ID   MLX56_MORAL             Reviewed;         415 AA.
AC   A7XQ02;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Mulatexin {ECO:0000303|PubMed:19476960};
DE            Short=MLX56 {ECO:0000303|PubMed:19476960};
DE   AltName: Full=Latex protein {ECO:0000312|EMBL:ABS86614.2};
DE   Flags: Precursor;
OS   Morus alba (White mulberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=3498;
RN   [1] {ECO:0000312|EMBL:ABS86614.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-30, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   STRAIN=cv. Shin-ichinose {ECO:0000269|PubMed:19476960};
RC   TISSUE=Latex {ECO:0000269|PubMed:19476960};
RX   PubMed=19476960; DOI=10.1016/j.phytochem.2009.04.014;
RA   Wasano N., Konno K., Nakamura M., Hirayama C., Hattori M., Tateishi K.;
RT   "A unique latex protein, MLX56, defends mulberry trees from insects.";
RL   Phytochemistry 70:880-888(2009).
CC   -!- FUNCTION: Chitin-binding protein which slows larval growth when
CC       consumed by the lepidopteran species S.ricini and M.brassica, but not
CC       when consumed by the mulberry specialist B.mori. Lacks chitinase
CC       activity. {ECO:0000269|PubMed:19476960}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19476960}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:19476960}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined MW of this protein is: 56
CC       kDa. {ECO:0000269|PubMed:19476960}.
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DR   EMBL; EF535852; ABS86614.2; -; mRNA.
DR   AlphaFoldDB; A7XQ02; -.
DR   SMR; A7XQ02; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd00035; ChtBD1; 1.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 2.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR22595:SF79; BASIC ENDOCHITINASE B; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   Pfam; PF00187; Chitin_bind_1; 2.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00270; ChtBD1; 2.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 2.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   1: Evidence at protein level;
KW   Chitin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Plant defense; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:19476960"
FT   CHAIN           22..415
FT                   /note="Mulatexin"
FT                   /evidence="ECO:0000269|PubMed:19476960"
FT                   /id="PRO_0000401103"
FT   DOMAIN          23..66
FT                   /note="Chitin-binding type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DOMAIN          125..167
FT                   /note="Chitin-binding type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          65..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..122
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..41
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..47
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        60..64
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        128..143
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        137..149
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        142..156
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        161..165
FT                   /evidence="ECO:0000250|UniProtKB:P11218,
FT                   ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   415 AA;  45148 MW;  3555EA15320D6457 CRC64;
     MKFRTLLIIF SLVFLLEIVS ASEPQCGRDA GGALCHGNLC CSHWGFCGTT AIYCDVDQGC
     QSQCWSSPPP PSPPPPPPSP PPPSPPPPSP PPPSPPPPSP PPPSPPPPSP PPPSPPPPGG
     PERPDHRCGR ALGNPPCNPG RCCSIHNWCG STAAYCRGSS CQYQCWNSLL SALISNGNNA
     ISKIISKSVF DEMFKHMKDC PSKGFYSYDA FIIATTSFPH FGTTGDITTR KRELAAFFAQ
     TSLATTGQRF DSQDLYVWGY CHINETTNGN DNDYCTSAHW PCPSGKKYNS RGAVQLTHNY
     NYGLAGEALG LDLINNPDLV ATDPVISFKT AIWFWMAQHD NKLSCHDILI NANSGYVIGN
     IIKNSGYQNG LITNTISTMR GIGYYKRYCD MLGVSYGDNL DSWYDQTHFS EVARM
//