ID   LECG_LACST              Reviewed;         135 AA.
AC   Q9PSM4;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=C-type lectin LmsL;
DE            Short=CTL;
DE   AltName: Full=Galactose-specific lectin;
DE   AltName: Full=Mutina;
OS   Lachesis stenophrys (Central American bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=88085 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=8843577; DOI=10.1016/0041-0101(96)00011-6;
RA   Aragon-Ortiz F., Mentele R., Auerswald E.A.;
RT   "Amino acid sequence of a lectin-like protein from Lachesis muta stenophyrs
RT   venom.";
RL   Toxicon 34:763-769(1996).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-40, FUNCTION, AND INDUCTION.
RC   TISSUE=Venom;
RA   Aragon-Ortiz F., Brenes-Brenes J.R., Gubensek F.;
RT   "Characterization and properties of a lectin-like protein from Lachesis
RT   muta snake venom.";
RL   Toxicon 28:143-143(1990).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=3671807;
RA   Gomez Leiva M.A., Aragon-Ortiz F.;
RT   "Purification and some properties of hemagglutinating protein mutina from
RT   bushmaster Lachesis muta snake venom.";
RL   Rev. Biol. Trop. 34:49-53(1986).
CC   -!- FUNCTION: Galactose-binding protein which recognizes specific
CC       carbohydrate structures and agglutinates a variety of animal cells by
CC       binding to cell-surface glycoproteins and glycolipids. Is a calcium-
CC       dependent lectin. Shows high hemagglutinating activity, that is
CC       inhibited by lactose, galactose and inositol.
CC       {ECO:0000269|PubMed:3671807, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P21963}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   AlphaFoldDB; Q9PSM4; -.
DR   SMR; Q9PSM4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
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; Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW   Metal-binding; Secreted.
FT   CHAIN           1..135
FT                   /note="C-type lectin LmsL"
FT                   /id="PRO_0000046645"
FT   DOMAIN          10..132
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           96..98
FT                   /note="Galactose-binding"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        31..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        38..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        106..123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   135 AA;  16223 MW;  D5E9083A065A8F56 CRC64;
     NNCPQDWLPM NGLCYKIFDE QKAWEDAEMF CRKYKPGCHL ASFHRYGESL EIAEYISDYH
     KGQAEVWIGL WDKKKDFSWE WTDRSCTDYL TWDKNQPDHY EGKEFCVELV SLTGYRLWND
     QVCESKNAFL CQCKF