ID   LECG_BITAR              Reviewed;         135 AA.
AC   Q9PSN0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=C-type lectin PAL;
DE            Short=CTL;
DE   AltName: Full=BaL;
DE   AltName: Full=Galactose-specific lectin;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8593494; DOI=10.1248/bpb.18.1620;
RA   Nikai T., Suzuki J., Komori Y., Ohkura M., Ohizumi Y., Sugihara H.;
RT   "Primary structure of the lectin from the venom of Bitis arietans (puff-
RT   adder).";
RL   Biol. Pharm. Bull. 18:1620-1622(1995).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=10484740; DOI=10.1016/s0041-0101(98)00239-6;
RA   Komori Y., Nikai T., Tohkai T., Sugihara H.;
RT   "Primary structure and biological activity of snake venom lectin (APL) from
RT   Agkistrodon p. piscivorus (Eastern cottonmouth).";
RL   Toxicon 37:1053-1064(1999).
CC   -!- FUNCTION: Galactose-binding lectin which recognizes specific
CC       carbohydrate structures and agglutinates a variety of animal cells by
CC       binding to cell-surface glycoproteins and glycolipids. This is a
CC       calcium-dependent lectin (PubMed:8593494). Shows high hemagglutinating
CC       activity (MHC is 0.25 ug/ml on rabbit erythrocytes) (PubMed:10484740).
CC       {ECO:0000269|PubMed:10484740, ECO:0000269|PubMed:8593494}.
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; Q9PSN0; -.
DR   SMR; Q9PSN0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR   GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR   GO; GO:0030395; F:lactose binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033296; F:rhamnose binding; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0140548; P:envenomation resulting in blood agglutination in another organism; IDA:UniProtKB.
DR   GO; GO:0035738; P:envenomation resulting in modulation of process in another organism; 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 PAL"
FT                   /id="PRO_0000046642"
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;  16158 MW;  3A01248FA884C5B2 CRC64;
     NNCPPDWLPM NGLCYKIFDE LKAWEDAERF CRKYKPGCHL ASFHQYGESL EIAEYISDYH
     KGQAEVWIGL WDKKKDFSWE WTDRSCTDYL TWDKNQPDHY QNKEFCVELV SLTGYRLWND
     QVCGSKNAFL CQCKF