GenomeNet

Database: UniProt
Entry: D6WKS5_TRICA
LinkDB: D6WKS5_TRICA
Original site: D6WKS5_TRICA 
ID   D6WKS5_TRICA            Unreviewed;      1499 AA.
AC   D6WKS5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Protein eyes shut homolog-like Protein {ECO:0000313|EMBL:EFA03035.1};
GN   Name=AUGUSTUS-3.0.2_10461 {ECO:0000313|EMBL:EFA03035.1};
GN   ORFNames=TcasGA2_TC010461 {ECO:0000313|EMBL:EFA03035.1};
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:EFA03035.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA03035.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03035.1,
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:EFA03035.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03035.1,
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; KQ971342; EFA03035.1; -; Genomic_DNA.
DR   RefSeq; XP_008200500.1; XM_008202278.2.
DR   STRING; 7070.D6WKS5; -.
DR   EnsemblMetazoa; TC010461_001; TC010461_001; TC010461.
DR   GeneID; 662068; -.
DR   KEGG; tca:662068; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3509; Eukaryota.
DR   HOGENOM; CLU_002251_0_0_1; -.
DR   InParanoid; D6WKS5; -.
DR   OMA; ECHRNEC; -.
DR   OrthoDB; 101939at2759; -.
DR   PhylomeDB; D6WKS5; -.
DR   Proteomes; UP000007266; Linkage group 5.
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:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 9.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.200; -; 4.
DR   Gene3D; 2.10.25.10; Laminin; 13.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR001791; Laminin_G.
DR   PANTHER; PTHR24044:SF420; NEUROGENIC LOCUS PROTEIN DELTA; 1.
DR   PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR   Pfam; PF00008; EGF; 6.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 3.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00179; EGF_CA; 12.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 10.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 13.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 13.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
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}; Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1499
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003089874"
FT   DOMAIN          27..63
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          65..101
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          103..139
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          141..181
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          183..219
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          221..257
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          259..296
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          491..528
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          535..712
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          708..741
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          744..781
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          791..975
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          976..1012
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1014..1052
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1058..1242
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1238..1275
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1313..1496
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        31..41
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        53..62
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        91..100
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        129..138
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        171..180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        209..218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        247..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        286..295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        518..527
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        771..780
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1002..1011
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1042..1051
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1265..1274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1499 AA;  163954 MW;  372743BC7D53087E CRC64;
     MPSVGSAGRS LFLLLAPFFL LPLESSAGLA CLSNPCVHGV CLDDLNSTYF CYCIDGYTGI
     QCQKNWNECW SSPCKNGGIC IDGVASFNCS CPPGFVGELC EEDFNECESN PCLNNGTCLD
     AANGYFCSCL PGYSGVHCEV DVAVCNATNE TRCANGGICV EGPGDSFSCK CQPGWEGLLC
     EGEVDECMSA PCQNGAVCVD LMADYSCACL FGFSGRNCED TVKICDVNPC ANGALCLKED
     RQPVCYCVPD FHGDLCQFQY DECQLGPKCM NGGTCVDGID NSTCSCPPNL TGVQCECLIL
     DNGGLDCTYT SPQTVPPIRT STIFHPTTTE TEVPNTTTVQ PFSTTIAWTT TEVVPPTTTY
     TQTQSTTELT ETILVYSTTP KVTEMSVVTT ETEPTTETTY STVTTTEIYT EPVFTTTTGK
     IITTMLSTET SSFPPVTTFL PMTSTPKQES NFSLPDETTT SFFTKKPETT TALTAFFTET
     TTKLLTDTTV VPFDCTKTHC QNGGTCVYKS ELGYQCLCPF HTEGDFCELK MGVQKAAFTG
     QSYLKHRLPD STNISIELDA KTLSSKGLLF YSNTDSTYMV LYIENGHLKF KFSCGYQTML
     LSELKVPVNN GDLMKIKAKL EFSKDLKRCD ASIKVNDSLS MTGDQLALKR RFSKPSGWLY
     LGGVPEEIAN INLPESGFVG CMLRLKISQK FLDIFNDAED GYGVTECSSL ACLSNPCSNG
     ATCYSHGEKW TCHCKNGFLG KMCEKSVCDT NPCLFGGTCI QFSGSGYICL CPFGKHGHFC
     ENDLKITEPN FASTIRGLSS YVAYPIPGGI SENMEIRFRF LPTVMDQISL LMFMGQKGHH
     NYYSDHMAVS FVKGYIMLTW NLGSGPRRIF TPQPIDEGAK NYQVRVGRSG RRAWLDVENL
     GNVTGRSPGN LIQLDVSPVL YLGGHDSLNF STLPHDLPLH TGFSGCIFDV ELITGNLVIP
     LQGSRQTIGR GVGQCGTTEC YEQSCQNGGI CLHHASTFMC LCQDGWFGPL CTFRRNPCDS
     DYHKCEAGAT CVPVISDYEC DCPIGKSGKF CEKDEDITDV NFTGLRSFLS LPPTEFSENH
     FNIEMEIRPL GDNGLLFFIE KPGSSFISLT LSSGSLELRI LSYKNKAAPN EPTTIRSTKI
     LIKGIWYKIQ LGIFGKKAYL SVDNIINSAV LSTENGINMS KENIFIGGHP DISTLPLLAV
     SKLPVPYKGC IRAFSANGVH IPLNKMSILS GRNINDCDGT PCGKDACLNG GTCWLDSFMK
     PHCSCPPAFY GNKCQSVSEC DTAKCKTTGV CVGPKCSCHL GWEGVYCERQ IKVTTPEFTG
     RSYLIVKKNN EKKRNTPGVE VKTLYLNFTT VKKDGLVLWS RKENSFVGMG LENGFLKIAY
     SVDNRTGTNL VTLPLSYKIS DGLWHNIELS FAPFLIKLDQ NKIVYNGKNK KMLENSTMST
     DGLFYIGGIP TKTTIKKETN GTFLDTFEGC IEGFATNGEQ VIRDFTPFEG RDVNVCRVV
//
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