ID   LECG_AGKPI              Reviewed;         135 AA.
AC   P0DM36;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=C-type lectin APL;
DE            Short=CTL;
OS   Agkistrodon piscivorus piscivorus (Eastern cottonmouth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8716;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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: Beta-galactoside lectin that agglutinates rabbit and human
CC       erythrocytes in a calcium-dependent fashion (MHC is 0.21 ug/ml on
CC       rabbit erythrocytes). Galactose (15 mM), lactose (20 mM), rhamnose (20
CC       mM) and EGTA strongly inhibit this activity.
CC       {ECO:0000269|PubMed:10484740}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10484740}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484740}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:10484740}.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DM36; -.
DR   SMR; P0DM36; -.
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; Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW   Metal-binding; Secreted.
FT   CHAIN           1..135
FT                   /note="C-type lectin APL"
FT                   /id="PRO_0000422555"
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;  16205 MW;  540929202347B197 CRC64;
     NNCPHDWLPM NGLCYKIFDE LKAWEDAERF CRKYKPGCHL ASFHTYGESL EIAEYISDYH
     KGQAEVWIGL WDKKKDFSWE WTDRSCTDYL TWDKNQPDVY QNKEFCVELV SLTGYRLWND
     QVCESKNAFL CQCKF