ID A7U8C9_TRICA Unreviewed; 534 AA.
AC A7U8C9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Chitin deacetylase 1 {ECO:0000313|EMBL:ABU25223.1};
DE EC=3.5.1.41 {ECO:0000313|EMBL:ABU25223.1};
GN Name=AUGUSTUS-3.0.2_14100 {ECO:0000313|EMBL:EFA03956.1};
GN ORFNames=TcasGA2_TC014100 {ECO:0000313|EMBL:EFA03956.1};
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:ABU25223.1};
RN [1] {ECO:0000313|EMBL:ABU25223.1}
RP NUCLEOTIDE SEQUENCE.
RA Arakane Y., Beeman R.W., Kramer K.J., Muthukrishnan S.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFA03956.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03956.1,
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 [3] {ECO:0000313|EMBL:EFA03956.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03956.1,
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).
RN [4] {ECO:0000313|EMBL:EFA03956.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03956.1};
RA Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT super scaffolding tool.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EU019711; ABU25223.1; -; mRNA.
DR EMBL; KQ971342; EFA03956.1; -; Genomic_DNA.
DR RefSeq; NP_001095946.1; NM_001102476.1.
DR AlphaFoldDB; A7U8C9; -.
DR SMR; A7U8C9; -.
DR STRING; 7070.A7U8C9; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR EnsemblMetazoa; TC014100_001; TC014100_001; TC014100.
DR GeneID; 657802; -.
DR KEGG; tca:657802; -.
DR CTD; 657802; -.
DR eggNOG; ENOG502QQP5; Eukaryota.
DR HOGENOM; CLU_022576_1_0_1; -.
DR InParanoid; A7U8C9; -.
DR OMA; FWSDATV; -.
DR OrthoDB; 4572257at2759; -.
DR BRENDA; 3.5.1.41; 6437.
DR Proteomes; UP000007266; Linkage group 5.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10974; CE4_CDA_like_1; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR45985; -; 1.
DR PANTHER; PTHR45985:SF6; FI03450P; 1.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000313|EMBL:ABU25223.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010103600"
FT DOMAIN 37..99
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DISULFID 117..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 124..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 136..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 534 AA; 60619 MW; 020C8F000B7FBB2A CRC64;
MALKQGALFI LAICACTVFA QQQAEETAPK KEDSFEVELC KDKDAGEWFR LVAGEGDNCR
DVIQCTSSGL QAIRCPAGLY FDIDKQTCDW KDSVKNCKLK NKERKVKPLL ITDEPLCPDG
SLACGDGNCI ERGLFCNGEK DCSDGSDENT CDIDNDPNRA PPCDPAVCVL PDCFCSEDGT
TIPGDLPSKD VPQMITITFD DAINNNNIEL YKEIFNGKRK NPNGCDIKAT FFVSHKYTNY
SAVQEMHRKG HEIAVHSITH NDDERFWSNA TVDDWAKEMA GMRIIAEKFA NLTDNSVVGV
RAPYLRVGGN NQFTMMEEQA FLYDSTITAP LSNPPLWPYT MYFRMPHRCH GNLQSCPTRS
HAVWEMVLNE LDRREDPTND EYLPGCAMVD SCSNILTGDQ FYNFLNHNFD RHYEENRAPL
GLYFHAAWLK NNPEFLDAFL YWVDEILANH NDVYFVTMTQ VIQWIQNPRT ITESKNFEPW
REKCVVEGNP HCWVPHSCKL TSKEVPGETI NLQTCVRCPN NYPWVNDPTG DGFF
//
