IDGFL_BOMMO
ID IDGFL_BOMMO Reviewed; 433 AA.
AC Q9GV28; P82223; P82224;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Chitinase-like protein EN03;
DE AltName: Full=Imaginal disk growth factor-like protein;
DE Flags: Precursor;
GN Name=EN03 {ECO:0000312|EMBL:BAB16695.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB16695.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Kinshu X Showa {ECO:0000269|PubMed:11222941};
RC TISSUE=Anterior silk gland {ECO:0000269|PubMed:11222941};
RX PubMed=11222941; DOI=10.1016/s0965-1748(00)00124-7;
RA Tsuzuki S., Iwami M., Sakurai S.;
RT "Ecdysteroid-inducible genes in the programmed cell death during insect
RT metamorphosis.";
RL Insect Biochem. Mol. Biol. 31:321-331(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 17-27.
RC STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC Fat body {ECO:0000269|PubMed:11280994};
RX PubMed=11280994;
RA Zhong B.-X.;
RT "Protein database for several tissues derived from five instar of
RT silkworm.";
RL Yi Chuan Xue Bao 28:217-224(2001).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Induced 2 to 4 hours after treatment with 20-hydroxyecdysone
CC (20E). Repressed by 8 hours after treatment with 20E, except in the
CC presence of cycloheximide. {ECO:0000269|PubMed:11222941}.
CC -!- MISCELLANEOUS: Lacks the typical Glu active site in position 152 that
CC is replaced by a Gln residue, preventing the hydrolase activity. Its
CC precise function remains unclear. {ECO:0000269|PubMed:11222941}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF
CC subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB041634; BAB16695.1; -; mRNA.
DR RefSeq; NP_001036847.1; NM_001043382.1.
DR STRING; 7091.BGIBMGA000648-TA; -.
DR PRIDE; Q9GV28; -.
DR GeneID; 692387; -.
DR KEGG; bmor:692387; -.
DR CTD; 100160032; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_3_2_1; -.
DR InParanoid; Q9GV28; -.
DR OrthoDB; 482694at2759; -.
DR BRENDA; 2.4.1.16; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02873; GH18_IDGF; 1.
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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR015520; IDGF.
DR PANTHER; PTHR11177:SF235; PTHR11177:SF235; 1.
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; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:11280994"
FT CHAIN 17..433
FT /note="Chitinase-like protein EN03"
FT /evidence="ECO:0000269|PubMed:11280994"
FT /id="PRO_0000274553"
FT DOMAIN 23..433
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 337..418
FT /evidence="ECO:0000250|UniProtKB:Q9V3D4"
SQ SEQUENCE 433 AA; 48144 MW; EB1406C67328A00B CRC64;
MKLFIALVGL LALAKALPAV THSKVLCYYD SRSYVRESQA RMLPLDLDPA LSFCTHLLYG
YAVIQPDTYK LVSLNENLDI DRTHDNYRAI TSLKAKYPGL TVLLSVGGDA DTEEPEKYNL
LLESQQARTA FINSGVLLAE QYGFDGIDLA WQFPRVKPKK IRSTWGSLWH GIKKTFGTTP
VDEKESEHRE GFTALVRELK QALIHKPKMQ LGVTVLPNVN STIYHDVPAI INLVDYVNVG
AYDYYTPTRN NKEADYTAPI YTPQNRNPLQ NADAAVTYWL TSGAPSQKIV LSXRLRSYLE
TGXDSEIAGV PPIHTDGPGE AGPYVKTEGL LSYPEVCGKL INPNQQKGMR PHLRKVTDPS
KRFGTYAFRL PDDNGEGGIW VSYEDPDTAG QKAAYVKSKN LGGVAIVDLS LDDFRGLCTG
DKYPILRAAK YRL