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Database: UniProt
Entry: D6WCY3_TRICA
LinkDB: D6WCY3_TRICA
Original site: D6WCY3_TRICA 
ID   D6WCY3_TRICA            Unreviewed;       550 AA.
AC   D6WCY3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Acyloxyacyl hydrolase-like Protein {ECO:0000313|EMBL:EEZ98824.2};
GN   Name=AUGUSTUS-3.0.2_04431 {ECO:0000313|EMBL:EEZ98824.2};
GN   ORFNames=TcasGA2_TC004431 {ECO:0000313|EMBL:EEZ98824.2};
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:EEZ98824.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EEZ98824.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ98824.2,
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:EEZ98824.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ98824.2,
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).
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DR   EMBL; KQ971311; EEZ98824.2; -; Genomic_DNA.
DR   RefSeq; XP_969018.2; XM_963925.3.
DR   AlphaFoldDB; D6WCY3; -.
DR   EnsemblMetazoa; TC004431_001; TC004431_001; TC004431.
DR   GeneID; 657467; -.
DR   KEGG; tca:657467; -.
DR   eggNOG; ENOG502QVQW; Eukaryota.
DR   HOGENOM; CLU_025769_0_0_1; -.
DR   OMA; PFCHLYP; -.
DR   OrthoDB; 4166at2759; -.
DR   Proteomes; UP000007266; Linkage group 2.
DR   GO; GO:0050528; F:acyloxyacyl hydrolase activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0009104; P:lipopolysaccharide catabolic process; IBA:GO_Central.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR   CDD; cd01826; acyloxyacyl_hydrolase_like; 1.
DR   Gene3D; 1.10.225.10; Saposin-like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR039676; AOAH.
DR   InterPro; IPR048593; AOAH_Saposin_N.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR15010; ACYLOXYACYL HYDROLASE; 1.
DR   PANTHER; PTHR15010:SF0; ACYLOXYACYL HYDROLASE; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   Pfam; PF20825; Saposin; 1.
DR   SMART; SM00741; SapB; 1.
DR   SUPFAM; SSF47862; Saposin; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS50015; SAP_B; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000313|EMBL:EEZ98824.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..550
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007310640"
FT   DOMAIN          24..102
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
SQ   SEQUENCE   550 AA;  63130 MW;  40CCEE5825916DF9 CRC64;
     MKTFQVFLFL LFCTSFTNAR GVNGGMSCAV CTVLTGVTMQ IAELHEEDLF NATKRLCNVL
     PNKIRHPCFR IVDKVEPYLT NLSEKITPDL FCLVYGTCRV DKGQPFCHLF PLTMEQEEME
     NVLKKEREKM LPKIDFCKLP YIKDICNILN NSYTSLAPVE DFDNDGFSAM ETGRGSDWRG
     RDCVDNDPQV YPGRRPLNSD YFSDSNCNGI WGTKNDTFLS LEQELCKKSQ PRGLIFIGDS
     IGAHFHMPEV WINPLLFSWP GLNGSSVILD EIDWPQFGFA TGFKNITRNI LIQGLTDSLY
     LRLRNRNRCN HRDYQNLSQN GASSYEGLNH VNSIARNRTT DNPALVIYAM QGNDVCNNFN
     DTINHMTSPE TFRRNVMKSL FLLDEKLPPQ SHVVLVELVE ADFIFPAMAE RLHPIGRLHK
     NVFYKNLYEW FNCMQIGPCT GWLNANQTLR DITSKRARKL STILKYIATN ETFKNFQVHY
     IQNPINYLVR NDKINITEFL EPVDSLHPNQ KAQVLLTETV WNFLEKLPVL GPVNPHNDEI
     IRIFGEQGGH
//
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