GenomeNet

Database: UniProt
Entry: D6W6H4_TRICA
LinkDB: D6W6H4_TRICA
Original site: D6W6H4_TRICA 
ID   D6W6H4_TRICA            Unreviewed;      1796 AA.
AC   D6W6H4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN   Name=AUGUSTUS-3.0.2_04709 {ECO:0000313|EMBL:EFA11111.1};
GN   ORFNames=TcasGA2_TC004709 {ECO:0000313|EMBL:EFA11111.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA11111.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA11111.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11111.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA11111.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11111.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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; KQ971307; EFA11111.1; -; Genomic_DNA.
DR   STRING; 7070.D6W6H4; -.
DR   EnsemblMetazoa; TC004709_001; TC004709_001; TC004709.
DR   eggNOG; KOG3509; Eukaryota.
DR   HOGENOM; CLU_001582_2_0_1; -.
DR   InParanoid; D6W6H4; -.
DR   OMA; AMEISPF; -.
DR   PhylomeDB; D6W6H4; -.
DR   Proteomes; UP000007266; Linkage group 1.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00055; EGF_Lam; 2.
DR   CDD; cd00104; KAZAL_FS; 7.
DR   CDD; cd00110; LamG; 3.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 3.30.60.30; -; 9.
DR   Gene3D; 2.10.25.10; Laminin; 6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10913:SF45; AGRIN; 1.
DR   PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07648; Kazal_2; 9.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   Pfam; PF00054; Laminin_G_1; 2.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00057; FIMAC; 5.
DR   SMART; SM00274; FOLN; 8.
DR   SMART; SM00280; KAZAL; 9.
DR   SMART; SM00282; LamG; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 9.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 8.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE   4: Predicted;
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..50
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          77..129
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          145..199
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          219..271
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          272..344
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          367..417
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          435..486
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          695..747
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          820..876
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          1029..1066
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1074..1252
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1253..1290
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1292..1329
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1337..1514
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1522..1560
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1615..1791
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        695..707
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        697..714
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        716..725
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1056..1065
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1280..1289
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1319..1328
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1550..1559
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1796 AA;  197469 MW;  CB11C46B77DE1E96 CRC64;
     MCQCPTHCKQ KVDLVCGTDG KTYANRCQLR VASCKARLNT RVKHDGECEQ NDPCRDKQCG
     FGARCVVSPD GRNASCVCPD KCPSYGDHTT SRPVCGSDGI DYRNQCELQK AACTSNTNIT
     IKFLGKCDPC AGVECAEPEV CQLDEHRNPV CRCGDSCPLE FTPVCGSDGK TYSNECTLRQ
     EACRARKNLH IIYRGKCSSG INPCMSVRCT LGEECAINKF GIARCQCPPS CEPIMRPVCS
     KDGRTFPSEC ELKRTACLTR TTIEISYSGV CGEKGPCSEY QCQNGATCVE RFGVAHCECP
     VCPAEFEPVC GSDGISYGNE CKLRLEACKH PRNITVLYDG PCNGCETKKC DFYSVCERDS
     ATEGRCVCPK SCTDPELNDG TVCGTDGVTY ANECELRMTS CKMKQFILVA YKGNCDLCQG
     VECKYGGRCE AGKCVCPTNC EGSGDEPVCA SNMMTFPNEC ELQKAMCLQP TNSPPLSVVF
     YGDCREKFPV AGSLSTTLSP FTAQTNNIGP GTDLDTVGPE NTIPDLSTVE KEACRDIHCD
     FEATCELGPD NFPRCTCQFD CASAALVSAS KPVCASDLQI YPSLCAMKME ACQRQEELRL
     RPLDLCQGME VKPCNGEKPL TDPLTGKELD CGSGPKRQDC PSGSYCHQTT RFSRCCPKDQ
     GLLEQKSCED SWHGCCPDGK TAAQGPNHAG CPSLCGCNKL GSYSDTCDPE TQQCRCRPGV
     GGAKCDRCEP GYWGLPKISS GYHGCIPCGC STFGSVRDDC EQMTGRCVCN PGVQGQKCTV
     CTSHDKVLGP NGCVPADLTT SPPTTCKELT CYFGATCVER GGFAICECHT ECPQENDAQV
     VCGSDGQTYA SACELRQVAC RTQKDIVVQA FGTCKDDMFP STDWPIRRYT PLQFTQPDDS
     NSPLSKSTRH LLVPDPRYYY GSSGSIMRPV QGVSYPAETD NKAAFEINVS ATGPNAIYNT
     RGGNYAPAYR PTPATVRVIT ALLGDLCSDN SDCMIMYSHC VSGACTCLPN HSESSDRQEC
     IADPNPTDEY RACSSSPCHH GSTCVDLPAA TFTCVCETNF TGSLCETEVI HKQYNTPAFH
     GRSYVKLKPL KAYHKLSIEV EFKTHSHDGL LLYNQQKPDG LGDFVSLAIV NGFVEFKYNL
     GNGHVLIRSV DKIQLGVFHR VVIKRYHRDG ILKLDEGEDV AGQAKGTLKA LDLLEDTYVG
     FLPSNYTRVY ENIGTAKGFR GCIRKLKIGR RPIELHVNRD DWVLGAEAVS ECGDSPCSAA
     PCANDAKCAL ITPETYRCEC GPHYRGEFCE KPIEPCRSNP CKFGSTCTPL SPDAYICECP
     PGRTGTRCEM EDKYMGIVNP EFSGSSYIRL PRLEGVRKTF SIEVYFMPKA ANGLILYNGQ
     LKNGRGDFIS LNLARGHLQF RFNLGSGIAN LTTKETVNIG KWHWARIFRD GREGILQLDN
     SSIVRGYSGT PLTELNLELP FYIGSLSEWD EVHRLSGASK GYKGVIQRIL LNGKPLPISA
     KLPDCSFDSN RNGCAFNVGS YDGLPCPISK NPCLNNGLCV PELDQFICKC PSNTKGKYCE
     ISQEETPAIK FNGATFLQFR NRGYRSHNLT ISDEYPDNEE DDIDNIEEDV VDNNTYDAYD
     DEEYYFDFYD TARRKPERGN RYEIKLRTFA SDALLLWRSK SRSIREDYFS IAVVNGYPEI
     SYNLGKQDVF WAIRSKTKID DGKWHTIQVR RRKRVGFISI DGEPPIKGLS KYGAISLRTN
     SKLWIGGTAN LPQGLPSAYY KGFEGCIQHI LVNAKPLDMV SNNELNKVNF CHDNEI
//
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