ID   IPLAA_MORAL             Reviewed;          13 AA.
AC   P86799;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   07-OCT-2020, entry version 16.
DE   RecName: Full=Insecticidal protein LA-a {ECO:0000303|PubMed:20109180};
DE            EC=3.2.1.132;
DE            EC=3.2.1.14;
DE   AltName: Full=Latex abundant protein a {ECO:0000303|PubMed:20109180};
DE   Flags: Fragment;
OS   Morus alba (White mulberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Morus.
OX   NCBI_TaxID=3498;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   GLYCOSYLATION.
RC   STRAIN=cv. Minamisakari {ECO:0000269|PubMed:20109180};
RC   TISSUE=Latex {ECO:0000269|PubMed:20109180};
RX   PubMed=20109180; DOI=10.1186/1471-2091-11-6;
RA   Kitajima S., Kamei K., Taketani S., Yamaguchi M., Kawai F., Komatsu A.,
RA   Inukai Y.;
RT   "Two chitinase-like proteins abundantly accumulated in latex of mulberry
RT   show insecticidal activity.";
RL   BMC Biochem. 11:6-6(2010).
RN   [2]
RP   SEQUENCE REVISION TO 1.
RA   Kitajima S.;
RL   Submitted (AUG-2011) to UniProtKB.
CC   -!- FUNCTION: Has insecticidal activity when consumed by D.melanogaster
CC       larvae. Has low chitinase and chitosanase activity.
CC       {ECO:0000269|PubMed:20109180}.
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         Evidence={ECO:0000269|PubMed:20109180};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC         Evidence={ECO:0000269|PubMed:20109180};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20109180}.
CC   -!- PTM: Glycosylated; contains galactose. {ECO:0000269|PubMed:20109180}.
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DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR   GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR   GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Plant defense; Polysaccharide degradation; Secreted.
FT   CHAIN           1..>13
FT                   /note="Insecticidal protein LA-a"
FT                   /id="PRO_0000401099"
FT   DOMAIN          3..>13
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   NON_TER         13
FT                   /evidence="ECO:0000303|PubMed:20109180"
SQ   SEQUENCE   13 AA;  1269 MW;  3351C83D2A05B408 CRC64;
     SEPQXGRDAG GAL