CHIT2_DROME
ID CHIT2_DROME Reviewed; 484 AA.
AC Q9W092; O17421;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable chitinase 2;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=Cht2 {ECO:0000312|EMBL:AAL13818.1, ECO:0000312|FlyBase:FBgn0022702};
GN ORFNames=CG2054;
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] {ECO:0000305, ECO:0000312|EMBL:AAF47562.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF47562.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAL13818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAB81859.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-167.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAB81859.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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:0000303|PubMed:9662472}.
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DR EMBL; AE014296; AAF47562.1; -; Genomic_DNA.
DR EMBL; AY058589; AAL13818.1; -; mRNA.
DR EMBL; AF026501; AAB81859.1; -; Genomic_DNA.
DR RefSeq; NP_001246550.1; NM_001259621.2.
DR RefSeq; NP_001261282.1; NM_001274353.1.
DR RefSeq; NP_477298.2; NM_057950.4.
DR AlphaFoldDB; Q9W092; -.
DR SMR; Q9W092; -.
DR BioGRID; 63756; 1.
DR IntAct; Q9W092; 1.
DR STRING; 7227.FBpp0297108; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q9W092; -.
DR PaxDb; Q9W092; -.
DR PRIDE; Q9W092; -.
DR DNASU; 38223; -.
DR EnsemblMetazoa; FBtr0072795; FBpp0072677; FBgn0022702.
DR EnsemblMetazoa; FBtr0305966; FBpp0297108; FBgn0022702.
DR EnsemblMetazoa; FBtr0334075; FBpp0306200; FBgn0022702.
DR GeneID; 38223; -.
DR KEGG; dme:Dmel_CG2054; -.
DR CTD; 38223; -.
DR FlyBase; FBgn0022702; Cht2.
DR VEuPathDB; VectorBase:FBgn0022702; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_3_0_1; -.
DR InParanoid; Q9W092; -.
DR OMA; WQDLKEE; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q9W092; -.
DR BioGRID-ORCS; 38223; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38223; -.
DR PRO; PR:Q9W092; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0022702; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9W092; baseline and differential.
DR Genevisible; Q9W092; DM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
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:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IMP:FlyBase.
DR GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
DR GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR Gene3D; 3.10.50.10; -; 1.
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; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW Hydrolase; Phosphoprotein; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..484
FT /note="Probable chitinase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000011948"
FT DOMAIN 41..432
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 98..99
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 125..128
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 169
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 231..234
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 384
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT DISULFID 45..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 484 AA; 54122 MW; A2B77899332452D4 CRC64;
MTLRSRLSGE APQLWLLLLL ASTASSLWAS VAARTGPLHD KVVVCYVSTW AVYRPEQGAY
AIENFDPNLC THVVYAFAGL DITQAAIKSL DPWQDLKEEY GKGGYEKMTG LKRSHPHLKV
SLAIGGWNEG SANYSTLVAN NLLRGRFVKQ VSSFIRKYNF DGLDLDWEYP TQRKGKPADR
ENFVLLTKEL REEFDEHGLL LTSAIGASKK VIDEAYDVRQ ISRYLDYLHI MCYDYHGSWD
RRVGYNAPLT APADDPLSVK FSIDYLLKLG APPEKLVMGL PFYGRTFKTL ASGFLNDVSE
GVGFKGPYTR EDGFLGYNEI CQTLSNQTSG WTREWDPQTS QVLAKSERNV FTQEINVVTY
DSSRSIANKV LFAMSKRLAG VMVWSVDTDD FLGNCKLDED TYEDFQKVTA APKRSSQNYP
LLRTINEATM LAVDELAVPE PQPDDSENEI PHGSIADRKN AGASMVSLGL GVTAVFMLLH
RLAQ
