CBP2_MOROL
ID CBP2_MOROL Reviewed; 104 AA.
AC C0HKC5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Chitin-binding protein 2 {ECO:0000303|PubMed:28634471};
DE Short=Mo-CBP2 {ECO:0000303|PubMed:28634471};
DE Flags: Fragments;
OS Moringa oleifera (Horseradish tree) (Moringa pterygosperma).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Moringaceae; Moringa.
OX NCBI_TaxID=3735 {ECO:0000303|PubMed:28634471};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:28634471};
RX PubMed=28634471; DOI=10.3389/fmicb.2017.00980;
RA Neto J.X.S., Pereira M.L., Oliveira J.T.A., Rocha-Bezerra L.C.B.,
RA Lopes T.D.P., Costa H.P.S., Sousa D.O.B., Rocha B.A.M., Grangeiro T.B.,
RA Freire J.E.C., Monteiro-Moreira A.C.O., Lobo M.D.P., Brilhante R.S.N.,
RA Vasconcelos I.M.;
RT "A Chitin-binding Protein Purified from Moringa oleifera Seeds Presents
RT Anticandidal Activity by Increasing Cell Membrane Permeability and Reactive
RT Oxygen Species Production.";
RL Front. Microbiol. 8:980-980(2017).
CC -!- FUNCTION: Chitin-binding protein. Has antifungal activity against
CC C.krusei, C.albicans, C.tropicalis and C.parapsilosis. Inhibits
CC C.albicans by increasing cell membrane permeability and production of
CC reactive oxygen species. Has no hemagglutinating activity.
CC {ECO:0000269|PubMed:28634471}.
CC -!- SUBUNIT: Oligomer in an unreduced state. {ECO:0000269|PubMed:28634471}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:28634471}.
CC -!- MASS SPECTROMETRY: Mass=13309; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:28634471};
CC -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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DR AlphaFoldDB; C0HKC5; -.
DR SMR; C0HKC5; -.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:UniProtKB.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Chitin-binding; Direct protein sequencing; Fungicide;
KW Glycoprotein.
FT CHAIN 1..104
FT /note="Chitin-binding protein 2"
FT /evidence="ECO:0000269|PubMed:28634471"
FT /id="PRO_0000439085"
FT NON_CONS 6..7
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 11..12
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 17..18
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 36..37
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 44..45
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 55..56
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 75..76
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_CONS 81..82
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:28634471"
FT NON_TER 104
FT /evidence="ECO:0000303|PubMed:28634471"
SQ SEQUENCE 104 AA; 11789 MW; DE168A771817742A CRC64;
QPDFQRCPSL RCCQQLRQAV QLTHQQQGQV GPQQVRQQFQ THQRIPAICN LQPMRQAVQL
AHQQQQGQVG PQQVRCCQQL RQAVQSQAAA AGQVGPQQVG HMYR
