LECB1_CRATA
ID LECB1_CRATA Reviewed; 165 AA.
AC U3KRG0; B8WI86;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 2.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Bark lectin isoform 1 {ECO:0000303|PubMed:22195573, ECO:0000303|PubMed:23823708};
DE Short=CrataBL {ECO:0000303|PubMed:23823708, ECO:0000312|PDB:4IHZ};
DE Short=CrataBL-form I {ECO:0000303|PubMed:22195573, ECO:0000303|PubMed:23823708};
OS Crateva tapia (Garlic-pear tree) (Crataeva tapia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Capparaceae; Crateva.
OX NCBI_TaxID=202635;
RN [1] {ECO:0000305, ECO:0000312|PDB:4IHZ}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-27 AND ASN-57,
RP DISULFIDE BONDS, AND X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RC TISSUE=Bark {ECO:0000269|PubMed:23823708};
RX PubMed=23823708; DOI=10.1371/journal.pone.0064426;
RA Ferreira R.D., Zhou D., Ferreira J.G., Silva M.C., Silva-Lucca R.A.,
RA Mentele R., Paredes-Gamero E.J., Bertolin T.C., Dos Santos Correia M.T.,
RA Paiva P.M., Gustchina A., Wlodawer A., Oliva M.L.;
RT "Crystal structure of Crataeva tapia bark protein (CrataBL) and its effect
RT in human prostate cancer cell lines.";
RL PLoS ONE 8:E64426-E64426(2013).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-19, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP GLYCOSYLATION, AND TOXIC DOSE.
RC TISSUE=Bark {ECO:0000269|PubMed:22195573};
RX PubMed=22195573; DOI=10.1016/j.plantsci.2011.10.018;
RA Araujo R.M., Ferreira R.S., Napoleao T.H., Carneiro-da-Cunha M.,
RA Coelho L.C., Correia M.T., Oliva M.L., Paiva P.M.;
RT "Crataeva tapia bark lectin is an affinity adsorbent and insecticidal
RT agent.";
RL Plant Sci. 183:20-26(2012).
CC -!- FUNCTION: Glucose and N-acetylglucosamine binding lectin. Has
CC hemagglutinating activity against human and rabbit erythrocytes which
CC does not require divalent cations. Inhibits factor Xa and, to a lesser
CC extent, trypsin. Does not inhibit neutrophil elastase, human plasma
CC kallikrein, papain, human plasmin, porcine pancreatic kallikrein and
CC bovin chymotrypsin. Has insecticidal activity against the termite
CC species N.corniger. Induces apoptosis in prostrate cancer cell lines
CC DU145 and PC3. {ECO:0000269|PubMed:22195573,
CC ECO:0000269|PubMed:23823708}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Hemagglutinating activity is stable between 30 and 60 degrees
CC Celsius. {ECO:0000269|PubMed:22195573};
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:22195573,
CC ECO:0000269|PubMed:23823708}.
CC -!- TOXIC DOSE: LD(50) is 0.45 mg/ml against the termite species
CC N.corniger. {ECO:0000269|PubMed:22195573}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000255}.
CC -!- CAUTION: Characterization did not differentiate between the two
CC isoforms determined by protein sequencing (PubMed:22195573,
CC PubMed:23823708). {ECO:0000305, ECO:0000305|PubMed:22195573,
CC ECO:0000305|PubMed:23823708}.
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DR PDB; 4IHZ; X-ray; 1.50 A; A/B=1-165.
DR PDB; 4II0; X-ray; 1.75 A; A/B=1-165.
DR PDBsum; 4IHZ; -.
DR PDBsum; 4II0; -.
DR AlphaFoldDB; U3KRG0; -.
DR SMR; U3KRG0; -.
DR iPTMnet; U3KRG0; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemagglutinin; Lectin; Protease inhibitor; Serine protease inhibitor;
KW Toxin.
FT CHAIN 1..165
FT /note="Bark lectin isoform 1"
FT /id="PRO_0000430494"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23823708"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23823708"
FT DISULFID 33..80
FT /evidence="ECO:0000269|PubMed:23823708"
FT DISULFID 126..133
FT /evidence="ECO:0000269|PubMed:23823708"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4IHZ"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4IHZ"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4IHZ"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4IHZ"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4IHZ"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:4II0"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4IHZ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4IHZ"
SQ SEQUENCE 165 AA; 18261 MW; A08DB1A5AD62A150 CRC64;
AILTGVPYYI LPSTSRAGFS PDNLRKNTSQ PSCPLDLITQ LRFPRRIGVP VIFTPQNSSL
KVVPLSHNLN IHTCSDLWFC PESKIWTVKS SSIHRGLVVT TGGTFRSLGS WFRIERHGDS
YKLVHCPRGS TPCRDVGIET VGGGGRRYLA PRDRPLAVRF TRASG
