LECG1_BUNMU
ID LECG1_BUNMU Reviewed; 158 AA.
AC Q90WI6; A1XXJ8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=C-type lectin BML-1;
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].
RC TISSUE=Venom gland;
RX PubMed=11600152; DOI=10.1016/s0041-0101(01)00172-6;
RA Zha H.-G., Lee W.-H., Zhang Y.;
RT "Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus
RT fasciatus and Bungarus multicinctus.";
RL Toxicon 39:1887-1892(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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-1 is able to agglutinate
CC erythrocytes. May be a calcium-dependent lectin.
CC {ECO:0000269|PubMed:17561224}.
CC -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000305}.
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; AF354272; AAK43586.1; -; mRNA.
DR EMBL; DQ787089; ABH05180.1; -; mRNA.
DR AlphaFoldDB; Q90WI6; -.
DR SMR; Q90WI6; -.
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 2: Evidence at transcript 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-1"
FT /id="PRO_0000355260"
FT DOMAIN 33..155
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 119..121
FT /note="Galactose-binding"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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 134
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"
FT CONFLICT 148
FT /note="A -> D (in Ref. 2; ABH05180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18706 MW; 66B71A29D1048805 CRC64;
MGHFTFTGLC LLAMFLSLRG AECYTCPIDW LPKNGLCYKV FSKHKTWFDA EKYCRKFKPG
CHLASLHSNA DAVEFSEYIS DYLTGRGHVW IGLRDTKKKY IWEWTDRSRT DFLPWRKNQP
DHFNNNEFCV EIVNFTGYLQ WNDDNCAALR PFLCQCKY
