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Database: UniProt
Entry: A0A139WBJ4_TRICA
LinkDB: A0A139WBJ4_TRICA
Original site: A0A139WBJ4_TRICA 
ID   A0A139WBJ4_TRICA        Unreviewed;      1227 AA.
AC   A0A139WBJ4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   18-SEP-2019, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYB25294.1};
GN   ORFNames=TcasGA2_TC034399 {ECO:0000313|EMBL:KYB25294.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga;
OC   Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB25294.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB25294.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB25294.1,
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.,
RA   Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M.,
RA   Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D.,
RA   Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J.,
RA   Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M.,
RA   Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T.,
RA   Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M.,
RA   Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C.,
RA   Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V.,
RA   Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J.,
RA   Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E.,
RA   Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y.,
RA   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.,
RA   Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H.,
RA   Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z.,
RA   Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E.,
RA   Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P.,
RA   Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y.,
RA   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.,
RA   Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F.,
RA   Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E.,
RA   Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M.,
RA   Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R.,
RA   Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S.,
RA   Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R.,
RA   Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y.,
RA   Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A.,
RA   Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G.,
RA   Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W.,
RA   Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z.,
RA   Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J.,
RA   Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A.,
RA   Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J.,
RA   Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y.,
RA   Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P.,
RA   Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S.,
RA   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:KYB25294.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB25294.1,
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
RT   information for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00553472}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KQ971372; KYB25294.1; -; Genomic_DNA.
DR   EnsemblMetazoa; TC034399_001; TC034399_001; TC034399.
DR   Proteomes; UP000007266; Linkage group 9.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR013818; Lipase/vitellogenin.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   InterPro; IPR000734; TAG_lipase.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007266};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Secreted {ECO:0000256|SAAS:SAAS00288740};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1155   1177       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      559    763       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      769    857       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN     1011   1048       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      108    128       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   DISULFID    829    849       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID   1038   1047       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1227 AA;  136310 MW;  12F3EA55E6E2AE1F CRC64;
     MNHSGSKKAR PYNAVQFWTQ SVICSPDWVY QTQKAQSGKS PLMMEDAITS NIVVIIKFAL
     GEVERLLREY TQNQEMVRNI GSHYYQIIYP VQLRQHKKMG ISTREIGSSK RGQVDGGYQG
     RGRPAKTGKH FHRTSLLLKA FNHKFRLDLE LNTTSFAIFL IKLRFLQATH RTEHHAETFS
     SQWSRTGFEA ENPNFYELIQ LDQSNIEQNL HDNARTVLLI HGWSENRTAD WFEDLKNAFL
     SRTDVVYNVI HVDYNKVASE LYPIAVKKSV AVGNQIGKFI LAMLKAVSLS NIEICGHSLG
     GQIAGYAGQY VLRKTGYRLP RITALDPAGP LFEGIFNINR KHLDRNDAEV VFVIHSDRGK
     FGYSYACGTV DVFPNNGVAI QPGCPDFGQN DILFCSHHMS YRFYIQAVAQ PQSLFAIQCK
     NYESFQKKDC EQSRIIDLGG EINPVDRGTC ILYTKQEEED IEHCYYHGTV QDYPGASAAF
     HTCNGVSGVI HLGNETFVIH PFYGGDLSKH PHVIFEARTN ANKGCANSGN MEWRLNTHAG
     FLPTSSNMRI KRDVREATKY IETAIVIDKA MFEKRNGSTR TDVVHDSIQI ANIADLYFRT
     LNTRVSVVYI ETWQGGNQAQ INRNEDIGRA LTNFNDYTSR KLFKIDKDTT QLLTGEVFVG
     GEAGMAVPAT VCTPKAVGIS VDINTYEPHL LAGTMAHMIG HNIGMGHDDG RNECHCRDWH
     GCIMAQAIIG QHNIQPYKFS ECSRSDYIDR LRTGNGICLL NKPNELEVRR TCGNRIVEDG
     EDCDCGTIDE CPSVDPCCDP ITCKLTTEAQ CASGPCCDNC MLKQRGVVCR EPSNECDLPE
     YCSGDSGECP VDVFKKNGHL CGYKGYCFNG VCPTLALQCQ SIWGYGGTAA DDQCFEKFNS
     KGSINGHCGS VGSNTFVKCA PENVKCGTLH CQKGKRQPLI GSGADQPPFS RTFITIQGTE
     YECKSIYRSS SGGSDDGESH RTVGLVLDGT PCGDNLICLN QTCTSIFPYI DQTKCPTNNP
     NLECSGHGFC TNLNKCYCEL GWGGPDCSLQ VEVAVLPMST RAPDTTAIDL TKSMQKKETP
     YGMYAVLSKR FDQQQSGKKT YYNQAGVSST PSIPRCRTSL SSLLVYKHRA HDGRFRNGVS
     FAGNNNSDNL ETLTMVFILV GVVKGVFICF AVVAVCYRKT TVRKYEKPYK KPIPKNYIHT
     AGNHSQEDSL DNANKILTLG GGVATFG
//
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