CHI10_DROME
ID CHI10_DROME Reviewed; 2286 AA.
AC Q9W5U2; O17420; O17422; Q7PL80; Q8MS85; Q9W5U3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable chitinase 10 {ECO:0000312|FlyBase:FBgn0250907};
DE EC=3.2.1.14;
DE AltName: Full=Probable chitinase 1;
DE AltName: Full=Probable chitinase 3 {ECO:0000312|FlyBase:FBgn0250907};
DE Flags: Precursor;
GN Name=Cht10 {ECO:0000312|FlyBase:FBgn0250907};
GN Synonyms=Cht1 {ECO:0000312|FlyBase:FBgn0250907},
GN Cht3 {ECO:0000312|FlyBase:FBgn0250907};
GN ORFNames=CG18140 {ECO:0000312|FlyBase:FBgn0250907};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 974-1086 AND 1418-1530.
RC STRAIN=Canton-S {ECO:0000269|PubMed:9662472};
RX PubMed=9662472; DOI=10.1111/j.1365-2583.1998.00065.x;
RA de la Vega H., Specht C.A., Liu Y., Robbins P.W.;
RT "Chitinases are a multi-gene family in Aedes, Anopheles and Drosophila.";
RL Insect Mol. Biol. 7:233-239(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1567-2286.
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014134; EAA46011.1; -; Genomic_DNA.
DR EMBL; BT021372; AAX33520.1; -; mRNA.
DR EMBL; AF026500; AAB81858.1; -; Genomic_DNA.
DR EMBL; AF026502; AAB81860.1; -; Genomic_DNA.
DR EMBL; AY119021; AAM50881.1; ALT_INIT; mRNA.
DR RefSeq; NP_001036422.1; NM_001042957.2.
DR RefSeq; NP_001260697.1; NM_001273768.1.
DR RefSeq; NP_001260698.1; NM_001273769.1.
DR AlphaFoldDB; Q9W5U2; -.
DR SMR; Q9W5U2; -.
DR BioGRID; 78241; 2.
DR DIP; DIP-19404N; -.
DR STRING; 7227.FBpp0110419; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; Q9W5U2; -.
DR DNASU; 3355116; -.
DR EnsemblMetazoa; FBtr0111127; FBpp0110419; FBgn0250907.
DR EnsemblMetazoa; FBtr0331165; FBpp0303592; FBgn0250907.
DR EnsemblMetazoa; FBtr0331166; FBpp0303593; FBgn0250907.
DR GeneID; 3355116; -.
DR KEGG; dme:Dmel_CG18140; -.
DR UCSC; CG18140-RA; d. melanogaster.
DR CTD; 3355116; -.
DR FlyBase; FBgn0250907; Cht10.
DR VEuPathDB; VectorBase:FBgn0250907; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000175593; -.
DR HOGENOM; CLU_228329_0_0_1; -.
DR InParanoid; Q9W5U2; -.
DR OMA; IAMGGWT; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q9W5U2; -.
DR BioGRID-ORCS; 3355116; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3355116; -.
DR PRO; PR:Q9W5U2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0250907; Expressed in eye disc (Drosophila) and 35 other tissues.
DR ExpressionAtlas; Q9W5U2; baseline and differential.
DR Genevisible; Q9W5U2; DM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 4.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01607; CBM_14; 4.
DR Pfam; PF00704; Glyco_hydro_18; 4.
DR SMART; SM00494; ChtBD2; 4.
DR SMART; SM00636; Glyco_18; 4.
DR SUPFAM; SSF51445; SSF51445; 4.
DR SUPFAM; SSF54556; SSF54556; 4.
DR SUPFAM; SSF57625; SSF57625; 4.
DR PROSITE; PS50940; CHIT_BIND_II; 4.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 4.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2286
FT /note="Probable chitinase 10"
FT /id="PRO_0000077051"
FT DOMAIN 219..589
FT /note="GH18 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 689..744
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 797..850
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 866..920
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 965..1334
FT /note="GH18 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 1409..1777
FT /note="GH18 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 1826..1878
FT /note="Chitin-binding type-2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 1908..2277
FT /note="GH18 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 592..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1087
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 1531
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 2030
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 266
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 294..297
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 339
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 408..411
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 560
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1018..1019
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1043..1046
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1088
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1155..1158
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1305
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1462..1463
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1487..1490
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1532
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1599..1602
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 1748
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 223..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 721..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 827..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 897..910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 969..994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 1413..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 1857..1868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 1912..1937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 2286 AA; 258777 MW; B4FC42CE4719F12A CRC64;
MHPYVPSVLV VVVLAISVKA HIRVDKLQIH SESNYKPAFI RSAVESIPLD IDAILLLRNS
TKPEFGDAFL PLRSAVESIP KLYQSNTSRF RKNPDVRSFV RDSVESLPND EDGLEHIEIF
TKYYNSVSDV AGVDLKSKKL THVNLDPGTI SDKYAAFIAR GNSEDYYPKS YRAGSPHQEL
LKMMNIEHTD KLDRYSDLQH QQSYGALGLA NRNDLKMTKK VLCYMSNWAF YRSGEAHFVP
EQIDPNLCSA IIYSFASLDP DHLTIREFDS WVDLDNQYYR RVTSLGVPVL IALGGWTDSS
GSKYSRLVSD NLKRRVFISS VSSFLLRHGF SGLHLDWNYP KCWQSDCSRG PVTDRPNLTK
LLRELRTEFQ SVDPKFQLGV AISGYKEIIK EAYDFPALSD IVDYMTVMTY DYHGAWEQKT
GHVSPLYGLS SDTYPQYNTN YTMQLLLKMG ARREKLVLSI PFYGQSFTLA TAHQILAGPG
VAASGPGDAG ELTKQPGMLA YYEICQRLTK FNWISDRNLN VIFGPFAMLN DQWVGYEDPT
SAQAKARYAA NNNFAGVAAW TIDLDDFRNL CCNESYPLLR AINRALGRLD SEPPTQPNCK
RPTLLATPVP PQMTTISSDG SGGLGQNHDH TTSLPSGQIS SSPVSTTITS TFPWWSSTTK
RPREPTKTTA QPTHTTILIP AGINPVVQPS NCKSGEFFAD SNNCNAYYHC FFAGELQQQF
CPSGLHWNNE AKGCDWPSSA QCSLKLDQHL STSYPNPIQT SKKPETTLKP NKKPSEISTH
HQVNSTSSRP QYMRPTILEC TEGDYYPHRN CRKYYICVNK ALVPSECGGD LHWDGIKKLC
DWPENVQCVT SKKYLKIIKS SSANEEDPCK GEKRVPYPGN CSKYLFCLWN RLQASDCPPG
LHYNERIGNC DWPAAAKCNP KGSESSEEAE LNAMPKPPTP QTPSSHLRPT YPTEKPVPKP
RDSHYKVICY FTNWAWYRKG IGRFTPDDIN TELCTHVIYG FAVLDYSELV LRTHDSWADV
ENNFYTRVTS LKSKGIKVSL ALGGWNDSQG DKYSRLVRSP MARSRFVRHA LEFIEKYGFE
GLDLDWEYPV CWQTECNKGS TEEKDGFTAW VQELSEAFRP RGLMLSTAVS PSRKIIDAGY
DIPQLSRYFD WIAVMTYDFH GHWDKKTGHV APLYHHPDDD FEYFNVNYSI NYWMEKGAPS
QKLVMGIPLY GQSFTLENTN SSGLNAKAPA PGEAGEFTRA AGFLAYYEIC ERVNRQGWQV
VHDEFGRMGP YAYKGTQWVS YDSPDMVRKK SLLVRSLKLG GGMVWALDLD DFKNRCGNGV
HPLLTEIHNV LKDPPSLMEI PGPIETTPTE YPGMEEEIHE SNGEGPEVQP IEAVMQTCEN
EGEEHEGILD PNHVLEEENI EATEMATEFK IICYFTNWAW YRQGGGKFLP EDIDSDLCTH
IIYGFAVLSR DNLTIQPHDS WADLDNKFYE RIVAYRKKGA KVTVAIGGWN DSAGDKYSRL
VRNPEARSRF IRNVLDFIEE YNFDGLDLDW EYPVCWQVDC KKGTAEEKIG FSALVRELFY
AFQPRGLILS AAVSPNKKVI DAGYEVAELS HYFSWISVMA YDYHGQWDKK TGHVAPMYSH
PEGTANFNAN FSMNYWISMG ADRRKLVMGI PLYGQSFSLA ETTKHQLNAP TYGGGEAGEA
TRARGFLAYY EICLKIRHHR WNVVRDTKGR IGPFAYHGDQ WVSFDDVPMI RHKSEYIKAM
GLGGAMIWAL DLDDFKNVCE CESYPLLKAI NRVLRGFGGP QPKCLLENPK STMKPNIKPP
FRPTINAPSG PNLDSPTQNV SLNVLSIKCH SKNYLAHEWD CTKYYICEHG TYVERSCPLG
LQWNKTYCDW PTNVQSSLGS NQRTQEPAVH RPNPTSVITE PPIINNSYKV VCYFTSWAWY
RSSQGKFVPE DIDANLCTHL IYGFAVLDSK SLTIKTHDSW TDIDNRFYER VVEYKQRGLR
VMLAIGGWND SLGSKYARLV LNSQSRRRFV ASVISFLEQH GFEGLDLAWE FPVCWQVNCN
RGNPTEKDGF VALVKELSEA FKENGLILSA AVSPSKMVID AGYNVFELSP YFDWVAVMTY
DFHGHWDMRT GQIAPLFHRG GDENLYLNGN FSIHYWLERG IPNDKLVMGM PMYGQTFTLA
DQNRRSLNDK TVGPGKAGTF TRADGFLAYY EICEKVVNDD WKVVRDEEGI FGSYAYSGNQ
WISYDDVTTI RRKSQFIKSL QLGGGMIWAL DLDDFRGLCG CGKHPLLRTL SQELLGIPGQ
KAKDCI
