LECG_CROAT
ID LECG_CROAT Reviewed; 135 AA.
AC P21963;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=C-type lectin Cal;
DE Short=CTL;
DE AltName: Full=Galactose-specific lectin {ECO:0000303|PubMed:15049685};
DE AltName: Full=Rattlesnake lectin {ECO:0000303|PubMed:15049685};
DE Short=RSL {ECO:0000303|PubMed:15049685};
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1989986; DOI=10.1016/s0021-9258(18)52246-8;
RA Hirabayashi J., Kusunoki T., Kasai K.;
RT "Complete primary structure of a galactose-specific lectin from the venom
RT of the rattlesnake Crotalus atrox. Homologies with Ca2(+)-dependent-type
RT lectins.";
RL J. Biol. Chem. 266:2320-2326(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-22; 34-61; 62-71; 76-84 AND 104-126, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH LACTOSE AND
RP 2-THIODIGALACTOSIDE, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=15049685; DOI=10.1021/bi035871a;
RA Walker J.R., Nagar B., Young N.M., Hirama T., Rini J.M.;
RT "X-ray crystal structure of a galactose-specific C-type lectin possessing a
RT novel decameric quaternary structure.";
RL Biochemistry 43:3783-3792(2004).
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. Calcium-
CC dependent lectin. Shows high hemagglutinating activity (MHC=10 ng/ml)
CC (PubMed:1989986). {ECO:0000269|PubMed:1989986}.
CC -!- SUBUNIT: Homodecamer of disulfide-linked dimers arranged in two pseudo-
CC 5-fold symmetric pentamers. {ECO:0000269|PubMed:15049685}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1989986}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1989986}.
CC -!- MASS SPECTROMETRY: Mass=16284; Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR PIR; A38609; A38609.
DR PDB; 1JZN; X-ray; 2.20 A; A/B/C/D/E=1-135.
DR PDB; 1MUQ; X-ray; 2.30 A; A/B/C/D/E=1-135.
DR PDBsum; 1JZN; -.
DR PDBsum; 1MUQ; -.
DR AlphaFoldDB; P21963; -.
DR SMR; P21963; -.
DR UniLectin; P21963; -.
DR EvolutionaryTrace; P21963; -.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hemagglutinin; Lectin; Metal-binding; Secreted.
FT CHAIN 1..135
FT /note="C-type lectin Cal"
FT /id="PRO_0000046644"
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 /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT DISULFID 3..14
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT DISULFID 31..131
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT DISULFID 38..133
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT DISULFID 86
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT DISULFID 106..123
FT /evidence="ECO:0000269|PubMed:15049685,
FT ECO:0007744|PDB:1JZN, ECO:0007744|PDB:1MUQ"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:1JZN"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1JZN"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1JZN"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1JZN"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1JZN"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1JZN"
SQ SEQUENCE 135 AA; 16291 MW; 04BAC45DB2B721C8 CRC64;
NNCPLDWLPM NGLCYKIFNQ LKTWEDAEMF CRKYKPGCHL ASFHRYGESL EIAEYISDYH
KGQENVWIGL RDKKKDFSWE WTDRSCTDYL TWDKNQPDHY QNKEFCVELV SLTGYRLWND
QVCESKDAFL CQCKF
