ID   LEC_DENFN               Reviewed;         167 AA.
AC   B2KNH9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Mannose-specific lectin;
DE   AltName: Full=Agglutinin {ECO:0000303|PubMed:18776994, ECO:0000303|PubMed:19495769, ECO:0000312|EMBL:ABU62812.1};
DE   Flags: Precursor;
GN   Name=dfa {ECO:0000312|EMBL:ABU62812.1};
OS   Dendrobium findlayanum (Findlay's orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=179355;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-26, FUNCTION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Pseudobulb {ECO:0000269|PubMed:19495769};
RX   PubMed=19495769; DOI=10.1007/s00299-009-0724-0;
RA   Sattayasai N., Sudmoon R., Nuchadomrong S., Chaveerach A., Kuehnle A.R.,
RA   Mudalige-Jayawickrama R.G., Bunyatratchata W.;
RT   "Dendrobium findleyanum agglutinin: production, localization, anti-fungal
RT   activity and gene characterization.";
RL   Plant Cell Rep. 28:1243-1252(2009).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Pseudobulb {ECO:0000269|PubMed:18776994};
RX   PubMed=18776994; DOI=10.1093/abbs/40.9.811;
RA   Sudmoon R., Sattayasai N., Bunyatratchata W., Chaveerach A.,
RA   Nuchadomrong S.;
RT   "Thermostable mannose-binding lectin from Dendrobium findleyanum with
RT   activities dependent on sulfhydryl content.";
RL   Acta Biochim. Biophys. Sin. 40:811-818(2008).
CC   -!- FUNCTION: Mannose-specific lectin. Shows agglutinating activity towards
CC       chicken erythrocytes. Has antifungal activity against A.alternata and
CC       Collectotrichum species. {ECO:0000269|PubMed:18776994,
CC       ECO:0000269|PubMed:19495769}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18776994}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P30617}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pseudobulb, with highest levels of
CC       expression in the non-swollen internode (at protein level).
CC       {ECO:0000269|PubMed:18776994, ECO:0000269|PubMed:19495769}.
CC   -!- DEVELOPMENTAL STAGE: Detected at low levels in very young and young
CC       stages, before increasing to high levels during the nearly mature and
CC       mature stages. {ECO:0000269|PubMed:19495769}.
CC   -!- MISCELLANEOUS: Mannose-binding activity stable when incubated at 85
CC       degrees Celsius for 10 minutes, and increases 3 to 4 fold when
CC       incubated at 85 degrees Celsius for 10 minutes in the presence of 0.14
CC       M 2-mercaptoethanol. Mannose-binding activity decreases to 27% when
CC       incubated at 85 degrees Celsius for 10 minutes in the presence of 0.35
CC       M iodoacetate. Antifungal and hemagglutinating activity stable when
CC       incubated at 100 degrees Celsius for 5 minutes. Antifungal and
CC       hemagglutinating activity increase when incubated at 100 degrees
CC       Celsius for 5 minutes in the presence of 0.14 M 2-mercaptoethanol.
CC       {ECO:0000269|PubMed:18776994}.
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DR   EMBL; EF577046; ABU62812.1; -; mRNA.
DR   AlphaFoldDB; B2KNH9; -.
DR   SMR; B2KNH9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IDA: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:0034120; P:positive regulation of erythrocyte aggregation; IDA:UniProtKB.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Hemagglutinin; Lectin; Mannose-binding; Plant defense; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:19495769"
FT   CHAIN           25..167
FT                   /note="Mannose-specific lectin"
FT                   /id="PRO_0000395875"
FT   DOMAIN          25..138
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000250|UniProtKB:P30617,
FT                   ECO:0000255|PROSITE-ProRule:PRU00038"
SQ   SEQUENCE   167 AA;  18738 MW;  AF8F5FB49B01F525 CRC64;
     MAFSISSTMI FLLSLALFST LVSADNHLLP GERLNPGNFL KQDRYMLIMQ EDCNLVLYNL
     NKPEWATKTA NQGSRCFVTL QSDGNFVIYD EHEQEGRNEA IWASKTDGEN GNYVIILQKD
     GNLVLYSKPI FATGTNRFGS TAVVVAKRNR KAHFGVEQNI IEVTTNL