ID   LECM2_BUNMU             Reviewed;         158 AA.
AC   A1XXJ9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=C-type lectin BML-2;
DE            Short=CTL;
DE   Flags: Precursor;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17561224; DOI=10.1016/j.toxicon.2007.04.019;
RA   Lin L.-P., Lin Q., Wang Y.-Q.;
RT   "Cloning, expression and characterization of two C-type lectins from the
RT   venom gland of Bungarus multicinctus.";
RL   Toxicon 50:411-419(2007).
CC   -!- FUNCTION: Recombinant C-type lectin BML-2 is able to agglutinate
CC       erythrocytes. May be a calcium-dependent lectin.
CC       {ECO:0000269|PubMed:17561224}.
CC   -!- SUBUNIT: Dimer. Probably non-covalently linked.
CC       {ECO:0000269|PubMed:17561224}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   EMBL; DQ787090; ABH05181.1; -; mRNA.
DR   AlphaFoldDB; A1XXJ9; -.
DR   SMR; A1XXJ9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Glycoprotein; Hemagglutinin; Lectin;
KW   Metal-binding; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..158
FT                   /note="C-type lectin BML-2"
FT                   /id="PRO_0000355261"
FT   DOMAIN          33..155
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           119..121
FT                   /note="Mannose-binding"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        54..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        61..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        129..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   158 AA;  18269 MW;  02FAD38C0E916EF4 CRC64;
     MGHFTFTGLC LLAMFLSLRG AECYTCPIDW LPKNGLCYKV FSNPNTWLDA ELFCRKFKPG
     CRLASLHRDA DSADLAEYIS DYLKVDGSVW IGLNDPQKKR TWVWSDRSSS NYFSWNQGEP
     NNSKNKEYCV HLWAPTGYLK WNDAPCESLH PFLCQCKY