068YKN2_ECHMU
Original site: A0A068YKN2_ECHMU 
ID   A0A068YKN2_ECHMU        Unreviewed;       535 AA.
AC   A0A068YKN2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Fibrillin 2 {ECO:0000313|EMBL:CDS42819.1};
GN   ORFNames=EmuJ_001054000 {ECO:0000313|EMBL:CDS42819.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42819.1};
RN   [1] {ECO:0000313|EMBL:CDS42819.1}
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:CDS42819.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the LTBP family.
CC       {ECO:0000256|ARBA:ARBA00038081}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN902842; CDS42819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YKN2; -.
DR   STRING; 6211.A0A068YKN2; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   OMA; HECINTY; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 1.
DR   InterPro; IPR026823; cEGF.
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; IPR017878; TB_dom.
DR   InterPro; IPR036773; TB_dom_sf.
DR   PANTHER; PTHR24034:SF111; -; 1.
DR   PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF12661; hEGF; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF57581; TB module/8-cys domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51364; TB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Growth factor binding {ECO:0000256|ARBA:ARBA00023183};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..535
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009741812"
FT   DOMAIN          137..187
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   DOMAIN          202..242
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          244..287
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          292..330
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
SQ   SEQUENCE   535 AA;  59045 MW;  230FEF85F5A36D82 CRC64;
     MQVTFGVRIL LPLLVLFLSS PRLCDAYSSG RGPNVCGTFY GLTLCCKGWT KSLDGLCTTA
     ICDGNCGERG SCIAPNQCRC EDGRVQDDCL MEDDNGYLAD EPVRCPSNCN NQGRCINGKC
     VCDFGFKGSA CDEEEIGPCF IQTERGVCKN KVTDPGNKTA MMTQNACCGS IGVAWGGLCQ
     RCSAQSSYCG KGYIRLNHHC VDINECEIPN VCMGGICRNT DGSFECDCPY GHVYDKNTVQ
     CRPILDGCQK NPKACTPGGR CIPLHGTAYI CQCDSGYVAT DGNTRCRKEE VALNYCEIFE
     GRLCKNGECH PTASSYDCTC NPGYVPSRFK KQCIKEFNAC TFYGNSVCTN GQCVPVDRSF
     RCICNPGYVL SGDGTACLDK CQQLGPSVCQ NGFCVPRPYG DYECRCHYGY QPSPDRKSCL
     MQLNPFQTSK REPLSSGNIY RGSYQADWPQ ENRVYHHVKP QLGETRWQPS SRVKYPNPCA
     DSAVRRKCMG GFCINLGRGS YECRCYKGYR AVNGNQQCVA DYGRTNRKYN WPTRG
//
DBGET integrated database retrieval system