ID   LECG_THANI              Reviewed;         159 AA.
AC   Q66S03;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Galactose-specific lectin nattectin;
DE            Short=CTL;
DE   Flags: Precursor;
OS   Thalassophryne nattereri (Copper Joe toadfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Batrachoidaria; Batrachoididae; Thalassophryne.
OX   NCBI_TaxID=289382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-41, FUNCTION, BIOASSAY,
RP   SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21396978; DOI=10.1016/j.biochi.2011.03.001;
RA   Lopes-Ferreira M., Magalhaes G.S., Fernandez J.H.,
RA   Junqueira-de-Azevedo Ide L., Le Ho P., Lima C., Valente R.H.,
RA   Moura-da-Silva A.M.;
RT   "Structural and biological characterization of nattectin, a new C-type
RT   lectin from the venomous fish Thalassophryne nattereri.";
RL   Biochimie 93:971-980(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Magalhaes G.S., Lopes-Ferreira M., Junqueira-de-Azevedo I.L.M., Ho P.L.,
RA   Moura-da-Silva A.M.;
RT   "A survey of gene expression and diversity in the venom gland of
RT   Thalassophryne nattereri through the generation of expressed sequence tags
RT   (ESTs).";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Galactose specific lectin that exhibits hemagglutination
CC       activity (minimum hemagluttination concentration = 2.5 ug/well) in a
CC       calcium-independent fashion. Has remarkable pro-inflammatory activity,
CC       inducing neutrophil mobilization in mice. Plays a crucial role in the
CC       innate immune system and chronic manifestations, especially in
CC       neutrophil mobilization. {ECO:0000269|PubMed:21396978}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21396978}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- INDUCTION: Hemagglutination is completely inhibited by galactose. Is
CC       not inhibited by mannose, and the chelating agent EDTA.
CC       {ECO:0000269|PubMed:21396978}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:21396978}.
CC   -!- MASS SPECTROMETRY: Mass=15087; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21396978};
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   EMBL; AY707913; AAU11827.1; -; mRNA.
DR   AlphaFoldDB; Q66S03; -.
DR   SMR; Q66S03; -.
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   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; 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; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hemagglutinin; Inflammatory response; Lectin;
KW   Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..24
FT                   /id="PRO_0000017566"
FT   CHAIN           27..159
FT                   /note="Galactose-specific lectin nattectin"
FT                   /id="PRO_0000017567"
FT   DOMAIN          38..156
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           122..124
FT                   /note="Galactose-binding"
FT   BINDING         122
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
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   DISULFID        31..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        59..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        132..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   159 AA;  17868 MW;  8CC369EC195A2FAA CRC64;
     MASVPHFTVF LFLACALGIG ANVTRRATSS CPKGWTHHGS RCFTFHRGSM DWASAEAACI
     RKGGNLASIH NRREQNFITH LIHKLSGENR RTWIGGNDAV KEGMWFWSDG SKFNYKGWKK
     GQPDKHVPAE HCAETNFKGA FWNNALCKVK RSFLCAKNL